Ferredoxin fold
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A ferredoxin fold is a common α+β protein fold with a signature βαββαβ secondary structure along its backbone. Structurally, the ferredoxin fold can be regarded as a long, symmetric hairpin that is wrapped once around, so that its two terminal β-strands hydrogen-bond to the central two β-strands, forming a four-stranded, antiparallel β-sheet covered on one side by two α-helices.
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Protein tertiary structure | ||
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General: | Structural domain | Protein folding | |
All-α folds: | Helix bundle | Globin fold | Homeodomain fold | Alpha solenoid | |
All-β folds: | Immunoglobulin fold | Beta barrel | Beta-propeller domain | |
α/β folds: | TIM barrel | Leucine-rich repeat | Flavodoxin fold | Thioredoxin fold | Trefoil knot fold | |
α+β folds: | Ferredoxin fold | Ribonuclease A | SH2-like fold | |
Irregular folds: | Conotoxin | |
←Secondary structure | Structure determination methods | Quaternary structure→ |