3fsl

X-ray diffraction
2.35Å resolution

Crystal structure of tyrosine aminotransferase tripple mutant (P181Q,R183G,A321K) from Escherichia coli at 2.35 A resolution

Released:
Source organism: Escherichia coli K-12
Entry authors: Malashkevich VN, Ng B, Kirsch JF

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: 43.57 KDa
Source organism: Escherichia coli K-12
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 PLR 6 x PLR
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7A
Spacegroup: P212121
Unit cell:
a: 98.88Å b: 119.16Å c: 242.89Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.215 0.213 0.26
Expression system: Escherichia coli