PDBe 1dq8

X-ray diffraction
2.1Å resolution

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

Released:

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: 425-888; Coverage: 52%)
Gene name: HMGCR
Sequence domains: Hydroxymethylglutaryl-coenzyme A reductase
Structure domains:

Ligands and Environments


Cofactor: Ligand COA 4 x COA
2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12B
Spacegroup: P21
Unit cell:
a: 75.297Å b: 130.182Å c: 92.547Å
α: 90° β: 106.48° γ: 90°
R-values:
R R work R free
0.199 0.199 0.239
Expression system: Escherichia coli