› 1iwi

X-ray diffraction
2Å resolution

Putidaredoxin-Binding Stablilizes an Active Conformer of Cytochrome P450cam in its Reduced State; Crystal Structure of Cytochrome P450cam

Released:
DOI: 10.2210/pdb1iwi/pdb
PDB entry 1iwi coloured by chain, front view.
PDB entry 1iwi coloured by chain, side view.
PDB entry 1iwi coloured by chain, top view.
Source organism: Pseudomonas putida
Primary publication:
Infrared spectroscopic and mutational studies on putidaredoxin-induced conformational changes in ferrous CO-P450cam.
Nagano S, Shimada H, Tarumi A, Hishiki T, Kimata-Ariga Y, Egawa T, Suematsu M, Park SY, Adachi S, Shiro Y, Ishimura Y
Biochemistry 42 14507-14 (2003)
PMID: 14661963

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: 46.72 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: 109.16Å b: 104.33Å c: 36.18Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.177 0.177 0.182
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Heme enzyme structure and function.
Poulos TL. (2014)
8 more

1 mention without citation

Structural motif-based homology modeling of CYP27A1 and site-directed mutational analyses affecting vitamin D hydroxylation.
Prosser et al. (2006)