› 1maq

X-ray diffraction
2.3Å resolution

CRYSTAL STRUCTURES OF TRUE ENZYMATIC REACTION INTERMEDIATES: ASPARTATE AND GLUTAMATE KETIMINES IN ASPARTATE AMINOTRANSFERASE

Released:
DOI: 10.2210/pdb1maq/pdb
PDB 1maq coloured by chain and viewed from the front.
PDB 1maq coloured by chain and viewed from the side.
PDB 1maq coloured by chain and viewed from the top.
Source organism: Gallus gallus
Primary publication:
Crystal structures of true enzymatic reaction intermediates: aspartate and glutamate ketimines in aspartate aminotransferase.
Malashkevich VN, Toney MD, Jansonius JN
Biochemistry 32 13451-62 (1993)
PMID: 7903048

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aspartate aminotransferase, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 401 amino acids
Theoretical weight: 44.99 KDa
Source organism: Gallus gallus
Expression system: unidentified
UniProt:
  • Canonical: P00508 (Residues: 23-423; Coverage: null%)
Gene name: GOT2
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand PGU 1 x PGU
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2221
Unit cell:
a: 70Å b: 92.1Å c: 128.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.169 not available not available
Expression system: unidentified

Quick links

Citations

5 review citations

Ornithine Aminotransferase, an Important Glutamate-Metabolizing Enzyme at the Crossroads of Multiple Metabolic Pathways.
Ginguay et al. (2017)
4 more

3 mentions without citation

PLP-dependent H(2)S biogenesis.
Singh et al. (2011)
2 more