2r2n

X-ray diffraction
1.95Å resolution

The crystal structure of human kynurenine aminotransferase II in complex with kynurenine

Released:
Source organism: Homo sapiens
Primary publication:
Crystal structure of human kynurenine aminotransferase II.
J Biol Chem 283 3567-3573 (2008)
PMID: 18056995

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, C, D
Molecule details ›
Chains: A, B, C, D
Length: 425 amino acids
Theoretical weight: 47.4 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8N5Z0 (Residues: 1-425; Coverage: 100%)
Gene names: AADAT, KAT2, KYAT2
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments


Cofactor: Ligand PMP 4 x PMP
2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P21
Unit cell:
a: 70.843Å b: 109.36Å c: 119.354Å
α: 90° β: 94.68° γ: 90°
R-values:
R R work R free
0.196 0.194 0.223
Expression system: Escherichia coli BL21(DE3)