› 1gwi

X-ray diffraction
1.92Å resolution

The 1.92 A structure of Streptomyces coelicolor A3(2) CYP154C1: A new monooxygenase that functionalizes macrolide ring systems

Released:
DOI: 10.2210/pdb1gwi/pdb
PDB entry 1gwi coloured by chain, front view.
PDB entry 1gwi coloured by chain, side view.
PDB entry 1gwi coloured by chain, top view.
Source organism: Streptomyces coelicolor A3(2)
Primary publication:
The 1.92-A structure of Streptomyces coelicolor A3(2) CYP154C1. A new monooxygenase that functionalizes macrolide ring systems.
Podust LM, Kim Y, Arase M, Neely BA, Beck BJ, Bach H, Sherman DH, Lamb DC, Kelly SL, Waterman MR
J. Biol. Chem. 278 12214-21 (2003)
PMID: 12519772

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192194 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytochrome P450-family protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 411 amino acids
Theoretical weight: 44.48 KDa
Source organism: Streptomyces coelicolor A3(2)
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9L142 (Residues: 1-407; Coverage: 100%)
Gene names: SC6D11.13c, SCO7417
Sequence domains: Cytochrome P450
Structure domains: Cytochrome P450

Ligands and Environments

2 bound ligands:
Ligand SO4 8 x SO4
Ligand HEM 2 x HEM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 62.728Å b: 131.973Å c: 134.886Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.208 0.228
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Variations on a (t)heme--novel mechanisms, redox partners and catalytic functions in the cytochrome P450 superfamily.
Munro et al. (2007)
7 more

10 mentions without citation

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