4dq6

X-ray diffraction
1.5Å resolution

Crystal structure of PLP-bound putative aminotransferase from Clostridium difficile 630

Released:
Source organism: Clostridioides difficile 630
Entry authors: Shabalin IG, Onopriyenko O, Kudritska M, Chruszcz M, Grimshaw S, Porebski PJ, Cooper DR, Savchenko A, Anderson WF, Minor W, Center for Structural Genomics of Infectious Diseases (CSGID)

Function and Biology Details

Reaction catalysed:
(1a) an L-cysteine-S-conjugate = a thiol + 2-aminoporp-2-enoate
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-172674 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
cysteine-S-conjugate beta-lyase Chains: A, B
Molecule details ›
Chains: A, B
Length: 391 amino acids
Theoretical weight: 45.09 KDa
Source organism: Clostridioides difficile 630
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q183G9 (Residues: 1-388; Coverage: 100%)
Gene name: CD630_27330
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 2 x PLP
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P21
Unit cell:
a: 79.426Å b: 56.094Å c: 85.275Å
α: 90° β: 99.33° γ: 90°
R-values:
R R work R free
0.154 0.152 0.186
Expression system: Escherichia coli BL21