3ii0

X-ray diffraction
2.05Å resolution

Crystal structure of human Glutamate oxaloacetate transaminase 1 (GOT1)

Released:
Source organism: Homo sapiens
Entry authors: Ugochukwu E, Pilka E, Cooper C, Bray JE, Yue WW, Muniz J, Chaikuad A, von Delft F, Bountra C, Arrowsmith CH, Weigelt J, Edwards A, Kavanagh KL, Oppermann U, Structural Genomics Consortium (SGC)

Function and Biology Details

Reactions catalysed:
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
L-cysteine + 2-oxoglutarate = 2-oxo-3-sulfanylpropanoate + L-glutamate
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
PDBe Complex ID:
PDB-CPX-147888 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aspartate aminotransferase, cytoplasmic Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 422 amino acids
Theoretical weight: 47.76 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P17174 (Residues: 14-412; Coverage: 97%)
Gene name: GOT1
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments


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

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P212121
Unit cell:
a: 78.531Å b: 107.347Å c: 239.997Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.18 0.223
Expression system: Escherichia coli