› 3fwf

X-ray diffraction
1.83Å resolution

Ferric camphor bound cytochrome P450cam containing a Selenocysteine as the 5th heme ligand, monoclinic crystal form

Released:
DOI: 10.2210/pdb3fwf/pdb
PDB entry 3fwf coloured by chain, front view.
PDB entry 3fwf coloured by chain, side view.
PDB entry 3fwf coloured by chain, top view.
Source organism: Pseudomonas putida
Primary publication:
Probing the role of the proximal heme ligand in cytochrome P450cam by recombinant incorporation of selenocysteine.
Aldag C, Gromov IA, García-Rubio I, von Koenig K, Schlichting I, Jaun B, Hilvert D
Proc Natl Acad Sci U S A 106 5481-6 (2009)
PMID: 19293375

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 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
Molecule details ›
Chains: A, B
Length: 405 amino acids
Theoretical weight: 45.64 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 HEM 2 x HEM
2 bound ligands:
Ligand CAM 2 x CAM
Ligand K 4 x K
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P21
Unit cell:
a: 67.52Å b: 61.93Å c: 94.46Å
α: 90° β: 90.8° γ: 90°
R-values:
R R work R free
0.164 0.162 0.207
Expression system: Escherichia coli

Quick links

Citations

5 review citations

[NiFe] hydrogenases: a common active site for hydrogen metabolism under diverse conditions.
Shafaat et al. (2013)
4 more

2 mentions without citation

Conformational plasticity and structure/function relationships in cytochromes P450.
Pochapsky et al. (2010)
1 more