Carbonic anhydrase II

"CA II" redirects here. For the spectral features of calcium, see Calcium § H_and_K_lines.

PDB rendering based on 12ca^[1].

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes

12CA, 1A42, 1AM6, 1AVN, 1BCD, 1BIC, 1BN1, 1BN3, 1BN4, 1BNM, 1BNN, 1BNQ, 1BNT, 1BNU, 1BNV, 1BNW, 1BV3, 1CA2, 1CA3, 1CAH, 1CAI, 1CAJ, 1CAK, 1CAL, 1CAM, 1CAN, 1CAO, 1CAY, 1CAZ, 1CCS, 1CCT, 1CCU, 1CIL, 1CIM, 1CIN, 1CNB, 1CNC, 1CNG, 1CNH, 1CNI, 1CNJ, 1CNK, 1CNW, 1CNX, 1CNY, 1CRA, 1CVA, 1CVB, 1CVC, 1CVD, 1CVE, 1CVF, 1CVH, 1DCA, 1DCB, 1EOU, 1F2W, 1FQL, 1FQM, 1FQN, 1FQR, 1FR4, 1FR7, 1FSN, 1FSQ, 1FSR, 1G0E, 1G0F, 1G1D, 1G3Z, 1G45, 1G46, 1G48, 1G4J, 1G4O, 1G52, 1G53, 1G54, 1H4N, 1H9N, 1H9Q, 1HCA, 1HEA, 1HEB, 1HEC, 1HED, 1HVA, 1I8Z, 1I90, 1I91, 1I9L, 1I9M, 1I9N, 1I9O, 1I9P, 1I9Q, 1IF4, 1IF5, 1IF6, 1IF7, 1IF8, 1IF9, 1KWQ, 1KWR, 1LG5, 1LG6, 1LGD, 1LUG, 1LZV, 1MOO, 1MUA, 1OKL, 1OKM, 1OKN, 1OQ5, 1RAY, 1RAZ, 1RZA, 1RZB, 1RZC, 1RZD, 1RZE, 1T9N, 1TB0, 1TBT, 1TE3, 1TEQ, 1TEU, 1TG3, 1TG9, 1TH9, 1THK, 1TTM, 1UGA, 1UGB, 1UGC, 1UGD, 1UGE, 1UGF, 1UGG, 1XEG, 1XEV, 1XPZ, 1XQ0, 1YDA, 1YDB, 1YDC, 1YDD, 1YO0, 1YO1, 1YO2, 1Z9Y, 1ZE8, 1ZFK, 1ZFQ, 1ZGE, 1ZGF, 1ZH9, 1ZSA, 1ZSB, 1ZSC, 2ABE, 2AW1, 2AX2, 2CA2, 2CBA, 2CBB, 2CBC, 2CBD, 2CBE, 2EU2, 2EU3, 2EZ7, 2F14, 2FMG, 2FMZ, 2FNK, 2FNM, 2FNN, 2FOQ, 2FOS, 2FOU, 2FOV, 2GD8, 2GEH, 2H15, 2H4N, 2HD6, 2HKK, 2HL4, 2HNC, 2HOC, 2ILI, 2NNG, 2NNO, 2NNS, 2NNV, 2NWO, 2NWP, 2NWY, 2NWZ, 2NXR, 2NXS, 2NXT, 2O4Z, 2OSF, 2OSM, 2POU, 2POV, 2POW, 2Q1B, 2Q1Q, 2Q38, 2QO8, 2QOA, 2QP6, 2VVA, 2VVB, 2WD2, 2WD3, 2WEG, 2WEH, 2WEJ, 2WEO, 2X7S, 2X7T, 2X7U, 3B4F, 3BET, 3BL0, 3BL1, 3C7P, 3CA2, 3CAJ, 3CYU, 3D8W, 3D92, 3D93, 3D9Z, 3DAZ, 3DBU, 3DC3, 3DC9, 3DCC, 3DCS, 3DCW, 3DD0, 3DD8, 3DV7, 3DVB, 3DVC, 3DVD, 3EFI, 3EFT, 3F4X, 3F8E, 3FFP, 3GZ0, 3HFP, 3HKN, 3HKQ, 3HKT, 3HKU, 3HLJ, 3HS4, 3IBI, 3IBL, 3IBN, 3IBU, 3IEO, 3IGP, 3K2F, 3K34, 3K7K, 3KIG, 3KKX, 3KNE, 3KOI, 3KOK, 3KON, 3KS3, 3KWA, 3L14, 3M04, 3M14, 3M1J, 3M1K, 3M1Q, 3M1W, 3M2N, 3M2X, 3M2Y, 3M2Z, 3M3X, 3M40, 3M5E, 3M5S, 3M5T, 3M67, 3M96, 3M98, 3MHC, 3MHI, 3MHL, 3MHM, 3MHO, 3ML2, 3MMF, 3MNA, 3MNH, 3MNI, 3MNJ, 3MNK, 3MNU, 3MWO, 3MYQ, 3MZC, 3N0N, 3N2P, 3N3J, 3N4B, 3NB5, 3NI5, 3NJ9, 3OIK, 3OIL, 3OIM, 3OKU, 3OKV, 3OY0, 3OYQ, 3OYS, 3P3H, 3P3J, 3P44, 3P4V, 3P55, 3P58, 3P5A, 3P5L, 3PJJ, 3PO6, 3PYK, 3QYK, 3R16, 3R17, 3RG3, 3RG4, 3RGE, 3RJ7, 3RLD, 3RYJ, 3RYV, 3RYX, 3RYY, 3RYZ, 3RZ0, 3RZ1, 3RZ5, 3RZ7, 3RZ8, 3S71, 3S72, 3S73, 3S74, 3S75, 3S76, 3S77, 3S78, 3S8X, 3S9T, 3SAP, 3SAX, 3SBH, 3SBI, 3T5U, 3T5Z, 3T82, 3T83, 3T84, 3T85, 3TMJ, 3TVN, 3TVO, 3U3A, 3U45, 3U47, 3U7C, 3V2J, 3V2M, 3V3F, 3V3G, 3V3H, 3V3I, 3V3J, 3V5G, 3V7X, 3VBD, 3ZP9, 4BCW, 4BF1, 4BF6, 4CA2, 4CAC, 4CQ0, 4DZ7, 4DZ9, 4E3D, 4E3F, 4E3G, 4E3H, 4E49, 4E4A, 4E5Q, 4FIK, 4FL7, 4FPT, 4FRC, 4FU5, 4FVN, 4FVO, 4G0C, 4GL1, 4HBA, 4HEW, 4HEY, 4HEZ, 4HF3, 4HT0, 4IDR, 4ILX, 4ITO, 4ITP, 4IWZ, 4JS6, 4JSA, 4JSS, 4JSW, 4JSZ, 4K0S, 4K0T, 4K0Z, 4K13, 4K1Q, 4KAP, 4KNI, 4KNJ, 4KUV, 4KUW, 4KUY, 4KV0, 4L5U, 4L5V, 4L5W, 4LHI, 4LP6, 4M2R, 4M2U, 4M2V, 4M2W, 4MDG, 4MDL, 4MDM, 4MLT, 4MLX, 4MO8, 4MTY, 4N0X, 4N16, 4PQ7, 4PYX, 4PYY, 4PZH, 4Q06, 4Q07, 4Q08, 4Q09, 4Q49, 4Q6D, 4Q6E, 4Q78, 4Q7P, 4Q7S, 4Q7V, 4Q7W, 4Q81, 4Q83, 4Q87, 4Q8X, 4Q8Y, 4Q8Z, 4Q90, 4Q99, 4Q9Y, 4QEF, 4QIY, 4QJM, 4QK1, 4QK2, 4QK3, 4QSA, 4QSB, 4QSI, 4QTL, 4QY3, 4R59, 4R5A, 4R5B, 4RFC, 4RFD, 4RIU, 4RIV, 4RN4, 4RUX, 4RUY, 4RUZ, 4XE1, 4Y0J, 4YGJ, 4YGK, 4YGL, 4YGN, 5AMD, 5AMG, 5AML, 5CA2, 5CAC, 6CA2, 7CA2, 8CA2, 9CA2

Identifiers

Symbols

CA2 ; CA-II; CAC; CAII; Car2; HEL-76

External IDs

OMIM: 611492 MGI: 88269 HomoloGene: 37256 ChEMBL: 205 GeneCards: CA2 Gene

EC number

4.2.1.1

Gene ontology
Molecular function	• arylesterase activity • carbonate dehydratase activity • protein binding • zinc ion binding
Cellular component	• extracellular space • cytoplasm • cytosol • plasma membrane • microvillus • basolateral plasma membrane • axon • myelin sheath • apical part of cell • extracellular exosome
Biological process	• kidney development • morphogenesis of an epithelium • one-carbon metabolic process • response to pH • response to zinc ion • bicarbonate transport • positive regulation of synaptic transmission, GABAergic • positive regulation of cellular pH reduction • angiotensin-activated signaling pathway • odontogenesis of dentin-containing tooth • response to estrogen • regulation of anion transport • small molecule metabolic process • positive regulation of osteoclast differentiation • positive regulation of bone resorption • secretion • regulation of intracellular pH • cellular response to fluid shear stress • positive regulation of dipeptide transmembrane transport • regulation of chloride transport
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

760

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 8:
85.46 – 85.48 Mb

Chr 3:
14.89 – 14.9 Mb

PubMed search

Carbonic anhydrase II (gene name CA2), is one of fourteen forms of human α carbonic anhydrases. Carbonic anhydrase catalyzes reversible hydration of carbon dioxide. Defects in this enzyme are associated with osteopetrosis and renal tubular acidosis. Renal carbonic anhydrase allows the reabsorption of bicarbonate ions in the proximal tubule. ^[2]

Interactions

Carbonic anhydrase II has been shown to interact with Band 3^[3]^[4]^[5]^[6] and Sodium-hydrogen antiporter 1.^[7]

References

↑ Nair, S. K.; Calderone, T. L.; Christianson, D. W.; Fierke, C. A. (1991). "Altering the mouth of a hydrophobic pocket. Structure and kinetics of human carbonic anhydrase II mutants at residue Val-121". The Journal of biological chemistry 266 (26): 17320–17325. PMID 1910042.
↑ "Entrez Gene: CA2 carbonic anhydrase II".
↑ Sterling, D; Reithmeier R A; Casey J R (December 2001). "A transport metabolon. Functional interaction of carbonic anhydrase II and chloride/bicarbonate exchangers". J. Biol. Chem. (United States) 276 (51): 47886–94. doi:10.1074/jbc.M105959200. ISSN 0021-9258. PMID 11606574.
↑ Vince, J W; Reithmeier R A (October 1998). "Carbonic anhydrase II binds to the carboxyl terminus of human band 3, the erythrocyte C1-/HCO3- exchanger". J. Biol. Chem. (UNITED STATES) 273 (43): 28430–7. doi:10.1074/jbc.273.43.28430. ISSN 0021-9258. PMID 9774471.
↑ Vince, J W; Carlsson U; Reithmeier R A (November 2000). "Localization of the Cl-/HCO3- anion exchanger binding site to the amino-terminal region of carbonic anhydrase II". Biochemistry (UNITED STATES) 39 (44): 13344–9. doi:10.1021/bi0015111. ISSN 0006-2960. PMID 11063570.
↑ Vince, J W; Reithmeier R A (May 2000). "Identification of the carbonic anhydrase II binding site in the Cl(-)/HCO(3)(-) anion exchanger AE1". Biochemistry (UNITED STATES) 39 (18): 5527–33. doi:10.1021/bi992564p. ISSN 0006-2960. PMID 10820026.
↑ Li, Xiuju; Alvarez Bernardo; Casey Joseph R; Reithmeier Reinhart A F; Fliegel Larry (September 2002). "Carbonic anhydrase II binds to and enhances activity of the Na+/H+ exchanger". J. Biol. Chem. (United States) 277 (39): 36085–91. doi:10.1074/jbc.M111952200. ISSN 0021-9258. PMID 12138085.

Sly WS, Hu PY (1995). "Human carbonic anhydrases and carbonic anhydrase deficiencies.". Annu. Rev. Biochem. 64 (1): 375–401. doi:10.1146/annurev.bi.64.070195.002111. PMID 7574487.
Kumpulainen T (1979). "Immunohistochemical localization of human carbonic anhydrase isoenzyme C.". Histochemistry 62 (3): 271–80. doi:10.1007/BF00508355. PMID 114507.
Henderson LE, Henriksson D, Nyman PO (1976). "Primary structure of human carbonic anhydrase C.". J. Biol. Chem. 251 (18): 5457–63. PMID 823150.
Hu PY, Roth DE, Skaggs LA; et al. (1993). "A splice junction mutation in intron 2 of the carbonic anhydrase II gene of osteopetrosis patients from Arabic countries.". Hum. Mutat. 1 (4): 288–92. doi:10.1002/humu.1380010404. PMID 1301935.
Roth DE, Venta PJ, Tashian RE, Sly WS (1992). "Molecular basis of human carbonic anhydrase II deficiency.". Proc. Natl. Acad. Sci. U.S.A. 89 (5): 1804–8. doi:10.1073/pnas.89.5.1804. PMC 48541. PMID 1542674.
Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin.". J. Infect. 24 (3): 317–20. doi:10.1016/S0163-4453(05)80037-4. PMID 1602151.
Schwartz GJ, Brion LP, Corey HE, Dorfman HD (1991). "Case report 668. Carbonic anhydrase II deficiency syndrome (osteopetrosis associated with renal tubular acidosis and cerebral calcification).". Skeletal Radiol. 20 (6): 447–52. PMID 1925679.
Venta PJ, Welty RJ, Johnson TM; et al. (1991). "Carbonic anhydrase II deficiency syndrome in a Belgian family is caused by a point mutation at an invariant histidine residue (107 His----Tyr): complete structure of the normal human CA II gene.". Am. J. Hum. Genet. 49 (5): 1082–90. PMC 1683243. PMID 1928091.
Venta PJ, Tashian RE (1990). "PCR detection of the TAQ1 polymorphism at the CA2 locus.". Nucleic Acids Res. 18 (18): 5585. doi:10.1093/nar/18.18.5585. PMC 332284. PMID 1977133.
Sato S, Zhu XL, Sly WS (1990). "Carbonic anhydrase isozymes IV and II in urinary membranes from carbonic anhydrase II-deficient patients.". Proc. Natl. Acad. Sci. U.S.A. 87 (16): 6073–6. doi:10.1073/pnas.87.16.6073. PMC 54474. PMID 2117271.
Kaunisto K, Parkkila S, Tammela T; et al. (1990). "Immunohistochemical localization of carbonic anhydrase isoenzymes in the human male reproductive tract.". Histochemistry 94 (4): 381–6. doi:10.1007/BF00266444. PMID 2121671.
Backman U, Danielsson B, Wistrand PJ (1991). "The excretion of carbonic anhydrase isozymes CA I and CA II in the urine of apparently healthy subjects and in patients with kidney disease.". Scand. J. Clin. Lab. Invest. 50 (6): 627–33. doi:10.3109/00365519009089180. PMID 2123360.
Forsman C, Behravan G, Osterman A, Jonsson BH (1989). "Production of active human carbonic anhydrase II in E. coli.". Acta Chem. Scand. B 42 (5): 314–8. PMID 2850697.
Venta PJ, Montgomery JC, Hewett-Emmett D, Tashian RE (1986). "Comparison of the 5' regions of human and mouse carbonic anhydrase II genes and identification of possible regulatory elements.". Biochim. Biophys. Acta 826 (4): 195–201. doi:10.1016/0167-4781(85)90006-5. PMID 3000449.
Ohlsson A, Cumming WA, Paul A, Sly WS (1986). "Carbonic anhydrase II deficiency syndrome: recessive osteopetrosis with renal tubular acidosis and cerebral calcification.". Pediatrics 77 (3): 371–81. PMID 3081869.
Nakai H, Byers MG, Venta PJ; et al. (1987). "The gene for human carbonic anhydrase II (CA2) is located at chromosome 8q22.". Cytogenet. Cell Genet. 44 (4): 234–5. doi:10.1159/000132378. PMID 3107918.
Montgomery JC, Venta PJ, Tashian RE, Hewett-Emmett D (1987). "Nucleotide sequence of human liver carbonic anhydrase II cDNA.". Nucleic Acids Res. 15 (11): 4687. doi:10.1093/nar/15.11.4687. PMC 340889. PMID 3108857.
Murakami H, Marelich GP, Grubb JH; et al. (1988). "Cloning, expression, and sequence homologies of cDNA for human carbonic anhydrase II.". Genomics 1 (2): 159–66. doi:10.1016/0888-7543(87)90008-5. PMID 3121496.
Eriksson AE, Jones TA, Liljas A (1989). "Refined structure of human carbonic anhydrase II at 2.0 A resolution.". Proteins 4 (4): 274–82. doi:10.1002/prot.340040406. PMID 3151019.
Eriksson AE, Kylsten PM, Jones TA, Liljas A (1989). "Crystallographic studies of inhibitor binding sites in human carbonic anhydrase II: a pentacoordinated binding of the SCN- ion to the zinc at high pH.". Proteins 4 (4): 283–93. doi:10.1002/prot.340040407. PMID 3151020.

PDB gallery

12ca: ALTERING THE MOUTH OF A HYDROPHOBIC POCKET. STRUCTURE AND KINETICS OF HUMAN CARBONIC ANHYDRASE II MUTANTS AT RESIDUE VAL-121

1a42: HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH BRINZOLAMIDE

1am6: CARBONIC ANHYDRASE II INHIBITOR: ACETOHYDROXAMATE

1avn: HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH THE HISTAMINE ACTIVATOR

1bcd: X-RAY CRYSTALLOGRAPHIC STRUCTURE OF A COMPLEX BETWEEN HUMAN CARBONIC ANHYDRASE II AND A NEW TOPICAL INHIBITOR, TRIFLUOROMETHANE SULPHONAMIDE

1bic: CRYSTALLOGRAPHIC ANALYSIS OF THR-200-> HIS HUMAN CARBONIC ANHYDRASE II AND ITS COMPLEX WITH THE SUBSTRATE, HCO3-

1bn1: CARBONIC ANHYDRASE II INHIBITOR

1bn3: CARBONIC ANHYDRASE II INHIBITOR

1bn4: CARBONIC ANHYDRASE II INHIBITOR

1bnm: CARBONIC ANHYDRASE II INHIBITOR

1bnn: CARBONIC ANHYDRASE II INHIBITOR

1bnq: CARBONIC ANHYDRASE II INHIBITOR

1bnt: CARBONIC ANHYDRASE II INHIBITOR

1bnu: CARBONIC ANHYDRASE II INHIBITOR

1bnv: CARBONIC ANHYDRASE II INHIBITOR

1bnw: CARBONIC ANHYDRASE II INHIBITOR

1bv3: HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH UREA

1ca2: REFINED STRUCTURE OF HUMAN CARBONIC ANHYDRASE II AT 2.0 ANGSTROMS RESOLUTION

1ca3: UNEXPECTED PH-DEPENDENT CONFORMATION OF HIS-64, THE PROTON SHUTTLE OF CARBONIC ANHYDRASE II.

1cah: STRUCTURE OF COBALT CARBONIC ANHYDRASE COMPLEXED WITH BICARBONATE

1cai: STRUCTURAL ANALYSIS OF THE ZINC HYDROXIDE-THR 199-GLU 106 HYDROGEN BONDING NETWORK IN HUMAN CARBONIC ANHYDRASE II

1caj: STRUCTURAL ANALYSIS OF THE ZINC HYDROXIDE-THR 199-GLU 106 HYDROGEN BONDING NETWORK IN HUMAN CARBONIC ANHYDRASE II

1cak: STRUCTURAL ANALYSIS OF THE ZINC HYDROXIDE-THR 199-GLU 106 HYDROGEN BONDING NETWORK IN HUMAN CARBONIC ANHYDRASE II

1cal: STRUCTURAL ANALYSIS OF THE ZINC HYDROXIDE-THR 199-GLU 106 HYDROGEN BONDING NETWORK IN HUMAN CARBONIC ANHYDRASE II

1cam: STRUCTURAL ANALYSIS OF THE ZINC HYDROXIDE-THR 199-GLU 106 HYDROGEN BONDING NETWORK IN HUMAN CARBONIC ANHYDRASE II

1can: CRYSTALLOGRAPHIC STUDIES OF THE BINDING OF PROTONATED AND UNPROTONATED INHIBITORS TO CARBONIC ANHYDRASE USING HYDROGEN SULPHIDE AND NITRATE ANIONS

1cao: CRYSTALLOGRAPHIC STUDIES OF THE BINDING OF PROTONATED AND UNPROTONATED INHIBITORS TO CARBONIC ANHYDRASE USING HYDROGEN SULPHIDE AND NITRATE ANIONS

1cay: WILD-TYPE AND E106Q MUTANT CARBONIC ANHYDRASE COMPLEXED WITH ACETATE

1caz: WILD-TYPE AND E106Q MUTANT CARBONIC ANHYDRASE COMPLEXED WITH ACETATE

1ccs: STRUCTURE-ASSISTED REDESIGN OF A PROTEIN-ZINC BINDING SITE WITH FEMTOMOLAR AFFINITY

1cct: STRUCTURE-ASSISTED REDESIGN OF A PROTEIN-ZINC BINDING SITE WITH FEMTOMOLAR AFFINITY

1ccu: STRUCTURE-ASSISTED REDESIGN OF A PROTEIN-ZINC BINDING SITE WITH FEMTOMOLAR AFFINITY

1cil: THE POSITIONS OF HIS-64 AND A BOUND WATER IN HUMAN CARBONIC ANHYDRASE II UPON BINDING THREE STRUCTURALLY RELATED INHIBITORS

1cim: THE POSITIONS OF HIS-64 AND A BOUND WATER IN HUMAN CARBONIC ANHYDRASE II UPON BINDING THREE STRUCTURALLY RELATED INHIBITORS

1cin: THE POSITIONS OF HIS-64 AND A BOUND WATER IN HUMAN CARBONIC ANHYDRASE II UPON BINDING THREE STRUCTURALLY RELATED INHIBITORS

1cnb: COMPENSATORY PLASTIC EFFECTS IN THE REDESIGN OF PROTEIN-ZINC BINDING SITES

1cnc: COMPENSATORY PLASTIC EFFECTS IN THE REDESIGN OF PROTEIN-ZINC BINDING SITES

1cng: X-RAY CRYSTALLOGRAPHIC STUDIES OF ENGINEERED HYDROGEN BOND NETWORKS IN A PROTEIN-ZINC BINDING SITE

1cnh: X-RAY CRYSTALLOGRAPHIC STUDIES OF ENGINEERED HYDROGEN BOND NETWORKS IN A PROTEIN-ZINC BINDING SITE

1cni: X-RAY CRYSTALLOGRAPHIC STUDIES OF ENGINEERED HYDROGEN BOND NETWORKS IN A PROTEIN-ZINC BINDING SITE

1cnj: X-RAY CRYSTALLOGRAPHIC STUDIES OF ENGINEERED HYDROGEN BOND NETWORKS IN A PROTEIN-ZINC BINDING SITE

1cnk: X-RAY CRYSTALLOGRAPHIC STUDIES OF ENGINEERED HYDROGEN BOND NETWORKS IN A PROTEIN-ZINC BINDING SITE

1cnw: SECONDARY INTERACTIONS SIGNIFICANTLY REMOVED FROM THE SULFONAMIDE BINDING POCKET OF CARBONIC ANHYDRASE II INFLUENCE BINDING CONSTANTS

1cnx: SECONDARY INTERACTIONS SIGNIFICANTLY REMOVED FROM THE SULFONAMIDE BINDING POCKET OF CARBONIC ANHYDRASE II INFLUENCE BINDING CONSTANTS

1cny: SECONDARY INTERACTIONS SIGNIFICANTLY REMOVED FROM THE SULFONAMIDE BINDING POCKET OF CARBONIC ANHYDRASE II INFLUENCE BINDING CONSTANTS

1cra: THE COMPLEX BETWEEN HUMAN CARBONIC ANHYDRASE II AND THE AROMATIC INHIBITOR 1,2,4-TRIAZOLE

1cva: STRUCTURAL AND FUNCTIONAL IMPORTANCE OF A CONSERVED HYDROGEN BOND NETWORK IN HUMAN CARBONIC ANHYDRASE II

1cvb: STRUCTURAL AND FUNCTIONAL IMPORTANCE OF A CONSERVED HYDROGEN BOND NETWORK IN HUMAN CARBONIC ANHYDRASE II

1cvc: REDESIGNING THE ZINC BINDING SITE OF HUMAN CARBONIC ANHYDRASE II: STRUCTURE OF A HIS2ASP-ZN2+ METAL COORDINATION POLYHEDRON

1cvd: STRUCTURAL CONSEQUENCES OF REDESIGNING A PROTEIN-ZINC BINDING SITE

1cve: STRUCTURAL CONSEQUENCES OF REDESIGNING A PROTEIN-ZINC BINDING SITE

1cvf: STRUCTURAL CONSEQUENCES OF REDESIGNING A PROTEIN-ZINC BINDING SITE

1cvh: STRUCTURAL CONSEQUENCES OF REDESIGNING A PROTEIN-ZINC BINDING SITE

1dca: STRUCTURE OF AN ENGINEERED METAL BINDING SITE IN HUMAN CARBONIC ANHYDRASE II REVEALS THE ARCHITECTURE OF A REGULATORY CYSTEINE SWITCH

1dcb: STRUCTURE OF AN ENGINEERED METAL BINDING SITE IN HUMAN CARBONIC ANHYDRASE II REVEALS THE ARCHITECTURE OF A REGULATORY CYSTEINE SWITCH

1eou: CRYSTAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH AN ANTICONVULSANT SUGAR SULFAMATE

1f2w: THE MECHANISM OF CYANAMIDE HYDRATION CATALYZED BY CARBONIC ANHYDRASE II REVEALED BY CRYOGENIC X-RAY DIFFRACTION

1fql: X-RAY CRYSTAL STRUCTURE OF ZINC-BOUND F95M/W97V CARBONIC ANHYDRASE (CAII) VARIANT

1fqm: X-RAY CRYSTAL STRUCTURE OF ZINC-BOUND F93I/F95M/W97V CARBONIC ANHYDRASE (CAII) VARIANT

1fqn: X-RAY CRYSTAL STRUCTURE OF METAL-FREE F93I/F95M/W97V CARBONIC ANHYDRASE (CAII) VARIANT

1fqr: X-RAY CRYSTAL STRUCTURE OF COBALT-BOUND F93I/F95M/W97V CARBONIC ANHYDRASE (CAII) VARIANT

1fr4: X-RAY CRYSTAL STRUCTURE OF COPPER-BOUND F93I/F95M/W97V CARBONIC ANHYDRASE (CAII) VARIANT

1fr7: X-RAY CRYSTAL STRUCTURE OF ZINC-BOUND F93S/F95L/W97M CARBONIC ANHYDRASE (CAII) VARIANT

1fsn: X-RAY CRYSTAL STRUCTURE OF METAL-FREE F93S/F95L/W97M CARBONIC ANHYDRASE (CAII) VARIANT

1fsq: X-RAY CRYSTAL STRUCTURE OF COBALT-BOUND F93S/F95L/W97M CARBONIC ANHYDRASE (CAII) VARIANT

1fsr: X-RAY CRYSTAL STRUCTURE OF COPPER-BOUND F93S/F95L/W97M CARBONIC ANHYDRASE (CAII) VARIANT

1g0e: SITE-SPECIFIC MUTANT (HIS64 REPLACED WITH ALA) OF HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH 4-METHYLIMIDAZOLE

1g0f: SITE-SPECIFIC MUTANT (HIS64 REPLACED WITH ALA) OF HUMAN CARBONIC ANHYDRASE II

1g1d: CARBONIC ANHYDRASE II COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(2-FLUOROPHENYL)METHYL]-BENZAMIDE

1g3z: CARBONIC ANHYDRASE II (F131V)

1g45: CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(2-FLUOROPHENYL)METHYL]-BENZAMIDE

1g46: CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(2,3-DIFLUOROPHENYL)METHYL]-BENZAMIDE

1g48: CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(2,6-DIFLUOROPHENYL)METHYL]-BENZAMIDE

1g4j: CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(2,3,4,5,6-PENTAFLUOROPHENYL)METHYL]-BENZAMIDE

1g4o: CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N-PHENYLMETHYLBENZAMIDE

1g52: CARBONIC ANHYDRASE II COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(2,3-DIFLUOROPHENYL)METHYL]-BENZAMIDE

1g53: CARBONIC ANHYDRASE II COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(2,6-DIFLUOROPHENYL)METHYL]-BENZAMIDE

1g54: CARBONIC ANHYDRASE II COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(2,3,4,5,6-PENTAFLUOROPHENYL)METHYL]-BENZAMIDE

1g6v: Complex of the camelid heavy-chain antibody fragment CAB-CA05 with bovine carbonic anhydrase

1h4n: H94N CARBONIC ANHYDRASE II COMPLEXED WITH TRIS

1h9n: H119N CARBONIC ANHYDRASE II

1h9q: H119Q CARBONIC ANHYDRASE II

1hca: UNEXPECTED PH-DEPENDENT CONFORMATION OF HIS-64, THE PROTON SHUTTLE OF CARBONIC ANHYDRASE II.

1hea: CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) (HCA II) (E.C.4.2.1.1) MUTANT WITH LEU 198 REPLACED BY ARG (L198R)

1heb: STRUCTURAL CONSEQUENCES OF HYDROPHILIC AMINO-ACID SUBSTITUTIONS IN THE HYDROPHOBIC POCKET OF HUMAN CARBONIC ANHYDRASE II

1hec: STRUCTURAL CONSEQUENCES OF HYDROPHILIC AMINO-ACID SUBSTITUTIONS IN THE HYDROPHOBIC POCKET OF HUMAN CARBONIC ANHYDRASE II

1hed: STRUCTURAL CONSEQUENCES OF HYDROPHILIC AMINO-ACID SUBSTITUTIONS IN THE HYDROPHOBIC POCKET OF HUMAN CARBONIC ANHYDRASE II

1hva: ENGINEERING THE ZINC BINDING SITE OF HUMAN CARBONIC ANHYDRASE II: STRUCTURE OF THE HIS-94-> CYS APOENZYME IN A NEW CRYSTALLINE FORM

1i8z: CARBONIC ANHYDRASE II COMPLEXED WITH AL-6629 2H-THIENO[3,2-E]-1,2-THIAZINE-6-SULFONAMIDE, 2-(3-METHOXYPHENYL)-3-(4-MORPHOLINYL)-, 1,1-DIOXIDE

1i90: CARBONIC ANHYDRASE II COMPLEXED WITH AL-8520 2H-THIENO[3,2-E]-1,2-THIAZINE-6-SULFONAMIDE, 4-AMINO-3,4-DIHYDRO-2-(3-METHOXYPROPYL)-, 1,1-DIOXIDE, (R)

1i91: CARBONIC ANHYDRASE II COMPLEXED WITH AL-6619 2H-THIENO[3,2-E]-1,2-THIAZINE-6-SULFONAMIDE, 2-(3-HYDROXYPHENYL)-3-(4-MORPHOLINYL)-, 1,1-DIOXIDE

1i9l: CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(4-FLUOROPHENYL)METHYL]-BENZAMIDE

1i9m: CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(2,4-DIFLUOROPHENYL)METHYL]-BENZAMIDE

1i9n: CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(2,5-DIFLUOROPHENYL)METHYL]-BENZAMIDE

1i9o: CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(2,3,4-TRIFLUOROPHENYL)METHYL]-BENZAMIDE

1i9p: CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(2,4,6-TRIFLUOROPHENYL)METHYL]-BENZAMIDE

1i9q: CARBONIC ANHYDRASE II (F131V) COMPLEXED WITH 4-(AMINOSULFONYL)-N-[(3,4,5-TRIFLUOROPHENYL)METHYL]-BENZAMIDE

1if4: Carbonic Anhydrase II Complexed With 4-fluorobenzenesulfonamide

1if5: Carbonic Anhydrase II Complexed With 2,6-difluorobenzenesulfonamide

1if6: Carbonic Anhydrase II Complexed With 3,5-difluorobenzenesulfonamide

1if7: Carbonic Anhydrase II Complexed With (R)-N-(3-Indol-1-yl-2-methyl-propyl)-4-sulfamoyl-benzamide

1if8: Carbonic Anhydrase II Complexed With (S)-N-(3-Indol-1-yl-2-methyl-propyl)-4-sulfamoyl-benzamide

1if9: Carbonic Anhydrase II Complexed With N-[2-(1H-Indol-5-yl)-butyl]-4-sulfamoyl-benzamide

1kwq: HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH INHIBITOR 2000-07

1kwr: HUMAN CARBONIC ANHYDRASE II COMPLEXED WITH INHIBITOR 0134-36

1lg5: Crystal Structure Analysis of the HCA II Mutant T199P in complex with beta-mercaptoethanol

1lg6: Crystal Structure Analysis of HCA II Mutant T199P in Complex with Thiocyanate

1lgd: Crystal Structure Analysis of HCA II Mutant T199P in Complex with Bicarbonate

1lug: Full Matrix Error Analysis of Carbonic Anhydrase

1lzv: Site-Specific Mutant (Tyr7 replaced with His) of Human Carbonic Anhydrase II

1moo: Site Specific Mutant (H64A) of Human Carbonic Anhydrase II at high resolution

1mua: STRUCTURE AND ENERGETICS OF A NON-PROLINE CIS-PEPTIDYL LINKAGE IN AN ENGINEERED PROTEIN

1okl: CARBONIC ANHYDRASE II COMPLEX WITH THE 1OKL INHIBITOR 5-DIMETHYLAMINO-NAPHTHALENE-1-SULFONAMIDE

1okm: CARBONIC ANHYDRASE II COMPLEX WITH THE 1OKM INHIBITOR 4-SULFONAMIDE-[1-(4-AMINOBUTANE)]BENZAMIDE

]

1okn: CARBONIC ANHYDRASE II COMPLEX WITH THE 1OKN INHIBITOR 4-SULFONAMIDE-[1-(4-N-(5-FLUORESCEIN THIOUREA)BUTANE)]

1oq5: CARBONIC ANHYDRASE II IN COMPLEX WITH NANOMOLAR INHIBITOR

1ray: THE STRUCTURE OF HUMAN CARBONIC ANHYDRASE II IN COMPLEX WITH BROMIDE AND AZIDE

1raz: THE STRUCTURE OF HUMAN CARBONIC ANHYDRASE II IN COMPLEX WITH BROMIDE AND AZIDE

1rza: X-RAY ANALYSIS OF METAL SUBSTITUTED HUMAN CARBONIC ANHYDRASE II DERIVATIVES

1rzb: X-RAY ANALYSIS OF METAL SUBSTITUTED HUMAN CARBONIC ANHYDRASE II DERIVATIVES

1rzc: X-RAY ANALYSIS OF METAL SUBSTITUTED HUMAN CARBONIC ANHYDRASE II DERIVATIVES

1rzd: X-RAY ANALYSIS OF METAL SUBSTITUTED HUMAN CARBONIC ANHYDRASE II DERIVATIVES

1rze: X-RAY ANALYSIS OF METAL SUBSTITUTED HUMAN CARBONIC ANHYDRASE II DERIVATIVES

1t9n: Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II

1tb0: Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II

1tbt: Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II

1te3: Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II

1teq: Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II

1teu: Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II

1tg3: Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II

1tg9: Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II

1th9: Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II

1thk: Effect of Shuttle Location and pH Environment on H+ Transfer in Human Carbonic Anhydrase II

1ttm: Human carbonic anhydrase II complexed with 667-coumate

1uga: HUMAN CARBONIC ANHYDRASE II[HCAII] (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY PHE (A65F)

1ugb: HUMAN CARBONIC ANHYDRASE II[HCAII] (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY GLY (A65G)

1ugc: HUMAN CARBONIC ANHYDRASE II [HCAII] (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY HIS (A65H)

1ugd: HUMAN CARBONIC ANHYDRASE II[HCAII] (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY SER (A65S)

1uge: HUMAN CARBONIC ANHYDRASE II [HCAII] (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY LEU (A65L)

1ugf: HUMAN CARBONIC ANHYDRASE II [HCAII] (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY THR (A65T)

1ugg: HUMAN CARBONIC ANHYDRASE II[HCAII] (E.C.4.2.1.1) MUTANT WITH ALA 65 REPLACED BY SER (A65S)-ORTHORHOMBIC FORM

1xeg: Crystal structure of human carbonic anhydrase II complexed with an acetate ion

1xev: Crystal structure of human carbonic anhydrase II in a new crystal form

1xpz: Structure of human carbonic anhydrase II with 4-[4-O-sulfamoylbenzyl)(4-cyanophenyl)amino]-4H-[1,2,4]-triazole

1xq0: Structure of human carbonic anhydrase II with 4-[(3-bromo-4-O-sulfamoylbenzyl)(4-cyanophenyl)amino]-4H-[1,2,4]-triazole

1yda: STRUCTURAL BASIS OF INHIBITOR AFFINITY TO VARIANTS OF HUMAN CARBONIC ANHYDRASE II

1ydb: STRUCTURAL BASIS OF INHIBITOR AFFINITY TO VARIANTS OF HUMAN CARBONIC ANHYDRASE II

1ydc: STRUCTURAL BASIS OF INHIBITOR AFFINITY TO VARIANTS OF HUMAN CARBONIC ANHYDRASE II

1ydd: STRUCTURAL BASIS OF INHIBITOR AFFINITY TO VARIANTS OF HUMAN CARBONIC ANHYDRASE II

1yo0: Proton Transfer from His200 in Human Carbonic Anhydrase II

1yo1: Proton Transfer from His200 in Human Carbonic Anhydrase II

1yo2: Proton Transfer from His200 in Human Carbonic Anhydrase II

1z9y: carbonic anhydrase II in complex with furosemide as sulfonamide inhibitor

1ze8: Carbonic anhydrase II in complex with a membrane-impermeant sulfonamide inhibitor

1zfk: carbonic anhydrase II in complex with N-4-sulfonamidphenyl-N'-4-methylbenzosulfonylurease as sulfonamide inhibitor

1zfq: carbonic anhydrase II in complex with ethoxzolamidphenole as sulfonamide inhibitor

1zge: carbonic anhydrase II in complex with p-Sulfonamido-o,o'-dichloroaniline as sulfonamide inhibitor

1zgf: carbonic anhydrase II in complex with trichloromethiazide as sulfonamide inhibitor

1zh9: carbonic anhydrase II in complex with N-4-Methyl-1-piperazinyl-N'-(p-sulfonamide)phenylthiourea as sulfonamide inhibitor

1zsa: CARBONIC ANHYDRASE II MUTANT E117Q, APO FORM

1zsb: CARBONIC ANHYDRASE II MUTANT E117Q, TRANSITION STATE ANALOGUE ACETAZOLAMIDE

1zsc: CARBONIC ANHYDRASE II MUTANT E117Q, HOLO FORM

2abe: Carbonic anhydrase activators: X-ray crystal structure of the adduct of human isozyme II with L-histidine as a platform for the design of stronger activators

2aw1: Carbonic anhydrase inhibitors: Valdecoxib binds to a different active site region of the human isoform II as compared to the structurally related cyclooxygenase II ""selective"" inhibitor Celecoxib

2ax2: Production and X-ray crystallographic analysis of fully deuterated human carbonic anhydrase II

2ca2: CRYSTALLOGRAPHIC STUDIES OF INHIBITOR BINDING SITES IN HUMAN CARBONIC ANHYDRASE II. A PENTACOORDINATED BINDING OF THE SCN-ION TO THE ZINC AT HIGH P*H

2cba: STRUCTURE OF NATIVE AND APO CARBONIC ANHYDRASE II AND SOME OF ITS ANION-LIGAND COMPLEXES

2cbb: STRUCTURE OF NATIVE AND APO CARBONIC ANHYDRASE II AND SOME OF ITS ANION-LIGAND COMPLEXES

2cbc: STRUCTURE OF NATIVE AND APO CARBONIC ANHYDRASE II AND SOME OF ITS ANION-LIGAND COMPLEXES

2cbd: STRUCTURE OF NATIVE AND APO CARBONIC ANHYDRASE II AND SOME OF ITS ANION-LIGAND COMPLEXES

2cbe: STRUCTURE OF NATIVE AND APO CARBONIC ANHYDRASE II AND SOME OF ITS ANION-LIGAND COMPLEXES

2eu2: Human Carbonic Anhydrase II in complex with novel inhibitors

2eu3: Human Carbonic anhydrase II in complex with novel inhibitors

2ez7: Carbonic anhydrase activators. Activation of isozymes I, II, IV, VA, VII and XIV with L- and D-histidine and crystallographic analysis of their adducts with isoform II: engineering proton transfer processes within the active site of an enzyme

2f14: The Crystal Structure of the Human Carbonic Anhydrase II in Complex with a Fluorescent Inhibitor

2fmg: Carbonic anhydrase activators. Activation of isoforms I, II, IV, VA, VII and XIV with L- and D- phenylalanine and crystallographic analysis of their adducts with isozyme II: sterospecific recognition within the active site of an enzyme and its consequences for the drug design, structure with L-phenylalanine

2fmz: Carbonic anhydrase activators. Activation of isoforms I, II, IV, VA, VII and XIV with L- and D- phenylalanine, structure with D-Phenylalanine.

2fnk: Activation of Human Carbonic Anhydrase II by exogenous proton donors

2fnm: Activation of human carbonic anhdyrase II by exogenous proton donors

2fnn: Activation of human carbonic anhydrase II by exogenous proton donors

2foq: Human Carbonic Anhydrase II complexed with two-prong inhibitors

2fos: Human Carbonic Anhydrase II complexed with two-prong inhibitors

2fou: Human Carbonic Anhydrase II complexed with two-prong inhibitors

2fov: Human Carbonic Anhydrase II complexed with two-prong inhibitors

2gd8: Crystal structure analysis of the human carbonic anhydrase II in complex with a 2-substituted estradiol bis-sulfamate

2geh: N-Hydroxyurea, a versatile zinc binding function in the design of metalloenzyme inhibitors

2h15: Carbonic anhydrase inhibitors: Clashing with Ala65 as a means of designing isozyme-selective inhibitors that show low affinity for the ubiquitous isozyme II

2h4n: H94N CARBONIC ANHYDRASE II COMPLEXED WITH ACETAZOLAMIDE

2hd6: Crystal structure of the human carbonic anhydrase II in complex with a hypoxia-activatable sulfonamide.

2hkk: Carbonic anhydrase activators: Solution and X-ray crystallography for the interaction of andrenaline with various carbonic anhydrase isoforms

2hl4: Crystal structure analysis of human carbonic anhydrase II in complex with a benzenesulfonamide derivative

2hnc: Crystal structure of the human carbonic anhydrase II in complex with the 5-amino-1,3,4-thiadiazole-2-sulfonamide inhibitor.

2hoc: Crystal structure of the human carbonic anhydrase II in complex with the 5-(4-amino-3-chloro-5-fluorophenylsulfonamido)-1,3,4-thiadiazole-2-sulfonamide inhibitor

2ili: Refine atomic structure of human carbonic anhydrase II

2nng: Structure of inhibitor binding to Carbonic Anhydrase II

2nno: Structure of inhibitor binding to Carbonic Anhydrase II

2nns: Structure of inhibitor binding to Carbonic Anhydrase II

2nnv: Structure of inhibitor binding to Carbonic Anhydrase II

2nwo: Structural and kinetic effect of hydrophobic mutations in the active site of human carbonic anhydrase II

2nwp: Structural and kinetic effects of hydrophobic mutations in the active site of human carbonic anhydrase II

2nwy: Structural and kinetic effects of hydrophobic mutations on the active site of human carbonic anhydrase II

2nwz: Structural and kinetic effects of hydrophobic mutations on the active site of human carbonic anhydrase II

2nxr: Structural effects of hydrophobic mutations on the active site of human carbonic anhydrase II

2nxs: Structural and kinetic effects of hydrophobic mutations in the active site of human carbonic anhydrase II

2nxt: Structural and kinetic effects of hydrophobic mutations in the active site of human carbonic anhydrase II

2o4z: Crystal structure of the Carbonic Anhydrase II complexed with hydroxysulfamide inhibitor

3ca2: CRYSTALLOGRAPHIC STUDIES OF INHIBITOR BINDING SITES IN HUMAN CARBONIC ANHYDRASE II. A PENTACOORDINATED BINDING OF THE SCN-ION TO THE ZINC AT HIGH P*H

4ca2: ENGINEERING THE HYDROPHOBIC POCKET OF CARBONIC ANHYDRASE II

4cac: REFINED STRUCTURE OF HUMAN CARBONIC ANHYDRASE II AT 2.0 ANGSTROMS RESOLUTION

5ca2: CONFORMATIONAL MOBILITY OF HIS-64 IN THE THR-200 (RIGHT ARROW) SER MUTANT OF HUMAN CARBONIC ANHYDRASE II

5cac: REFINED STRUCTURE OF HUMAN CARBONIC ANHYDRASE II AT 2.0 ANGSTROMS RESOLUTION

6ca2: ENGINEERING THE HYDROPHOBIC POCKET OF CARBONIC ANHYDRASE II

7ca2: ENGINEERING THE HYDROPHOBIC POCKET OF CARBONIC ANHYDRASE II

8ca2: ENGINEERING THE HYDROPHOBIC POCKET OF CARBONIC ANHYDRASE II

9ca2: ENGINEERING THE HYDROPHOBIC POCKET OF CARBONIC ANHYDRASE II

Carbonic anhydrases

CA1 CA2 CA3 CA4 CA5A CA5B CA6 CA7 CA8 CA9 CA10 CA11 CA12 CA13 CA14

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Carbonic anhydrase II

Interactions

References

Further reading