3dsb

X-ray diffraction
1.48Å resolution

The crystal structure of a possible acetyltransferase from Clostridium difficile 630

Released:
Source organism: Clostridioides difficile 630
Entry authors: Tan K, Shackelford G, Joachimiak A, Midwest Center for Structural Genomics (MCSG)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-acetyltransferase domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 157 amino acids
Theoretical weight: 19.18 KDa
Source organism: Clostridioides difficile 630
Expression system: Escherichia coli
UniProt:
  • Canonical: Q185U9 (Residues: 14-167; Coverage: 92%)
Gene name: CD630_21620
Sequence domains: Acetyltransferase (GNAT) family
Structure domains: Aminopeptidase

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 41.488Å b: 66.765Å c: 133.884Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.17 0.168 0.205
Expression system: Escherichia coli