› 1qgx

X-ray diffraction
1.6Å resolution

Function and Biology Details

Reaction catalysed: 
Adenosine 3',5'-bisphosphate + H(2)O = adenosine 5'-phosphate + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152225 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3'(2'),5'-bisphosphate nucleotidase Chain: A
Molecule details ›
Chain: A
Length: 357 amino acids
Theoretical weight: 39.2 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: P32179 (Residues: 1-357; Coverage: 100%)
Gene names: HAL2, MET22, YOL064C
Sequence domains: Inositol monophosphatase family
Structure domains:

Ligands and Environments

5 bound ligands:
Ligand MG 2 x MG
Ligand PO4 1 x PO4
Ligand SO4 1 x SO4
Ligand AMP 1 x AMP
Ligand BME 1 x BME
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 54.68Å b: 44.91Å c: 71.6Å
α: 90° β: 111.08° γ: 90°
R-values:
R R work R free
0.197 0.197 0.235
Expression system: Saccharomyces cerevisiae

Quick links

Citations

4 review citations

Molecular targets of lithium action.
Phiel et al. (2001)
3 more

5 mentions without citation

Overview of protein structural and functional folds.
Sun et al. (2004)
4 more