› 3den

X-ray diffraction
2.2Å resolution

Function and Biology Details

Reaction catalysed: 
Pyruvate + L-aspartate-4-semialdehyde = (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate + H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141377 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
4-hydroxy-tetrahydrodipicolinate synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 292 amino acids
Theoretical weight: 31.46 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6L2 (Residues: 1-292; Coverage: 100%)
Gene names: JW2463, b2478, dapA
Sequence domains: Dihydrodipicolinate synthetase family
Structure domains: Aldolase class I

Ligands and Environments

3 bound ligands:
Ligand K 2 x K
Ligand GOL 3 x GOL
Ligand PO4 3 x PO4
1 modified residue:
Ligand KGC 2 x KGC

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P3121
Unit cell:
a: 121.196Å b: 121.196Å c: 110.565Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.186 0.183 0.241
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Molecular evolution of an oligomeric biocatalyst functioning in lysine biosynthesis.
Soares da Costa et al. (2018)
6 other articles

3 mentions without citation

Insight into de-regulation of amino acid feedback inhibition: a focus on structure analysis method.
Naz et al. (2023)
2 more