› 4a6r

X-ray diffraction
1.35Å resolution

Crystal structure of the omega transaminase from Chromobacterium violaceum in the apo form, crystallised from polyacrylic acid

Released:
DOI: 10.2210/pdb4a6r/pdb
PDB entry 4a6r coloured by chain, front view.
PDB entry 4a6r coloured by chain, side view.
PDB entry 4a6r coloured by chain, top view.
Source organism: Chromobacterium violaceum
Primary publication:
Crystal structures of the Chromobacterium violaceumω-transaminase reveal major structural rearrangements upon binding of coenzyme PLP.
Humble MS, Cassimjee KE, Håkansson M, Kimbung YR, Walse B, Abedi V, Federsel HJ, Berglund P, Logan DT
FEBS J 279 779-92 (2012)
PMID: 22268978

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-181841 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Putative 8-amino-7-oxononanoate synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 459 amino acids
Theoretical weight: 51.28 KDa
Source organism: Chromobacterium violaceum
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q7NWG4 (Residues: 1-459; Coverage: 100%)
Gene name: CV_2025
Sequence domains: Aminotransferase class-III
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand TA8 2 x TA8
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I911-2
Spacegroup: P1
Unit cell:
a: 58.59Å b: 61.87Å c: 63.54Å
α: 108.03° β: 87.31° γ: 105.16°
R-values:
R R work R free
0.135 0.134 0.163
Expression system: Escherichia coli BL21(DE3)

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Citations

4 review citations

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

8 mentions without citation

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