Research workbench
Superoxide reductase (neelaredoxin) from ignicoccus hospitalis T24K
Analyse Superoxide reductase (neelaredoxin) from ignicoccus hospitalis T24K in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4BRJ
- Type
- protein
- Length
- 124 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Desulfoferrodoxin, ferrous iron-binding region
- UniProt
- A8AC72
- Ligands
- FE
Structure
x-ray diffraction · 1 distinct chain · 6% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Desulfoferrodoxin, ferrous iron-binding region | protein | 124 | 6% helix, 48% strand | A8AC72 |
Ligands and binding sites
- FE · Fe (III) ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 4BRJ · Superoxide reductase (Neelaredoxin) from Ignicoccus hospitalis T24K · the same entry in another collection · 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 A8AC72
- Elsewhere: RCSB PDB 4BRJ · PDBe 4BRJ · UniProt A8AC72
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