› 3uqn

X-ray diffraction
1.94Å resolution

Crystal structure of dihydrodipicolinate synthase from Acinetobacter baumannii complexed with Oxamic acid at 1.9 Angstrom resolution

Released:
DOI: 10.2210/pdb3uqn/pdb
PDB entry 3uqn coloured by chain, front view.
PDB entry 3uqn coloured by chain, side view.
PDB entry 3uqn coloured by chain, top view.
Source organism: Acinetobacter baumannii ATCC 19606 = CIP 70.34 = JCM 6841
Entry authors: Singh A, Kaushik S, Sinha M, Kaur P, 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 GOL 2 x GOL
Ligand OXM 2 x OXM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P21
Unit cell:
a: 51.374Å b: 122.637Å c: 52.332Å
α: 90° β: 115.46° γ: 90°
R-values:
R R work R free
0.18 0.179 0.198
Expression system: Escherichia coli

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