› 2ay5

X-ray diffraction
2.4Å resolution

AROMATIC AMINO ACID AMINOTRANSFERASE WITH 3-INDOLEPROPIONIC ACID

Released:
DOI: 10.2210/pdb2ay5/pdb
PDB entry 2ay5 coloured by chain, front view.
PDB entry 2ay5 coloured by chain, side view.
PDB entry 2ay5 coloured by chain, top view.
Source organism: Paracoccus denitrificans
Primary publication:
The active site of Paracoccus denitrificans aromatic amino acid aminotransferase has contrary properties: flexibility and rigidity.
Okamoto A, Ishii S, Hirotsu K, Kagamiyama H
Biochemistry 38 1176-84 (1999)
PMID: 9930977

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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P212121
Unit cell:
a: 124Å b: 122.06Å c: 55.11Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.161 0.161 0.218
Expression system: Escherichia coli

Quick links

Citations

4 review citations

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

1 mention without citation

Structural Evidence of Active Site Adaptability towards Different Sized Substrates of Aromatic Amino Acid Aminotransferase from Psychrobacter Sp. B6.
Bujacz et al. (2021)