› 1ay4

X-ray diffraction
2.33Å resolution

Function and Biology Details

Reaction catalysed: 
An aromatic amino acid + 2-oxoglutarate = an aromatic oxo acid + 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-161156 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aromatic-amino-acid aminotransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 394 amino acids
Theoretical weight: 42.78 KDa
Source organism: Paracoccus denitrificans
Expression system: Escherichia coli
UniProt:
  • Canonical: P95468 (Residues: 1-394; Coverage: 100%)
Gene name: tyrB
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 2 x PLP
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P212121
Unit cell:
a: 123.72Å b: 123.06Å c: 55.16Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.175 0.237
Expression system: Escherichia coli

Quick links

Citations

8 review citations

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

6 mentions without citation

Structural Consideration of the Working Mechanism of Fold Type I Transaminases From Eubacteria: Overt and Covert Movement.
Kwon et al. (2019)
5 more