1hwl

X-ray diffraction
2.1Å resolution

COMPLEX OF THE CATALYTIC PORTION OF HUMAN HMG-COA REDUCTASE WITH ROSUVASTATIN (FORMALLY KNOWN AS ZD4522)

Released:
Source organism: Homo sapiens
Primary publication:
Structural mechanism for statin inhibition of HMG-CoA reductase.
Science 292 1160-4 (2001)
PMID: 11349148

Function and Biology Details

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-137325 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-hydroxy-3-methylglutaryl-coenzyme A reductase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 467 amino acids
Theoretical weight: 50.02 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P04035 (Residues: 426-888; Coverage: 52%)
Gene name: HMGCR
Sequence domains: Hydroxymethylglutaryl-coenzyme A reductase
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: P21
Unit cell:
a: 74.432Å b: 172.512Å c: 79.987Å
α: 90° β: 117.36° γ: 90°
R-values:
R R work R free
0.219 0.219 0.239
Expression system: Escherichia coli