› 5cpp

X-ray diffraction
2.08Å resolution

THE STRUCTURAL BASIS FOR SUBSTRATE-INDUCED CHANGES IN REDOX POTENTIAL AND SPIN EQUILIBRIUM IN CYTOCHROME P-450(CAM)

Released:
DOI: 10.2210/pdb5cpp/pdb
PDB entry 5cpp coloured by chain, front view.
PDB entry 5cpp coloured by chain, side view.
PDB entry 5cpp coloured by chain, top view.
Source organism: Pseudomonas putida
Primary publication:
The structural basis for substrate-induced changes in redox potential and spin equilibrium in cytochrome P-450CAM.
Raag R, Poulos TL
Biochemistry 28 917-22 (1989)
PMID: 2713354

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: 414 amino acids
Theoretical weight: 46.59 KDa
Source organism: Pseudomonas putida
Expression system: Not provided
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 ADO 1 x ADO
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 108.67Å b: 103.9Å c: 36.38Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 not available not available
Expression system: Not provided

Quick links

Citations

12 review citations

Cytochrome P450: what have we learned and what are the future issues?
Guengerich FP. (2004)
11 more

8 mentions without citation

LIGSITEcsc: predicting ligand binding sites using the Connolly surface and degree of conservation.
Huang et al. (2006)
7 more