› 2ykv

X-ray diffraction
1.9Å resolution

Structural Determinants of the Beta-Selectivity of a Bacterial Aminotransferase

Released:
DOI: 10.2210/pdb2ykv/pdb
PDB entry 2ykv coloured by chain, front view.
PDB entry 2ykv coloured by chain, side view.
PDB entry 2ykv coloured by chain, top view.
Source organism: Mesorhizobium sp. LUK
Primary publication:
Structural determinants of the β-selectivity of a bacterial aminotransferase.
Wybenga GG, Crismaru CG, Janssen DB, Dijkstra BW
J Biol Chem 287 28495-502 (2012)
PMID: 22745123

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-107110 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-transaminase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 465 amino acids
Theoretical weight: 49.59 KDa
Source organism: Mesorhizobium sp. LUK
Expression system: Escherichia coli
UniProt:
  • Canonical: A3EYF7 (Residues: 1-445; Coverage: 100%)
Sequence domains: Aminotransferase class-III
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand IK2 3 x IK2
Ligand EDO 20 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: C2
Unit cell:
a: 183.582Å b: 94.321Å c: 102.307Å
α: 90° β: 113.99° γ: 90°
R-values:
R R work R free
0.177 0.176 0.206
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Recent achievements in developing the biocatalytic toolbox for chiral amine synthesis.
Kohls et al. (2014)
2 more

5 mentions without citation

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