PDBe 1hwk

X-ray diffraction
2.22Å resolution

COMPLEX OF THE CATALYTIC PORTION OF HUMAN HMG-COA REDUCTASE WITH ATORVASTATIN

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)
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: 74.596Å b: 172.724Å c: 80.008Å
α: 90° β: 117.73° γ: 90°
R-values:
R R work R free
0.212 0.212 0.235
Expression system: Escherichia coli