1k2o

X-ray diffraction
1.65Å resolution

Cytochrome P450Cam with Bound BIS(2,2'-BIPYRIDINE)-(5-METHYL-2-2'-BIPYRIDINE)-C2-ADAMANTANE RUTHENIUM (II)

Released:
Source organism: Pseudomonas putida
Primary publication:
Probing the open state of cytochrome P450cam with ruthenium-linker substrates.
Proc Natl Acad Sci U S A 98 12420-5 (2001)
PMID: 11606730

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:

Structure analysis Details

Assembly composition:
monomeric (preferred)
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: 414 amino acids
Theoretical weight: 46.56 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 2 x HEM
3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P1
Unit cell:
a: 63.87Å b: 67.05Å c: 72.52Å
α: 71.16° β: 65.2° γ: 62.31°
R-values:
R R work R free
0.21 0.21 0.226
Expression system: Escherichia coli