› 3mzs

X-ray diffraction
2.5Å resolution

Crystal Structure of Cytochrome P450 CYP11A1 in complex with 22-hydroxy-cholesterol

Released:
DOI: 10.2210/pdb3mzs/pdb
PDB entry 3mzs coloured by chain, front view.
PDB entry 3mzs coloured by chain, side view.
PDB entry 3mzs coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Structural basis for three-step sequential catalysis by the cholesterol side chain cleavage enzyme CYP11A1.
Mast N, Annalora AJ, Lodowski DT, Palczewski K, Stout CD, Pikuleva IA
J Biol Chem 286 5607-13 (2011)
PMID: 21159775

Function and Biology Details

Reaction catalysed: 
(1a) cholesterol + 2 reduced adrenodoxin + O(2) + 2 H(+) = (22R)-22-hydroxycholesterol + 2 oxidized adrenodoxin + H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132317 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cholesterol side-chain cleavage enzyme, mitochondrial Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 486 amino acids
Theoretical weight: 57.12 KDa
Source organism: Bos taurus
Expression system: Escherichia coli
UniProt:
  • Canonical: P00189 (Residues: 41-520; Coverage: 92%)
Gene name: CYP11A1
Sequence domains: Cytochrome P450
Structure domains: Cytochrome P450

Ligands and Environments


Cofactor: Ligand HEM 4 x HEM
2 bound ligands:
Ligand HC9 4 x HC9
Ligand IPA 4 x IPA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: P21
Unit cell:
a: 109.45Å b: 94.63Å c: 113.5Å
α: 90° β: 89.96° γ: 90°
R-values:
R R work R free
0.266 0.266 0.281
Expression system: Escherichia coli

Quick links

Citations

19 review citations

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

8 mentions without citation

Novel activities of CYP11A1 and their potential physiological significance.
Slominski et al. (2015)
7 more