Research workbench
Superoxide reductase (neelaredoxin) from archaeoglobus fulgidus E12V mutant
Analyse Superoxide reductase (neelaredoxin) from archaeoglobus fulgidus E12V mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4BFJ
- Type
- protein
- Length
- 248 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Superoxide reductase
- UniProt
- O29903
- Ligands
- FE
- Pockets
- 2 · best druggability 0.47
Structure
x-ray diffraction · 1 distinct chain · 7% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Superoxide reductase | protein | 124 | 7% helix, 53% strand | O29903 |
Ligands and binding sites
- FE · Fe (III) ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 182 | 0.47 | 0.75 | 42 | empty |
| 2 | 55 | 0.32 | 0.76 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1208 Ų buried · 20 hydrogen bonds · protein-protein
Compared structures
- 4BFJ · Superoxide reductase (Neelaredoxin) from Archaeoglobus fulgidus E12V mutant · the same entry in another collection · chain A against A, TM-score 1.00
- O29903 · AlphaFold monomer V2.0 prediction for putative superoxide reductase (O29903) · a predicted model of the same protein · chain A against A, TM-score 0.91
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 O29903
- Elsewhere: RCSB PDB 4BFJ · PDBe 4BFJ · UniProt O29903
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