› 1t86

X-ray diffraction
1.9Å resolution

Crystal Structure of the Ferrous Cytochrome P450cam Mutant (L358P/C334A)

Released:
DOI: 10.2210/pdb1t86/pdb
PDB entry 1t86 coloured by chain, front view.
PDB entry 1t86 coloured by chain, side view.
PDB entry 1t86 coloured by chain, top view.
Source organism: Pseudomonas putida
Primary publication:
Crystal structure of the cytochrome p450cam mutant that exhibits the same spectral perturbations induced by putidaredoxin binding.
Nagano S, Tosha T, Ishimori K, Morishima I, Poulos TL
J Biol Chem 279 42844-9 (2004)
PMID: 15269210

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
Molecule details ›
Chains: A, B
Length: 414 amino acids
Theoretical weight: 46.54 KDa
Source organism: Pseudomonas putida
Expression system: Escherichia coli BL21
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
2 bound ligands:
Ligand K 2 x K
Ligand CAM 2 x CAM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21
Unit cell:
a: 57.01Å b: 101.17Å c: 72.92Å
α: 90° β: 108.3° γ: 90°
R-values:
R R work R free
0.199 0.199 0.236
Expression system: Escherichia coli BL21

Quick links

Citations

10 review citations

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

2 mentions without citation

Updating the Paradigm: Redox Partner Binding and Conformational Dynamics in Cytochromes P450.
Poulos et al. (2022)
1 more