› 7aut

X-ray diffraction
1.6Å resolution

Function and Biology Details

Reactions catalysed: 
Polyphosphate + n H(2)O = (n+1) oligophosphate
Diphospho-myo-inositol polyphosphate + H(2)O = myo-inositol polyphosphate + phosphate
P(1),P(5)-bis(5'-adenosyl)pentaphosphate + H(2)O = adenosine 5'-tetraphosphate + AMP
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189183 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Diphosphoinositol polyphosphate phosphohydrolase DDP1 Chain: A
Molecule details ›
Chain: A
Length: 191 amino acids
Theoretical weight: 21.75 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: Q99321 (Residues: 1-188; Coverage: 100%)
Gene names: DDP1, O3575, YOR163W
Sequence domains: NUDIX domain

Ligands and Environments

2 bound ligands:
Ligand MG 1 x MG
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALBA BEAMLINE XALOC
Spacegroup: P3221
Unit cell:
a: 61.785Å b: 61.785Å c: 96.184Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.192 0.191 0.211
Expression system: Escherichia coli

Quick links

Citations

7 citation in other articles

Cleavage-Polyadenylation Factor Cft1 and SPX Domain Proteins Are Agents of Inositol Pyrophosphate Toxicosis in Fission Yeast.
Schwer et al. (2022)
6 more

1 mention without citation

Multiple substrate recognition by yeast diadenosine and diphosphoinositol polyphosphate phosphohydrolase through phosphate clamping.
Márquez-Moñino et al. (2021)