› 3r5d

X-ray diffraction
1.8Å resolution

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:
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-124408 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 347 amino acids
Theoretical weight: 36.29 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli
UniProt:
  • Canonical: G3XD76 (Residues: 1-344; Coverage: 100%)
Gene names: PA3666, dapD
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I911-3
Spacegroup: P21
Unit cell:
a: 83.038Å b: 102.002Å c: 134.903Å
α: 90° β: 89.97° γ: 90°
R-values:
R R work R free
0.203 0.202 0.236
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Dissociative mechanism for irreversible thermal denaturation of oligomeric proteins.
Chebotareva et al. (2016)
1 more

3 mentions without citation

Bayesian Weighing of Electron Cryo-Microscopy Data for Integrative Structural Modeling.
Bonomi et al. (2019)
2 more