› 1ydo

X-ray diffraction
2.71Å resolution

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-128616 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hydroxymethylglutaryl-CoA lyase YngG Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 307 amino acids
Theoretical weight: 34.08 KDa
Source organism: Bacillus subtilis subsp. subtilis str. 168
Expression system: Escherichia coli
UniProt:
  • Canonical: O34873 (Residues: 1-299; Coverage: 100%)
Gene names: BSU18230, yngG
Sequence domains: HMGL-like
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
Ligand IOD 4 x IOD
1 modified residue:
Ligand MSE 28 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P21
Unit cell:
a: 62.693Å b: 104.666Å c: 97.445Å
α: 90° β: 107.43° γ: 90°
R-values:
R R work R free
0.263 0.263 0.303
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Functionally diverse biotin-dependent enzymes with oxaloacetate decarboxylase activity.
Lietzan et al. (2014)
1 more

3 mentions without citation

MDockPP: A hierarchical approach for protein-protein docking and its application to CAPRI rounds 15-19.
Huang et al. (2010)
2 more