PDBe 1oxa

X-ray diffraction
2.1Å resolution

CYTOCHROME P450 (DONOR:O2 OXIDOREDUCTASE)

Released:
Source organism: Saccharopolyspora erythraea
Primary publication:
Structure of cytochrome P450eryF involved in erythromycin biosynthesis.
Nat. Struct. Biol. 2 144-53 (1995)
PMID: 7749919

Function and Biology Details

Reaction catalysed:
6-deoxyerythronolide B + NADPH + O(2) = erythronolide B + NADP(+) + H(2)O. 
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (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:

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