PDBe 2rij

X-ray diffraction
1.9Å resolution

Crystal structure of a putative 2,3,4,5-tetrahydropyridine-2-carboxylate n-succinyltransferase (cj1605c, dapd) from campylobacter jejuni at 1.90 A resolution

Released:
Source organism: Campylobacter jejuni
Entry author: Joint Center for Structural Genomics (JCSG)

Function and Biology Details

Reaction catalysed:
Succinyl-CoA + (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + H(2)O = CoA + N-succinyl-L-2-amino-6-oxoheptanedioate. 
Biochemical function:
Cellular component:

Structure analysis Details

Assemblies composition:
homo hexamer
homo trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase Chain: A
Molecule details ›
Chain: A
Length: 387 amino acids
Theoretical weight: 42.89 KDa
Source organism: Campylobacter jejuni
Expression system: Escherichia coli
UniProt:
  • Canonical: Q0P823 (Residues: 1-386; Coverage: 100%)
Gene names: Cj1605c, dapD
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: R32
Unit cell:
a: 135.093Å b: 135.093Å c: 213.742Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.157 0.156 0.185
Expression system: Escherichia coli