› 1aat

X-ray diffraction
2.8Å resolution

OXOGLUTARATE-INDUCED CONFORMATIONAL CHANGES IN CYTOSOLIC ASPARTATE AMINOTRANSFERASE

Released:
DOI: 10.2210/pdb1aat/pdb
PDB entry 1aat coloured by chain, front view.
PDB entry 1aat coloured by chain, side view.
PDB entry 1aat coloured by chain, top view.
Source organism: Gallus gallus
Primary publication:
[Conformational changes in cytosol aspartate aminotransferase induced by oxoglutarate].
Malashkevich VN, Kochkina VM, Torchinskiĭ IuM, Arutiunian EG
Dokl Akad Nauk SSSR 267 1257-61 (1982)
PMID: 7151682

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 domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132572 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aspartate aminotransferase, cytoplasmic Chains: A, B
Molecule details ›
Chains: A, B
Length: 411 amino acids
Theoretical weight: 45.87 KDa
Source organism: Gallus gallus
Expression system: Not provided
UniProt:
  • Canonical: P00504 (Residues: 2-412; Coverage: 100%)
Gene name: GOT1
Sequence domains: Aminotransferase class I and II

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 62.7Å b: 118.1Å c: 124.5Å
α: 90° β: 90° γ: 90°
Expression system: Not provided

Quick links

Citations

1 citations in other articles

Structural Insights into a Novel Class of Aspartate Aminotransferase from Corynebacterium glutamicum.
Son et al. (2016)