› 2a1n

X-ray diffraction
1.9Å resolution

Crystal structure of ferrous dioxygen complex of D251N cytochrome P450cam

Released:
DOI: 10.2210/pdb2a1n/pdb
PDB entry 2a1n coloured by chain, front view.
PDB entry 2a1n coloured by chain, side view.
PDB entry 2a1n coloured by chain, top view.
Source organism: Pseudomonas putida
Primary publication:
Crystallographic study on the dioxygen complex of wild-type and mutant cytochrome P450cam. Implications for the dioxygen activation mechanism.
Nagano S, Poulos TL
J Biol Chem 280 31659-63 (2005)
PMID: 15994329

Function and Biology Details

Reaction catalysed: 
(+)-camphor + reduced putidaredoxin + O(2) = (+)-exo-5-hydroxycamphor + oxidized putidaredoxin + 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-132314 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Camphor 5-monooxygenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 415 amino acids
Theoretical weight: 46.69 KDa
Source organism: Pseudomonas putida
Expression system: Escherichia coli
UniProt:
  • Canonical: P00183 (Residues: 1-415; Coverage: 100%)
Gene names: camC, cyp101
Sequence domains: Cytochrome P450
Structure domains: Cytochrome P450

Ligands and Environments


Cofactor: Ligand HEM 2 x HEM
4 bound ligands:
Ligand K 3 x K
Ligand OXY 2 x OXY
Ligand CAM 2 x CAM
Ligand TRS 1 x TRS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21
Unit cell:
a: 67.01Å b: 62.13Å c: 95.06Å
α: 90° β: 90.4° γ: 90°
R-values:
R R work R free
0.191 0.191 0.235
Expression system: Escherichia coli

Quick links

Citations

26 review citations

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

2 mentions without citation

Mechanisms of Cytochrome P450-Catalyzed Oxidations.
Guengerich FP. (2018)
1 more