3asa

X-ray diffraction
2.05Å resolution

Crystal structure of apo-LL-diaminopimelate aminotransferase from Chlamydia trachomatis

Released:

Function and Biology Details

Reaction catalysed:
LL-2,6-diaminoheptanedioate + 2-oxoglutarate = (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + L-glutamate + H(2)O
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
LL-diaminopimelate aminotransferase Chain: A
Molecule details ›
Chain: A
Length: 400 amino acids
Theoretical weight: 44.71 KDa
Source organism: Chlamydia trachomatis
Expression system: Escherichia coli
UniProt:
  • Canonical: O84395 (Residues: 1-394; Coverage: 100%)
Gene names: CT_390, aspC, dapL
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: I4122
Unit cell:
a: 110.246Å b: 110.246Å c: 205.626Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.229 0.226 0.277
Expression system: Escherichia coli