Ferredoxin fold

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Ribbon diagram of acylphosphatase (PDB accession code 2ACY), which adopts a ferredoxin fold with an extra β-strand at the C-terminus (shown in red). The ribbon is colored from blue (N-terminus) to red (C-terminus).
Ribbon diagram of acylphosphatase (PDB accession code 2ACY), which adopts a ferredoxin fold with an extra β-strand at the C-terminus (shown in red). The ribbon is colored from blue (N-terminus) to red (C-terminus).

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.




Protein tertiary structure
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→
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