2vgz

X-ray diffraction
2.3Å resolution

CRYSTAL STRUCTURE OF HUMAN KYNURENINE AMINOTRANSFERASE II

Released:

Function and Biology Details

Reactions catalysed:
L-2-aminoadipate + 2-oxoglutarate = 2-oxoadipate + L-glutamate
Glycine + 2-oxoglutarate = glyoxylate + L-glutamate
(1a) L-kynurenine + glyoxylate = 4-(2-aminophenyl)-2,4-dioxobutanoate + glycine 
(1a) L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate
L-methionine + glyoxylate = 4-methylthio-2-oxobutanoate + glycine
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-185410 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial Chains: A, B
Molecule details ›
Chains: A, B
Length: 427 amino acids
Theoretical weight: 47.64 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8N5Z0 (Residues: 2-425; Coverage: 100%)
Gene names: AADAT, KAT2, KYAT2
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 2 x PLP
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P21212
Unit cell:
a: 99.631Å b: 154.956Å c: 61.201Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.182 0.243
Expression system: Escherichia coli BL21(DE3)