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Structure paper

TitleStructural basis for interdomain communication in SHIP2 providing high phosphatase activity.
Journal, issue, pagesElife, Vol. 6, Year 2017
Publish dateJul 25, 2017 (structure data deposition date)
AuthorsLe Coq, J. / Camacho-Artacho, M. / Velazquez, J.V. / Santiveri, C.M. / Gallego, L.H. / Campos-Olivas, R. / Dolker, N. / Lietha, D.
External linksElife / PubMed:28792888
MethodsX-ray diffraction
Resolution1.85 - 2.65 Å
Structure data

PDB-5okm:
Crystal structure of human SHIP2 Phosphatase-C2
Method: X-RAY DIFFRACTION / Resolution: 1.96 Å

PDB-5okn:
Crystal structure of human SHIP2 Phosphatase-C2 D607A mutant
Method: X-RAY DIFFRACTION / Resolution: 2.65 Å

PDB-5oko:
Crystal structure of human SHIP2 Phosphatase-C2 double mutant F593D/L597D
Method: X-RAY DIFFRACTION / Resolution: 1.94 Å

PDB-5okp:
Crystal structure of human SHIP2 Phosphatase-C2 double mutant F593D/L597D
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

Chemicals

ChemComp-B3P:
2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH buffer*YM

ChemComp-NO3:
NITRATE ION

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HOH:
WATER

ChemComp-PO4:
PHOSPHATE ION

ChemComp-MG:
Unknown entry

Source
  • homo sapiens (human)
KeywordsHYDROLASE / SHIP2 / Phosphatase / C2 / phosphatidylinositol (3 / 4 / 5)-triphosphate

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