› 3pud

X-ray diffraction
2.8Å resolution

Crystal structure of Dhydrodipicolinate synthase from Acinetobacter baumannii at 2.8A resolution

Released:
DOI: 10.2210/pdb3pud/pdb
PDB entry 3pud coloured by chain, front view.
PDB entry 3pud coloured by chain, side view.
PDB entry 3pud coloured by chain, top view.
Source organism: Acinetobacter baumannii ATCC 19606 = CIP 70.34 = JCM 6841
Entry authors: Jithesh O, Yamini S, Kaur N, Gautam A, Tewari R, Kushwaha GS, Kaur P, Srinivasan A, Sharma S, Singh TP

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 analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-111945 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
4-hydroxy-tetrahydrodipicolinate synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 291 amino acids
Theoretical weight: 31.28 KDa
Source organism: Acinetobacter baumannii ATCC 19606 = CIP 70.34 = JCM 6841
Expression system: Escherichia coli
UniProt:
  • Canonical: D0CFC3 (Residues: 7-297; Coverage: 98%)
Gene names: HMPREF0010_03414, dapA
Sequence domains: Dihydrodipicolinate synthetase family
Structure domains: Aldolase class I

Ligands and Environments

2 bound ligands:
Ligand SO4 4 x SO4
Ligand GOL 5 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: R3
Unit cell:
a: 169.009Å b: 169.009Å c: 62.37Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.202 0.202 0.225
Expression system: Escherichia coli

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