PDBe 1ydn

X-ray diffraction
2.3Å resolution

Crystal Structure of the HMG-CoA Lyase from Brucella melitensis, Northeast Structural Genomics Target LR35.

Released:

Function and Biology Details

Reaction catalysed:
(S)-3-hydroxy-3-methylglutaryl-CoA = acetyl-CoA + acetoacetate
Biochemical function:
Biological process:
  • not assigned
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hydroxymethylglutaryl-CoA lyase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 295 amino acids
Theoretical weight: 31.64 KDa
Source organism: Brucella melitensis bv. 1 str. 16M
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8YEF2 (Residues: 1-287; Coverage: 100%)
Gene name: BMEI1926
Sequence domains: HMGL-like
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P21
Unit cell:
a: 82.272Å b: 86.399Å c: 87.683Å
α: 90° β: 118.7° γ: 90°
R-values:
R R work R free
0.275 0.271 0.304
Expression system: Escherichia coli