› 1j51

X-ray diffraction
2.2Å resolution

CRYSTAL STRUCTURE OF CYTOCHROME P450CAM MUTANT (F87W/Y96F/V247L/C334A) WITH 1,3,5-TRICHLOROBENZENE

Released:
DOI: 10.2210/pdb1j51/pdb
PDB entry 1j51 coloured by chain, front view.
PDB entry 1j51 coloured by chain, side view.
PDB entry 1j51 coloured by chain, top view.
Source organism: Pseudomonas putida
Primary publication:
Crystal structure of the F87W/Y96F/V247L mutant of cytochrome P-450cam with 1,3,5-trichlorobenzene bound and further protein engineering for the oxidation of pentachlorobenzene and hexachlorobenzene.
Chen X, Christopher A, Jones JP, Bell SG, Guo Q, Xu F, Rao Z, Wong LL
J Biol Chem 277 37519-26 (2002)
PMID: 12114516

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, C, D
Molecule details ›
Chains: A, B, C, D
Length: 414 amino acids
Theoretical weight: 46.59 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 4 x HEM
2 bound ligands:
Ligand K 4 x K
Ligand TCZ 3 x TCZ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P1
Unit cell:
a: 66.87Å b: 62.44Å c: 95.52Å
α: 89.98° β: 90.3° γ: 90.09°
R-values:
R R work R free
0.186 0.186 0.258
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Cytochromes P450 as versatile biocatalysts.
Bernhardt R. (2006)
8 more

1 mention without citation

Halogen bonds in biological molecules.
Auffinger et al. (2004)