› 3ivu

X-ray diffraction
2.72Å resolution

Homocitrate Synthase Lys4 bound to 2-OG

Released:
DOI: 10.2210/pdb3ivu/pdb
PDB entry 3ivu coloured by chain, front view.
PDB entry 3ivu coloured by chain, side view.
PDB entry 3ivu coloured by chain, top view.
Source organism: Schizosaccharomyces pombe
Primary publication:
Crystal structure and functional analysis of homocitrate synthase, an essential enzyme in lysine biosynthesis.
Bulfer SL, Scott EM, Couture JF, Pillus L, Trievel RC
J Biol Chem 284 35769-80 (2009)
PMID: 19776021

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + H(2)O + 2-oxoglutarate = (R)-2-hydroxybutane-1,2,4-tricarboxylate + CoA
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195413 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Homocitrate synthase, mitochondrial Chains: A, B
Molecule details ›
Chains: A, B
Length: 423 amino acids
Theoretical weight: 46.75 KDa
Source organism: Schizosaccharomyces pombe
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y823 (Residues: 1-418; Coverage: 100%)
Gene names: SPBC1105.02c, lys4
Sequence domains: HMGL-like
Structure domains: Aldolase class I

Ligands and Environments

3 bound ligands:
Ligand CO 2 x CO
Ligand NA 2 x NA
Ligand AKG 2 x AKG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P62
Unit cell:
a: 133.798Å b: 133.798Å c: 125.657Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.18 0.177 0.217
Expression system: Escherichia coli

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Citations

3 review citations

Biosynthesis of Nitrogenase Cofactors.
Burén et al. (2020)
2 more

2 mentions without citation

Crystal structure and functional analysis of homocitrate synthase, an essential enzyme in lysine biosynthesis.
Bulfer et al. (2009)
1 more