3flu

X-ray diffraction
2Å resolution

Crystal structure of dihydrodipicolinate synthase from the pathogen Neisseria meningitidis

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-191713 (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: 297 amino acids
Theoretical weight: 31.54 KDa
Source organism: Neisseria meningitidis serogroup B
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9JZR4 (Residues: 1-291; Coverage: 100%)
Gene names: NMB0929, dapA
Sequence domains: Dihydrodipicolinate synthetase family
Structure domains: Aldolase class I

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P212121
Unit cell:
a: 80.667Å b: 115.684Å c: 132.122Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.151 0.148 0.191
Expression system: Escherichia coli