› 1oxa

X-ray diffraction
2.1Å resolution

CYTOCHROME P450 (DONOR:O2 OXIDOREDUCTASE)

Released:
DOI: 10.2210/pdb1oxa/pdb
PDB entry 1oxa coloured by chain, front view.
PDB entry 1oxa coloured by chain, side view.
PDB entry 1oxa coloured by chain, top view.
Source organism: Saccharopolyspora erythraea
Primary publication:
Structure of cytochrome P450eryF involved in erythromycin biosynthesis.
Cupp-Vickery JR, Poulos TL
Nat Struct Biol 2 144-53 (1995)
PMID: 7749919

Function and Biology Details

Reaction catalysed: 
6-deoxyerythronolide B + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H(+) + O(2) = erythronolide B + 2 oxidized ferredoxin [iron-sulfur] cluster + H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169415 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
6-deoxyerythronolide B hydroxylase Chain: A
Molecule details ›
Chain: A
Length: 403 amino acids
Theoretical weight: 44.52 KDa
Source organism: Saccharopolyspora erythraea
UniProt:
  • Canonical: Q00441 (Residues: 2-404; Coverage: 100%)
Gene names: CYP107A1, SACE_0730, eryF
Sequence domains: Cytochrome P450
Structure domains: Cytochrome P450

Ligands and Environments

2 bound ligands:
Ligand HEM 1 x HEM
Ligand DEB 1 x DEB
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 54.16Å b: 79.67Å c: 99.48Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.196 not available

Quick links

Citations

34 review citations

Functional genomics of P450s.
Schuler et al. (2003)
33 more

12 mentions without citation

Recent Structural Insights into Cytochrome P450 Function.
Guengerich et al. (2016)
11 more