Research workbench
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
- 1VZG
- Type
- protein
- Length
- 250 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q46495
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 125 | — | Q46495 |
Compared structures
- 1VZG · 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
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 1VZG · PDBe 1VZG · UniProt Q46495
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