3srt

X-ray diffraction
2.5Å resolution

The crystal structure of a maltose O-acetyltransferase from Clostridium difficile 630

Released:
Source organism: Clostridioides difficile 630
Entry authors: Tan K, Gu M, Peterson S, Anderson WF, Joachimiak A, Center for Structural Genomics of Infectious Diseases (CSGID)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 188 amino acids
Theoretical weight: 21.15 KDa
Source organism: Clostridioides difficile 630
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q18A66 (Residues: 1-185; Coverage: 100%)
Gene names: CD630_08720, maa
Sequence domains:
Structure domains: Hexapeptide repeat proteins

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P213
Unit cell:
a: 152.884Å b: 152.884Å c: 152.884Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.165 0.164 0.186
Expression system: Escherichia coli BL21(DE3)