› 3mp3

X-ray diffraction
2.4Å resolution

Crystal Structure of Human Lyase in complex with inhibitor HG-CoA

Released:
DOI: 10.2210/pdb3mp3/pdb
PDB entry 3mp3 coloured by chain, front view.
PDB entry 3mp3 coloured by chain, side view.
PDB entry 3mp3 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Functional insights into human HMG-CoA lyase from structures of Acyl-CoA-containing ternary complexes.
Fu Z, Runquist JA, Montgomery C, Miziorko HM, Kim JJ
J Biol Chem 285 26341-9 (2010)
PMID: 20558737

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153052 (preferred)
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

3 bound ligands:
Ligand 3HG 1 x 3HG
Ligand MG 6 x MG
Ligand HGG 1 x HGG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: C2
Unit cell:
a: 197.37Å b: 117Å c: 86.87Å
α: 90° β: 112.31° γ: 90°
R-values:
R R work R free
0.212 0.212 0.281
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Enzymes of the mevalonate pathway of isoprenoid biosynthesis.
Miziorko HM. (2011)
11 other articles

1 mention without citation

Functional insights into human HMG-CoA lyase from structures of Acyl-CoA-containing ternary complexes.
Fu et al. (2010)