MolNFT v1 · #25579 · protein

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

1VZI · Desulfoferrodoxin: “Structure of superoxide reductase bound to ferrocyanide and active site expansion upon X-ray induced…”. X-ray diffraction, 3 ligands (FE2, CA, CL). MolNFT v1 #25579 on GenesisL1: 3D structure, binding sites and…

PDB: 1VZI
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: FE2, CA, CL

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Desulfoferrodoxin (EC 1.15.1.2)	protein	125	3% helix, 49% strand	Q46495

Ligands and binding sites

FE2 · Fe (II) ion · metal · 4 copies · chains A, B
CA · Calcium ion · metal · 2 copies · chains A, B
CL · Chloride ion · ion · 4 copies · 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 · 1635 Å² buried · 36 hydrogen bonds · protein-protein

Compared structures

1VZI · 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 B against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q46495
Elsewhere: RCSB PDB 1VZI · PDBe 1VZI · UniProt Q46495

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