Function and Biology Details
Reaction catalysed:
1-phosphatidyl-1D-myo-inositol 3-phosphate + H(2)O = 1-phosphatidyl-1D-myo-inositol + phosphate
Biochemical function:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152282 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Phosphatidylinositol-3-phosphatase SAC1
Molecule details ›
Chain: X
Length: 623 amino acids
Theoretical weight: 71.21 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: SacI homology domain
Length: 623 amino acids
Theoretical weight: 71.21 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P32368 (Residues: 1-623; Coverage: 100%)
Sequence domains: SacI homology domain
Vacuolar protein sorting-associated protein 74
Molecule details ›
Chain: A
Length: 345 amino acids
Theoretical weight: 39.33 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Golgi phosphoprotein 3 (GPP34)
Structure domains: yeast vps74-n-term truncation variant domain like
Length: 345 amino acids
Theoretical weight: 39.33 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: Q06385 (Residues: 1-345; Coverage: 100%)
Sequence domains: Golgi phosphoprotein 3 (GPP34)
Structure domains: yeast vps74-n-term truncation variant domain like
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
APS BEAMLINE 24-ID-C
Spacegroup:
R3
Expression system: Escherichia coli BL21(DE3)
