› 1geb

X-ray diffraction
2.03Å resolution

X-RAY CRYSTAL STRUCTURE AND CATALYTIC PROPERTIES OF THR252ILE MUTANT OF CYTOCHROME P450CAM

Released:
DOI: 10.2210/pdb1geb/pdb
PDB entry 1geb coloured by chain, front view.
PDB entry 1geb coloured by chain, side view.
PDB entry 1geb coloured by chain, top view.
Source organism: Pseudomonas putida
Primary publication:
X-ray crystal structure and catalytic properties of Thr252Ile mutant of cytochrome P450cam: roles of Thr252 and water in the active center.
Hishiki T, Shimada H, Nagano S, Egawa T, Kanamori Y, Makino R, Park SY, Adachi S, Shiro Y, Ishimura Y
J Biochem 128 965-74 (2000)
PMID: 11098139

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: 415 amino acids
Theoretical weight: 46.73 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 1 x HEM
1 bound ligand:
Ligand CAM 1 x CAM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44B2
Spacegroup: P212121
Unit cell:
a: 106.43Å b: 103.44Å c: 35Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.187 0.228
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Diversity of P450 enzymes in the biosynthesis of natural products.
Podust et al. (2012)
6 more