3ppl

X-ray diffraction
1.25Å resolution

Crystal structure of an aspartate transaminase (NCgl0237, Cgl0240) from CORYNEBACTERIUM GLUTAMICUM ATCC 13032 KITASATO at 1.25 A resolution

Released:
Entry author: Joint Center for Structural Genomics (JCSG)

Function and Biology Details

Reaction catalysed:
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-185672 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aspartate aminotransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 427 amino acids
Theoretical weight: 47.04 KDa
Source organism: Corynebacterium glutamicum ATCC 13032
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8NTR2 (Residues: 7-432; Coverage: 99%)
Gene name: Cgl0240
Sequence domains: Aspartate amino-transferase
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 2 x PLP
2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: C2
Unit cell:
a: 97.755Å b: 54.424Å c: 176.34Å
α: 90° β: 101.6° γ: 90°
R-values:
R R work R free
0.106 0.105 0.124
Expression system: Escherichia coli