› 2hdb

X-ray diffraction
2.2Å resolution

HMG-CoA synthase from Enterococcus faecalis. Mutation alanine 110 to glycine

Released:
DOI: 10.2210/pdb2hdb/pdb
PDB entry 2hdb coloured by chain, front view.
PDB entry 2hdb coloured by chain, side view.
PDB entry 2hdb coloured by chain, top view.
Source organism: Enterococcus faecalis
Primary publication:
A structural limitation on enzyme activity: the case of HMG-CoA synthase.
Steussy CN, Robison AD, Tetrick AM, Knight JT, Rodwell VW, Stauffacher CV, Sutherlin AL
Biochemistry 45 14407-14 (2006)
PMID: 17128980

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + H(2)O + acetoacetyl-CoA = (S)-3-hydroxy-3-methylglutaryl-CoA + CoA
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190291 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hydroxymethylglutaryl-CoA synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 383 amino acids
Theoretical weight: 42.18 KDa
Source organism: Enterococcus faecalis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9FD71 (Residues: 1-383; Coverage: 100%)
Gene name: mvaS
Sequence domains:
Structure domains: Peroxisomal Thiolase; Chain A, domain 1

Ligands and Environments

2 bound ligands:
Ligand SO4 3 x SO4
Ligand MES 2 x MES
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-ID-B
Spacegroup: I222
Unit cell:
a: 105.31Å b: 109.69Å c: 141.85Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.192 0.221
Expression system: Escherichia coli

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Citations

4 review citations

Enzymes of the mevalonate pathway of isoprenoid biosynthesis.
Miziorko HM. (2011)
3 more