› 3ird

X-ray diffraction
2.23Å resolution

Structure of dihydrodipicolinate synthase from Clostridium botulinum

Released:
DOI: 10.2210/pdb3ird/pdb
PDB entry 3ird coloured by chain, front view.
PDB entry 3ird coloured by chain, side view.
PDB entry 3ird coloured by chain, top view.
Source organism: Clostridium botulinum A str. Hall
Entry authors: Dobson RCJ, Atkinson S, Perugini MA

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 tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-107631 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
4-hydroxy-tetrahydrodipicolinate synthase Chain: A
Molecule details ›
Chain: A
Length: 291 amino acids
Theoretical weight: 31.55 KDa
Source organism: Clostridium botulinum A str. Hall
Expression system: Escherichia coli
UniProt:
  • Canonical: A5I6N2 (Residues: 2-292; Coverage: 100%)
Gene names: CBO3152, dapA
Sequence domains: Dihydrodipicolinate synthetase family
Structure domains: Aldolase class I

Ligands and Environments

4 bound ligands:
Ligand MLT 1 x MLT
Ligand NA 1 x NA
Ligand CL 2 x CL
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P42212
Unit cell:
a: 92.81Å b: 92.81Å c: 60.35Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.142 0.135 0.209
Expression system: Escherichia coli

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