3wwh

X-ray diffraction
1.65Å resolution

Crystal structure of the first R-stereoselective -transaminase identified from Arthrobacter sp. KNK168 (FERM-BP-5228)

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-123675 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
(R)-amine transaminase Chain: A
Molecule details ›
Chain: A
Length: 330 amino acids
Theoretical weight: 36.45 KDa
Source organism: Arthrobacter sp. KNK168
Expression system: Escherichia coli
UniProt:
  • Canonical: F7J696 (Residues: 1-330; Coverage: 100%)
Gene name: TAS
Sequence domains: Amino-transferase class IV
Structure domains:

Ligands and Environments


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

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: P42212
Unit cell:
a: 80.62Å b: 80.62Å c: 93.88Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.154 0.153 0.172
Expression system: Escherichia coli