2p85

X-ray diffraction
2.35Å resolution

Structure of Human Lung Cytochrome P450 2A13 with indole bound in two alternate conformations

Released:
Source organism: Homo sapiens
Primary publication:
Structure of the human lung cytochrome P450 2A13.
J Biol Chem 282 17306-13 (2007)
PMID: 17428784

Function and Biology Details

Reaction catalysed:
RH + [reduced NADPH--hemoprotein reductase] + O(2) = ROH + [oxidized NADPH--hemoprotein reductase] + H(2)O
Biochemical function:
Biological process:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172559 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytochrome P450 2A13 Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 476 amino acids
Theoretical weight: 54.8 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q16696 (Residues: 23-494; Coverage: 96%)
Gene name: CYP2A13
Sequence domains: Cytochrome P450
Structure domains: Cytochrome P450

Ligands and Environments


Cofactor: Ligand HEM 6 x HEM
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: P2
Unit cell:
a: 121.32Å b: 110.28Å c: 142Å
α: 90° β: 110.28° γ: 90°
R-values:
R R work R free
0.219 0.219 0.277
Expression system: Escherichia coli