Research workbench
Superoxide reductase (neelaredoxin) from archaeoglobus fulgidus E12V in the reduced form
Analyse Superoxide reductase (neelaredoxin) from archaeoglobus fulgidus E12V in the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4C4B
- Type
- protein
- Length
- 250 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Superoxide reductase
- UniProt
- O29903
- Ligands
- FE2
Structure
x-ray diffraction · 1 distinct chain · 7% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Superoxide reductase | protein | 125 | 7% helix, 50% strand | O29903 |
Ligands and binding sites
- FE2 · Fe (II) ion · metal · 2 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 3 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 · 1220 Ų buried · 21 hydrogen bonds · protein-protein
Compared structures
- 4C4B · Superoxide reductase (Neelaredoxin) from Archaeoglobus fulgidus E12V in the reduced form · 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 4C4B · PDBe 4C4B · UniProt O29903
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