› 1dhp

X-ray diffraction
2.3Å resolution

DIHYDRODIPICOLINATE SYNTHASE

Released:
DOI: 10.2210/pdb1dhp/pdb
PDB entry 1dhp coloured by chain, front view.
PDB entry 1dhp coloured by chain, side view.
PDB entry 1dhp coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The crystal structure of dihydrodipicolinate synthase from Escherichia coli at 2.5 A resolution.
Mirwaldt C, Korndörfer I, Huber R
J Mol Biol 246 227-39 (1995)
PMID: 7853400

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 domain:

Structure analysis Details

Assemblies composition:
homo tetramer
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141376 (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: 31.3 KDa
Source organism: Escherichia coli
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

1 bound ligand:
Ligand K 2 x K
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3121
Unit cell:
a: 122.41Å b: 122.41Å c: 111.22Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.197 0.197 not available
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Fucosyltransferases: structure/function studies.
de Vries et al. (2001)
7 more

18 mentions without citation

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