› 1pkf

X-ray diffraction
2.1Å resolution

Crystal Structure of Epothilone D-bound Cytochrome P450epoK

Released:
DOI: 10.2210/pdb1pkf/pdb
Model geometry
Fit model/data
PDB entry 1pkf coloured by chain, front view.
PDB entry 1pkf coloured by chain, side view.
PDB entry 1pkf coloured by chain, top view.
Source organism: Sorangium cellulosum
Primary publication:
Crystal structures of epothilone D-bound, epothilone B-bound, and substrate-free forms of cytochrome P450epoK.
Nagano S, Li H, Shimizu H, Nishida C, Ogura H, Ortiz de Montellano PR, Poulos TL
J Biol Chem 278 44886-93 (2003)
PMID: 12933799

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-191899 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Epothilone C/D epoxidase Chain: A
Molecule details ›
Chain: A
Length: 419 amino acids
Theoretical weight: 46.82 KDa
Source organism: Sorangium cellulosum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9KIZ4 (Residues: 1-419; Coverage: 100%)
Gene names: cyp167A1, epoF, epoK
Sequence domains: Cytochrome P450
Structure domains: Cytochrome P450

Ligands and Environments

2 bound ligands:
Ligand HEM 1 x HEM
Ligand EPD 1 x EPD
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P4322
Unit cell:
a: 60.43Å b: 60.43Å c: 252.77Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.22 0.219 0.275
Expression system: Escherichia coli

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Citations

12 review citations

Diversity of P450 enzymes in the biosynthesis of natural products.
Podust et al. (2012)
11 more

2 mentions without citation

Higher order organization of human placental aromatase.
Ghosh et al. (2011)
1 more