3oga

X-ray diffraction
1.75Å resolution

1.75 Angstrom resolution crystal structure of a putative NTP pyrophosphohydrolase (yfaO) from Salmonella typhimurium LT2

Released:
Entry authors: Halavaty AS, Minasov G, Shuvalova L, Winsor J, Dubrovska I, Peterson S, Anderson WF, Center for Structural Genomics of Infectious Diseases (CSGID)

Function and Biology Details

Reactions catalysed:
dCTP + H(2)O = dCMP + diphosphate
dUTP + H(2)O = dUMP + diphosphate
A nucleoside triphosphate + H(2)O = a nucleotide + diphosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-187301 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nucleoside triphosphatase NudI Chains: A, B
Molecule details ›
Chains: A, B
Length: 165 amino acids
Theoretical weight: 19.06 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8ZNF5 (Residues: 1-141; Coverage: 100%)
Gene names: STM2295, nudI
Sequence domains: NUDIX domain
Structure domains: Nucleoside Triphosphate Pyrophosphohydrolase

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P212121
Unit cell:
a: 41.589Å b: 81.104Å c: 110.075Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.186 0.218
Expression system: Escherichia coli BL21(DE3)