Research workbench
R2-like ligand-binding oxidase G68L mutant with anaerobically reconstituted MN/FE cofactor
Analyse R2-like ligand-binding oxidase G68L mutant with anaerobically reconstituted… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6I95
- Type
- protein
- Length
- 275 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q5KW80
- Ligands
- OCA, FE2, MN
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 275 | — | Q5KW80 |
Ligands and binding sites
- OCA · Octanoic acid (caprylic acid) · ligand · chains A
- FE2 · Fe (II) ion · metal · 2 copies · chains A
- MN · Manganese (II) ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6I95 · R2-like ligand-binding oxidase G68L mutant with anaerobically reconstituted Mn/Fe cofactor · 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 Q5KW80
- Elsewhere: RCSB PDB 6I95 · PDBe 6I95 · UniProt Q5KW80
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