PDBe 3wzf

X-ray diffraction
2.99Å resolution

Crystal structure of human cytoplasmic aspartate aminotransferase

Released:
Source organism: Homo sapiens
Entry authors: Jiang X, Chang H, Zhou Y, Chen L, Yang Q

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aspartate aminotransferase, cytoplasmic Chain: A
Molecule details ›
Chain: A
Length: 412 amino acids
Theoretical weight: 46.17 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P17174 (Residues: 2-413; Coverage: 100%)
Gene name: GOT1
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P43212
Unit cell:
a: 93.388Å b: 93.388Å c: 107.402Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.257 0.254 0.298
Expression system: Escherichia coli BL21(DE3)