› 3p3x

X-ray diffraction
2.3Å resolution

Crystal Structure of the Cytochrome P450 Monooxygenase AurH (nterm-AurH-I) from Streptomyces Thioluteus

Released:
DOI: 10.2210/pdb3p3x/pdb
PDB entry 3p3x coloured by chain, front view.
PDB entry 3p3x coloured by chain, side view.
PDB entry 3p3x coloured by chain, top view.
Source organism: Streptomyces thioluteus
Primary publication:
Structural fine-tuning of a multifunctional cytochrome P450 monooxygenase.
Zocher G, Richter ME, Mueller U, Hertweck C
J Am Chem Soc 133 2292-302 (2011)
PMID: 21280577

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180691 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Putative cytochrome P450 Chains: A, B
Molecule details ›
Chains: A, B
Length: 416 amino acids
Theoretical weight: 46.17 KDa
Source organism: Streptomyces thioluteus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q70KH6 (Residues: 1-406; Coverage: 100%)
Gene name: aurH
Sequence domains: Cytochrome P450
Structure domains: Cytochrome P450

Ligands and Environments

4 bound ligands:
Ligand HEM 2 x HEM
Ligand GOL 3 x GOL
Ligand SO4 1 x SO4
Ligand CL 2 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.2
Spacegroup: P21212
Unit cell:
a: 129.33Å b: 131.78Å c: 53.23Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.228 0.226 0.28
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Diversity of P450 enzymes in the biosynthesis of natural products.
Podust et al. (2012)
10 more

2 mentions without citation

Cytochromes P450 for natural product biosynthesis in Streptomyces: sequence, structure, and function.
Rudolf et al. (2017)
1 more