Research workbench
X-ray structure of E114A mutant of superoxide reductase from desulfoarculus baarsii in the native, reduced form
Analyse X-ray structure of E114A mutant of superoxide reductase from desulfoarculus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2JI2
- Type
- protein
- Length
- 502 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Desulfoferrodoxin
- EC
- 1.15.1.2
- UniProt
- Q46495
- Ligands
- FE, FE2, CA, NO3
Structure
x-ray diffraction · 2 distinct chains · 3% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Desulfoferrodoxin (EC 1.15.1.2) | protein | 126 | 3% helix, 48% strand | Q46495 |
| B, D | Desulfoferrodoxin (EC 1.15.1.2) | protein | 125 | 3% helix, 48% strand | Q46495 |
Ligands and binding sites
- FE · Fe (III) ion · metal · 4 copies · chains A, B, C, D
- FE2 · Fe (II) ion · metal · 4 copies · chains A, B, C, D
- CA · Calcium ion · metal · 4 copies · chains A, B, C, D
- NO3 · Nitrate ion · ion · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
3 interfaces between chains.
- A–B · 1634 Ų buried · 31 hydrogen bonds · protein-protein
- C–D · 1624 Ų buried · 31 hydrogen bonds · protein-protein
- A–D · 45 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 2JI2 · X-ray structure of E114A mutant of superoxide reductase from Desulfoarculus baarsii in… · the same entry in another collection · chain D against D, 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 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 2JI2 · PDBe 2JI2 · UniProt Q46495
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