› 2xfh

X-ray diffraction
1.9Å resolution

Structure of cytochrome P450 EryK cocrystallized with inhibitor clotrimazole.

Released:
DOI: 10.2210/pdb2xfh/pdb
PDB entry 2xfh coloured by chain, front view.
PDB entry 2xfh coloured by chain, side view.
PDB entry 2xfh coloured by chain, top view.
Source organism: Saccharopolyspora erythraea
Primary publication:
Azole drugs trap cytochrome P450 EryK in alternative conformational states.
Montemiglio LC, Gianni S, Vallone B, Savino C
Biochemistry 49 9199-206 (2010)
PMID: 20845962

Function and Biology Details

Reaction catalysed: 
Erythromycin D + NADPH + O(2) = erythromycin C + NADP(+) + H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155783 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Erythromycin C-12 hydroxylase Chain: A
Molecule details ›
Chain: A
Length: 411 amino acids
Theoretical weight: 45.35 KDa
Source organism: Saccharopolyspora erythraea
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P48635 (Residues: 2-397; Coverage: 100%)
Gene names: CYP113A1, SACE_0713, eryK
Sequence domains: Cytochrome P450
Structure domains: Cytochrome P450

Ligands and Environments


Cofactor: Ligand HEM 1 x HEM
2 bound ligands:
Ligand CL6 2 x CL6
Ligand DMS 1 x DMS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P1
Unit cell:
a: 37.92Å b: 53.68Å c: 58.109Å
α: 100.27° β: 90.93° γ: 94.19°
R-values:
R R work R free
0.184 0.181 0.231
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Challenges in assignment of allosteric effects in cytochrome P450-catalyzed substrate oxidations to structural dynamics in the hemoprotein architecture.
Hlavica P. (2017)
8 other articles

6 mentions without citation

Molecular Insights into Coumarin Analogues as Antimicrobial Agents: Recent Developments in Drug Discovery.
Cheke et al. (2022)
5 more