› 5ax8

X-ray diffraction
2.99Å resolution

Recombinant expression, purification and preliminary crystallographic studies of the mature form of human mitochondrial aspartate aminotransferase

Released:
DOI: 10.2210/pdb5ax8/pdb
PDB entry 5ax8 coloured by chain, front view.
PDB entry 5ax8 coloured by chain, side view.
PDB entry 5ax8 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Recombinant expression, purification and crystallographic studies of the mature form of human mitochondrial aspartate aminotransferase.
Jiang X, Wang J, Chang H, Zhou Y
Biosci Trends 10 79-84 (2016)
PMID: 26902786

Function and Biology Details

Reactions catalysed: 
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
(1a) L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132573 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aspartate aminotransferase, mitochondrial Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 407 amino acids
Theoretical weight: 45.58 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00505 (Residues: 30-430; Coverage: 93%)
Gene names: GOT2, KYAT4
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: P1
Unit cell:
a: 56.706Å b: 76.14Å c: 94.247Å
α: 78° β: 85.65° γ: 78.41°
R-values:
R R work R free
0.274 0.273 0.291
Expression system: Escherichia coli

Quick links

Citations

1 review citation

The Synthesis of Kynurenic Acid in Mammals: An Updated Kynurenine Aminotransferase Structural KATalogue.
Rossi et al. (2019)
4 other articles

3 mentions without citation

Kynurenine Aminotransferase Isozyme Inhibitors: A Review.
Nematollahi et al. (2016)
2 more