X-ray diffraction
2.2Å resolution

Crystal structure of Dihyrodipicolinate Synthase (dapA)

Primary publication:
Structure of dihydrodipicolinate synthase from Methanocaldococcus jannaschii.
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 65 1222-6 (2009)
PMID: 20054116

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:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
4-hydroxy-tetrahydrodipicolinate synthase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 289 amino acids
Theoretical weight: 31.61 KDa
Source organism: Methanocaldococcus jannaschii DSM 2661
Expression system: Escherichia coli
  • Canonical: Q57695 (Residues: 1-289; Coverage: 100%)
Gene names: MJ0244, dapA
Sequence domains: Dihydrodipicolinate synthetase family
Structure domains: Aldolase class I

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX10.1
Spacegroup: P21
Unit cell:
a: 80.469Å b: 76.532Å c: 101.863Å
α: 90° β: 106.87° γ: 90°
R R work R free
0.161 0.158 0.224
Expression system: Escherichia coli