1w7n

X-ray diffraction
2.9Å resolution

Crystal structure of human kynurenine aminotransferase I in PMP form

Released:
Source organism: Homo sapiens
Primary publication:
Crystal structure of human kynurenine aminotransferase I.
J Biol Chem 279 50214-20 (2004)
PMID: 15364907

Function and Biology Details

Reactions catalysed:
L-glutamine + phenylpyruvate = 2-oxoglutaramate + L-phenylalanine
(1a) L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate
(1a) an L-cysteine-S-conjugate = a thiol + 2-aminoporp-2-enoate
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-172574 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Kynurenine--oxoglutarate transaminase 1 Chain: A
Molecule details ›
Chain: A
Length: 422 amino acids
Theoretical weight: 47.93 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q16773 (Residues: 1-422; Coverage: 100%)
Gene names: CCBL1, KYAT1
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments


Cofactor: Ligand PMP 1 x PMP
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P3221
Unit cell:
a: 145.461Å b: 145.461Å c: 67.087Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.172 0.171 0.22
Expression system: Spodoptera frugiperda