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Structure of superoxide reductase bound to ferrocyanide and active site expansion upon X-ray induced photoreduction

Analyse Structure of superoxide reductase bound to ferrocyanide and active site… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1VZH
Type
protein
Length
250 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Desulfoferrodoxin
EC
1.15.1.2
UniProt
Q46495
Ligands
FC6, FE, CA

Structure

x-ray diffraction · 1 distinct chain · 3% helix, 49% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BDesulfoferrodoxin (EC 1.15.1.2)protein1253% helix, 49% strandQ46495

Ligands and binding sites

  • FC6 · Hexacyanoferrate(3-) · ligand · 2 copies · chains A, B
  • FE · Fe (III) ion · metal · 4 copies · chains A, B
  • CA · Calcium ion · metal · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Interfaces

1 interface between chains.

  • A–B · 1632 Ų buried · 32 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 1VZH · Structure of superoxide reductase bound to ferrocyanide and active site expansion upon… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q46495 · AlphaFold monomer V2.0 prediction for desulfoferrodoxin (Q46495) · a predicted model of the same protein · chain A against A, TM-score 0.99

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