PDBe 3n9z

X-ray diffraction
2.17Å resolution

Crystal structure of human CYP11A1 in complex with 22-hydroxycholesterol

Released:
Source organism: Homo sapiens

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:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Cholesterol side-chain cleavage enzyme, mitochondrial Chains: A, B
Molecule details ›
Chains: A, B
Length: 487 amino acids
Theoretical weight: 56.89 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P05108 (Residues: 41-521; Coverage: 92%)
Gene names: CYP11A, CYP11A1
Sequence domains: Cytochrome P450
Structure domains: Cytochrome P450
Adrenodoxin, mitochondrial Chains: C, D
Molecule details ›
Chains: C, D
Length: 123 amino acids
Theoretical weight: 13.49 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P10109 (Residues: 62-184; Coverage: 67%)
Gene names: ADX, FDX1
Sequence domains: 2Fe-2S iron-sulfur cluster binding domain

Ligands and Environments


Cofactor: Ligand HEM 2 x HEM
2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P21
Unit cell:
a: 83.383Å b: 115.095Å c: 86.213Å
α: 90° β: 101.82° γ: 90°
R-values:
R R work R free
0.211 0.21 0.243
Expression system: Escherichia coli