PDBe 2cw6

X-ray diffraction
2.1Å resolution

Crystal Structure of Human HMG-CoA Lyase: Insights into Catalysis and the Molecular Basis for Hydroxymethylglutaric Aciduria

Released:

Function and Biology Details

Reaction catalysed:
(S)-3-hydroxy-3-methylglutaryl-CoA = acetyl-CoA + acetoacetate
Biological process:
Cellular component:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo 12-mer
homo hexamer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hydroxymethylglutaryl-CoA lyase, mitochondrial Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 298 amino acids
Theoretical weight: 31.58 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P35914 (Residues: 28-325; Coverage: 92%)
Gene name: HMGCL
Sequence domains: HMGL-like
Structure domains: Aldolase class I

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: C2
Unit cell:
a: 196.99Å b: 117.08Å c: 86.83Å
α: 90° β: 112.5° γ: 90°
R-values:
R R work R free
0.226 0.226 0.265
Expression system: Escherichia coli