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:
Biological process:
Cellular component:
- not assigned
Sequence domains:
- LL-diaminopimelate aminotransferase/aminotransferase ALD1
- Aminotransferases, class-I, pyridoxal-phosphate-binding site
- Pyridoxal phosphate-dependent transferase, major domain
- Aminotransferase, class I/classII
- Pyridoxal phosphate-dependent transferase, small domain
- Pyridoxal phosphate-dependent transferase
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
LL-diaminopimelate aminotransferase (preferred)
PDBe Complex ID:
PDB-CPX-131406 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
LL-diaminopimelate aminotransferase
Molecule details ›
Chain: A
Length: 400 amino acids
Theoretical weight: 44.71 KDa
Source organism: Chlamydia trachomatis
Expression system: Escherichia coli
UniProt:
Sequence domains: Aminotransferase class I and II
Structure domains:
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%)
Sequence domains: Aminotransferase class I and II
Structure domains:
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
SSRL BEAMLINE BL9-2
Spacegroup:
I4122
Expression system: Escherichia coli
