› 6dnb

X-ray diffraction
1.7Å resolution

Crystal structure of T110A:S256A mutant human Glutamate oxaloacetate transaminase 1 (GOT1)

Released:
DOI: 10.2210/pdb6dnb/pdb
PDB entry 6dnb coloured by chain, front view.
PDB entry 6dnb coloured by chain, side view.
PDB entry 6dnb coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Biochemical Characterization and Structure-Based Mutational Analysis Provide Insight into the Binding and Mechanism of Action of Novel Aspartate Aminotransferase Inhibitors.
Holt MC, Assar Z, Beheshti Zavareh R, Lin L, Anglin J, Mashadova O, Haldar D, Mullarky E, Kremer DM, Cantley LC, Kimmelman AC, Stein AJ, Lairson LL, Lyssiotis CA
Biochemistry 57 6604-6614 (2018)
PMID: 30365304

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:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147888 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aspartate aminotransferase, cytoplasmic Chain: A
Molecule details ›
Chain: A
Length: 411 amino acids
Theoretical weight: 46.05 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P17174 (Residues: 3-413; Coverage: 100%)
Gene name: GOT1
Sequence domains: Aminotransferase class I and II
Structure domains: Type I PLP-dependent aspartate aminotransferase-like (Major domain)

Ligands and Environments

3 bound ligands:
Ligand PG4 2 x PG4
Ligand GOL 3 x GOL
Ligand PO4 1 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P6522
Unit cell:
a: 84.085Å b: 84.085Å c: 210.128Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.181 0.179 0.229
Expression system: Escherichia coli

Quick links

Citations

3 review citations

The Diverse Functions of Non-Essential Amino Acids in Cancer.
Choi et al. (2019)
2 more

2 mentions without citation

Biochemical Characterization and Structure-Based Mutational Analysis Provide Insight into the Binding and Mechanism of Action of Novel Aspartate Aminotransferase Inhibitors.
Holt et al. (2018)
1 more