› 1p2y

X-ray diffraction
2.3Å resolution

CRYSTAL STRUCTURE OF CYTOCHROME P450CAM IN COMPLEX WITH (S)-(-)-NICOTINE

Released:
DOI: 10.2210/pdb1p2y/pdb
PDB entry 1p2y coloured by chain, front view.
PDB entry 1p2y coloured by chain, side view.
PDB entry 1p2y coloured by chain, top view.
Source organism: Pseudomonas putida
Primary publication:
Crystallographic studies on the complex behavior of nicotine binding to P450cam (CYP101).
Strickler M, Goldstein BM, Maxfield K, Shireman L, Kim G, Matteson DS, Jones JP
Biochemistry 42 11943-50 (2003)
PMID: 14556625

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 domain:

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 Chain: A
Molecule details ›
Chain: A
Length: 420 amino acids
Theoretical weight: 47.42 KDa
Source organism: Pseudomonas putida
Expression system: Escherichia coli
UniProt:
  • Canonical: P00183 (Residues: 2-415; Coverage: 100%)
Gene names: camC, cyp101
Sequence domains: Cytochrome P450
Structure domains: Cytochrome P450

Ligands and Environments


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

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE A1
Spacegroup: P43212
Unit cell:
a: 64.05Å b: 64.05Å c: 251.06Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.25 0.223 0.263
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Non-Michaelis-Menten kinetics in cytochrome P450-catalyzed reactions.
Atkins WM. (2005)
2 more

7 mentions without citation

Variability in docking success rates due to dataset preparation.
Corbeil et al. (2012)
6 more