› 2rfc

X-ray diffraction
3.1Å resolution

Ligand bound (4-phenylimidazole) Crystal Structure of a Cytochrome P450 from the Thermoacidophilic Archaeon Picrophilus Torridus

Released:
DOI: 10.2210/pdb2rfc/pdb
Model geometry
Fit model/data
PDB entry 2rfc coloured by chain, front view.
PDB entry 2rfc coloured by chain, side view.
PDB entry 2rfc coloured by chain, top view.
Source organism: Picrophilus oshimae
Primary publication:
Crystal structure and properties of CYP231A2 from the thermoacidophilic archaeon Picrophilus torridus.
Ho WW, Li H, Nishida CR, de Montellano PR, Poulos TL
Biochemistry 47 2071-9 (2008)
PMID: 18197710

Function and Biology Details

Reaction catalysed: 
RH + [reduced NADPH--hemoprotein reductase] + O(2) = ROH + [oxidized NADPH--hemoprotein reductase] + H(2)O
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-179834 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytochrome P450 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 343 amino acids
Theoretical weight: 39.61 KDa
Source organism: Picrophilus oshimae
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q6KZ68 (Residues: 1-343; Coverage: 100%)
Gene name: PTO1399
Sequence domains: Cytochrome P450
Structure domains: Cytochrome P450

Ligands and Environments


Cofactor: Ligand HEM 4 x HEM
1 bound ligand:
Ligand PIM 4 x PIM
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SSRL BEAMLINE BL1-5
Spacegroup: P21
Unit cell:
a: 48.52Å b: 141.01Å c: 101.03Å
α: 90° β: 90.3° γ: 90°
R-values:
R R work R free
0.229 0.229 0.334
Expression system: Escherichia coli BL21

Quick links

Citations

3 review citations

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

1 mention without citation

Accurate Representation of Protein-Ligand Structural Diversity in the Protein Data Bank (PDB).
Shinada et al. (2020)