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TitlePeptide length and leaving-group sterics influence potency of Peptide phosphonate protease inhibitors.
Journal, issue, pagesChem. Biol., Vol. 18, Page 48-57, Year 2011
Publish dateJun 4, 2010 (structure data deposition date)
AuthorsBrown, C.M. / Ray, M. / Eroy-Reveles, A.A. / Egea, P. / Tajon, C. / Craik, C.S.
External linksChem. Biol. / PubMed:21276938
MethodsX-ray diffraction
Resolution1.19 Å
Structure data

PDB-3ncl:
Crystal Structure of MT-SP1 bound to Benzamidine Phosphonate Inhibitor
Method: X-RAY DIFFRACTION / Resolution: 1.19 Å

Chemicals

ChemComp-CCZ:
phenyl (4-carbamimidoylbenzyl)phosphonate

ChemComp-FMT:
FORMIC ACID

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsHYDROLASE / proteinase-inhibitor complex / serine proteinase / benzamidine / phosphonate / serine endopeptidases

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