Research workbench
Superoxide reductase (neelaredoxin) from nanoarchaeum equitans
Analyse Superoxide reductase (neelaredoxin) from nanoarchaeum equitans in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4BV1
- Type
- protein
- Length
- 436 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NEQ011
- UniProt
- Q74MF3
- Ligands
- FE
Structure
x-ray diffraction · 1 distinct chain · 3% helix, 61% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | NEQ011 | protein | 109 | 3% helix, 61% strand | Q74MF3 |
Ligands and binding sites
- FE · Fe (III) ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
6 interfaces between chains.
- A–D · 1426 Ų buried · 23 hydrogen bonds · protein-protein
- B–C · 1424 Ų buried · 22 hydrogen bonds · protein-protein
- A–B · 860 Ų buried · 15 hydrogen bonds · protein-protein
- C–D · 844 Ų buried · 17 hydrogen bonds · protein-protein
- A–C · 534 Ų buried · 8 hydrogen bonds · protein-protein
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 Q74MF3
- Elsewhere: RCSB PDB 4BV1 · PDBe 4BV1 · UniProt Q74MF3
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