PDBe 3n9y

X-ray diffraction
2.1Å resolution

Crystal structure of human CYP11A1 in complex with cholesterol

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: 114 amino acids
Theoretical weight: 12.57 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P10109 (Residues: 62-175; Coverage: 62%)
Gene names: ADX, FDX1
Sequence domains: 2Fe-2S iron-sulfur cluster binding domain
Structure domains: Ubiquitin-like (UB roll)

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 19-ID
Spacegroup: P21
Unit cell:
a: 82.999Å b: 114.686Å c: 86.019Å
α: 90° β: 101.96° γ: 90°
R-values:
R R work R free
0.207 0.205 0.242
Expression system: Escherichia coli