› 1z8o

X-ray diffraction
1.7Å resolution

Ferrous dioxygen complex of the wild-type cytochrome P450eryF

Released:
DOI: 10.2210/pdb1z8o/pdb
PDB entry 1z8o coloured by chain, front view.
PDB entry 1z8o coloured by chain, side view.
PDB entry 1z8o coloured by chain, top view.
Source organism: Saccharopolyspora erythraea
Primary publication:
Crystal structures of the ferrous dioxygen complex of wild-type cytochrome P450eryF and its mutants, A245S and A245T: investigation of the proton transfer system in P450eryF.
Nagano S, Cupp-Vickery JR, Poulos TL
J Biol Chem 280 22102-7 (2005)
PMID: 15824115

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: 404 amino acids
Theoretical weight: 45.15 KDa
Source organism: Saccharopolyspora erythraea
Expression system: Escherichia coli
UniProt:
  • Canonical: Q00441 (Residues: 1-404; Coverage: 100%)
Gene names: CYP107A1, SACE_0730, eryF
Sequence domains: Cytochrome P450
Structure domains: Cytochrome P450

Ligands and Environments

3 bound ligands:
Ligand HEM 1 x HEM
Ligand OXY 1 x OXY
Ligand DEB 1 x DEB
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P212121
Unit cell:
a: 53.9Å b: 78.64Å c: 97.21Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.194 0.216
Expression system: Escherichia coli

Quick links

Citations

19 review citations

Heme enzyme structure and function.
Poulos TL. (2014)
18 more

5 mentions without citation

Conformational plasticity and structure/function relationships in cytochromes P450.
Pochapsky et al. (2010)
4 more