› 2feu

X-ray diffraction
1.7Å resolution

P450CAM from Pseudomonas putida reconstituted with manganic protoporphyrin IX

Released:
DOI: 10.2210/pdb2feu/pdb
PDB entry 2feu coloured by chain, front view.
PDB entry 2feu coloured by chain, side view.
PDB entry 2feu coloured by chain, top view.
Source organism: Pseudomonas putida
Primary publication:
The status of high-valent metal oxo complexes in the P450 cytochromes.
Makris TM, von Koenig K, Schlichting I, Sligar SG
J Inorg Biochem 100 507-18 (2006)
PMID: 16510191

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 411 amino acids
Theoretical weight: 46.47 KDa
Source organism: Pseudomonas putida
Expression system: Escherichia coli
UniProt:
  • Canonical: P00183 (Residues: 11-415; Coverage: 98%)
Gene names: camC, cyp101
Sequence domains: Cytochrome P450
Structure domains: Cytochrome P450

Ligands and Environments


Cofactor: Ligand MNR 2 x MNR
3 bound ligands:
Ligand K 3 x K
Ligand CAM 2 x CAM
Ligand TRS 1 x TRS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P21
Unit cell:
a: 67.13Å b: 62.23Å c: 94.71Å
α: 90° β: 90.64° γ: 90°
R-values:
R R work R free
0.214 0.214 0.238
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Spectroscopic features of cytochrome P450 reaction intermediates.
Luthra et al. (2011)
8 more

1 mention without citation

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