3hij

X-ray diffraction
2.15Å resolution

Crystal structure of dihydrodipicolinate synthase from Bacillus anthracis in complex with its substrate, pyruvate

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-105681 (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: 292 amino acids
Theoretical weight: 31.33 KDa
Source organism: Bacillus anthracis
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A6L7H340 (Residues: 1-292; Coverage: 100%)
Gene names: GBAA_3935, dapA, dapA2
Sequence domains: Dihydrodipicolinate synthetase family
Structure domains: Aldolase class I

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX1
Spacegroup: P212121
Unit cell:
a: 84.484Å b: 124.617Å c: 130.979Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.155 0.153 0.21
Expression system: Escherichia coli