› 2fer

X-ray diffraction
1.7Å resolution

P450CAM from Pseudomonas putida reconstituted with manganic protoporphyrin IX

Released:
DOI: 10.2210/pdb2fer/pdb
PDB entry 2fer coloured by chain, front view.
PDB entry 2fer coloured by chain, side view.
PDB entry 2fer 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 Chain: A
Molecule details ›
Chain: A
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 1 x MNR
1 bound ligand:
Ligand K 1 x K
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA, null
Spacegroup: P212121
Unit cell:
a: 63.32Å b: 63.82Å c: 105.44Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.179 0.225
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)