› 1ama

X-ray diffraction
2.3Å resolution

DOMAIN CLOSURE IN MITOCHONDRIAL ASPARTATE AMINOTRANSFERASE

Released:
DOI: 10.2210/pdb1ama/pdb
PDB entry 1ama coloured by chain, front view.
PDB entry 1ama coloured by chain, side view.
PDB entry 1ama coloured by chain, top view.
Source organism: Gallus gallus
Primary publication:
Domain closure in mitochondrial aspartate aminotransferase.
McPhalen CA, Vincent MG, Picot D, Jansonius JN, Lesk AM, Chothia C
J Mol Biol 227 197-213 (1992)
PMID: 1522585

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 domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132574 (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: 95%)
Gene name: GOT2
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2221
Unit cell:
a: 69.7Å b: 91.4Å c: 128.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.159 not available not available
Expression system: unidentified

Quick links

Citations

11 review citations

Pyridoxal phosphate enzymes: mechanistic, structural, and evolutionary considerations.
Eliot et al. (2004)
10 more

18 mentions without citation

Toward a resolution of the introns early/late debate: only phase zero introns are correlated with the structure of ancient proteins.
de Souza et al. (1998)
17 more