Research workbench
Crystal structure of oxidoreductase, 2OG-FE(II) oxygenase family, from burkholderia pseudomallei
Analyse Crystal structure of oxidoreductase, 2OG-FE(II) oxygenase family, from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6N1F
- Type
- protein
- Length
- 832 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q3JFV4
- Ligands
- FE, CL
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 206 | — | Q3JFV4 |
| B | — | protein | 208 | — | Q3JFV4 |
| C | — | protein | 205 | — | Q3JFV4 |
| D | — | protein | 213 | — | Q3JFV4 |
Ligands and binding sites
- FE · Fe (III) ion · metal · 4 copies · chains A, B, C, D
- CL · Chloride ion · ion · 2 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6N1F · Crystal structure of Oxidoreductase, 2OG-Fe(II) oxygenase family, from Burkholderia… · 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 Q3JFV4
- Elsewhere: RCSB PDB 6N1F · PDBe 6N1F · UniProt Q3JFV4
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.