3tat

X-ray diffraction
3.5Å resolution

TYROSINE AMINOTRANSFERASE FROM E. COLI

Released:
Model geometry
Fit model/data
Data not deposited
Source organism: Escherichia coli
Primary publication:
Crystallization and preliminary crystallographic analysis of the Escherichia coli tyrosine aminotransferase.
Acta Crystallogr D Biol Crystallogr 55 1474-7 (1999)
PMID: 10417420

Function and Biology Details

Reactions catalysed:
(2S,3S)-3-methylphenylalanine + 2-oxoglutarate = (3S)-2-oxo-3-phenylbutanoate + L-glutamate
An aromatic amino acid + 2-oxoglutarate = an aromatic oxo acid + L-glutamate

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-138148 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aromatic-amino-acid aminotransferase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 397 amino acids
Theoretical weight: 43.58 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P04693 (Residues: 1-397; Coverage: 100%)
Gene names: JW4014, b4054, tyrB
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 6 x PLP
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P32
Unit cell:
a: 126.578Å b: 126.578Å c: 156.243Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.213 0.213 0.26
Expression system: Escherichia coli