1aka

X-ray diffraction
2.1Å resolution

STRUCTURAL BASIS FOR THE CATALYTIC ACTIVITY OF ASPARTATE AMINOTRANSFERASE K258H LACKING ITS PYRIDOXAL-5'-PHOSPHATE-BINDING LYSINE RESIDUE

Released:

Function and Biology Details

Reactions catalysed:
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
(1a) L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-132574 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aspartate aminotransferase, mitochondrial Chains: A, B
Molecule details ›
Chains: A, B
Length: 401 amino acids
Theoretical weight: 45 KDa
Source organism: Gallus gallus
Expression system: unidentified
UniProt:
  • Canonical: P00508 (Residues: 23-423; Coverage: 95%)
Gene name: GOT2
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 1 x PLP
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P1
Unit cell:
a: 55.87Å b: 58.8Å c: 75.81Å
α: 85.26° β: 108.96° γ: 115.57°
R-values:
R R work R free
0.169 not available not available
Expression system: unidentified