› 3jus

X-ray diffraction
2.9Å resolution

Crystal structure of human lanosterol 14alpha-demethylase (CYP51) in complex with econazole

Released:
DOI: 10.2210/pdb3jus/pdb
PDB entry 3jus coloured by chain, front view.
PDB entry 3jus coloured by chain, side view.
PDB entry 3jus coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis of human CYP51 inhibition by antifungal azoles.
Strushkevich N, Usanov SA, Park HW
J Mol Biol 397 1067-78 (2010)
PMID: 20149798

Function and Biology Details

Reaction catalysed: 
(1a) a 14-alpha-methylsteroid + [reduced NADPH--hemoprotein reductase] + O(2) = a 14-alpha-hydroxysteroid + [oxidized NADPH--hemoprotein reductase] + H(2)O
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172598 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Lanosterol 14-alpha demethylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 461 amino acids
Theoretical weight: 52.77 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q16850 (Residues: 60-508; Coverage: 88%)
Gene names: CYP51, CYP51A1
Sequence domains: Cytochrome P450
Structure domains: Cytochrome P450

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
3 bound ligands:
Ligand ECL 2 x ECL
Ligand HEM 2 x HEM
Ligand ECN 2 x ECN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P4212
Unit cell:
a: 146.626Å b: 146.626Å c: 110.56Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.203 0.272
Expression system: Escherichia coli

Quick links

Citations

18 review citations

Biosynthesis of cholesterol and other sterols.
Nes WD. (2011)
17 more

17 mentions without citation

Biochemical and physiological importance of the CYP26 retinoic acid hydroxylases.
Isoherranen et al. (2019)
16 more