3fcm

X-ray diffraction
2.2Å resolution

Crystal structure of a NUDIX hydrolase from Clostridium perfringens

Released:
Entry authors: Palani K, Burley SK, Swaninathan S, New York SGX Research Center for Structural Genomics (NYSGXRC)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-101666 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nudix hydrolase domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 197 amino acids
Theoretical weight: 23.36 KDa
Source organism: Clostridium perfringens ATCC 13124
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A0H2YP99 (Residues: 2-187; Coverage: 99%)
Gene name: CPF_0662
Sequence domains: NUDIX domain
Structure domains: Nucleoside Triphosphate Pyrophosphohydrolase

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P21212
Unit cell:
a: 80.395Å b: 132.459Å c: 41.361Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.253 0.229 0.28
Expression system: Escherichia coli