3si9

X-ray diffraction
2.1Å resolution

Crystal structure of Dihydrodipicolinate Synthase from Bartonella Henselae

Released:

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:
Cellular component:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-179648 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
4-hydroxy-tetrahydrodipicolinate synthase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 315 amino acids
Theoretical weight: 33.81 KDa
Source organism: Bartonella henselae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q6G468 (Residues: 1-294; Coverage: 100%)
Gene names: BH05000, dapA
Sequence domains: Dihydrodipicolinate synthetase family
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: P212121
Unit cell:
a: 79.963Å b: 106.334Å c: 136.253Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.183 0.233
Expression system: Escherichia coli BL21(DE3)