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Structure paper

TitleStructural mechanisms of inactivation in scabies mite serine protease paralogues.
Journal, issue, pagesJ. Mol. Biol., Vol. 390, Page 635-645, Year 2009
Publish dateApr 28, 2009 (structure data deposition date)
AuthorsFischer, K. / Langendorf, C.G. / Irving, J.A. / Reynolds, S. / Willis, C. / Beckham, S. / Law, R.H. / Yang, S. / Bashtannyk-Puhalovich, T.A. / McGowan, S. ...Fischer, K. / Langendorf, C.G. / Irving, J.A. / Reynolds, S. / Willis, C. / Beckham, S. / Law, R.H. / Yang, S. / Bashtannyk-Puhalovich, T.A. / McGowan, S. / Whisstock, J.C. / Pike, R.N. / Kemp, D.J. / Buckle, A.M.
External linksJ. Mol. Biol. / PubMed:19427318
MethodsX-ray diffraction
Resolution1.85 - 2 Å
Structure data

PDB-3h7o:
Crystal structure of scabies mite inactivated protease paralogue S-I1 (SMIPP-S-I1)
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

PDB-3h7t:
Crystal structure of scabies mite inactivated protease paralogue S-D1 (SMIPP-S-D1)
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-ZN:
Unknown entry

Source
  • sarcoptes scabiei type hominis (arthropod)
KeywordsHYDROLASE

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