6ckt

X-ray diffraction
1.8Å resolution

Crystal structure of 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase from Legionella pneumophila Philadelphia 1

Released:
Entry author: Seattle Structural Genomics Center for Infectious Disease (SSGCID)

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:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
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: 284 amino acids
Theoretical weight: 31.14 KDa
Source organism: Legionella pneumophila subsp. pneumophila str. Philadelphia 1
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
UniProt:
  • Canonical: Q5ZX45 (Residues: 1-276; Coverage: 100%)
Gene names: dapD, lpg0888
Sequence domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: R3
Unit cell:
a: 101.73Å b: 101.73Å c: 70.98Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.16 0.157 0.188
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'