› 3eqm

X-ray diffraction
2.9Å resolution

Crystal structure of human placental aromatase cytochrome P450 in complex with androstenedione

Released:
DOI: 10.2210/pdb3eqm/pdb
PDB entry 3eqm coloured by chain, front view.
PDB entry 3eqm coloured by chain, side view.
PDB entry 3eqm coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for androgen specificity and oestrogen synthesis in human aromatase.
Ghosh D, Griswold J, Erman M, Pangborn W
Nature 457 219-23 (2009)
PMID: 19129847

Function and Biology Details

Reaction catalysed: 
(1a) testosterone + [reduced NADPH--hemoprotein reductase] + O(2) = 19-hydroxytestosterone + H(2)O + [oxidized NADPH--hemoprotein reductase]
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145862 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aromatase Chain: A
Molecule details ›
Chain: A
Length: 503 amino acids
Theoretical weight: 57.95 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P11511 (Residues: 1-503; Coverage: 100%)
Gene names: ARO1, CYAR, CYP19, CYP19A1
Sequence domains: Cytochrome P450
Structure domains: Cytochrome P450

Ligands and Environments


Cofactor: Ligand HEM 1 x HEM
2 bound ligands:
Ligand ASD 1 x ASD
Ligand PO4 2 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P3221
Unit cell:
a: 140.208Å b: 140.208Å c: 119.266Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.215 0.214 0.244

Quick links

Citations

45 review citations

The molecular biology, biochemistry, and physiology of human steroidogenesis and its disorders.
Miller et al. (2011)
44 more

94 mentions without citation

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