› 1yaa

X-ray diffraction
2.05Å resolution

ASPARTATE AMINOTRANSFERASE FROM SACCHAROMYCES CEREVISIAE CYTOPLASM

Released:
DOI: 10.2210/pdb1yaa/pdb
PDB entry 1yaa coloured by chain, front view.
PDB entry 1yaa coloured by chain, side view.
PDB entry 1yaa coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Crystal structure of Saccharomyces cerevisiae cytosolic aspartate aminotransferase.
Jeffery CJ, Barry T, Doonan S, Petsko GA, Ringe D
Protein Sci 7 1380-7 (1998)
PMID: 9655342

Function and Biology Details

Reaction catalysed: 
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)
Assembly name:
PDBe Complex ID:
PDB-CPX-150007 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aspartate aminotransferase, cytoplasmic Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 412 amino acids
Theoretical weight: 45.36 KDa
Source organism: Saccharomyces cerevisiae
UniProt:
  • Canonical: P23542 (Residues: 2-412; Coverage: 98%)
Gene names: AAT2, ASP5, L1746, YLR027C
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 4 x PLP
1 bound ligand:
Ligand MAE 4 x MAE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P212121
Unit cell:
a: 130.31Å b: 134.63Å c: 98.75Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.231 0.231 0.299

Quick links

Citations

2 review citations

Structure, evolution and action of vitamin B6-dependent enzymes.
Jansonius JN. (1998)
1 more

5 mentions without citation

Searching the protein structure database for ligand-binding site similarities using CPASS v.2.
Powers et al. (2011)
4 more