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TitleMutation of surface residues to promote crystallization of activated factor XI as a complex with benzamidine: an essential step for the iterative structure-based design of factor XI inhibitors.
Journal, issue, pagesActa Crystallogr. ,Sect. D, Vol. 61, Page 1418-1425, Year 2005
Publish dateApr 26, 2005 (structure data deposition date)
AuthorsJin, L. / Pandey, P. / Babine, R.E. / Weaver, D.T. / Abdel-Meguid, S.S. / Strickler, J.E.
External linksActa Crystallogr. ,Sect. D / PubMed:16204896
MethodsX-ray diffraction
Resolution1.73 - 2.7 Å
Structure data

PDB-1zhm:
Crystal Structure of the Catalytic Domain of the Coagulation Factor XIa in Complex with Benzamidine (S434A-T475A-K437 Mutant)
Method: X-RAY DIFFRACTION / Resolution: 1.96 Å

PDB-1zhp:
Crystal Structure of the Catalytic Domain of Coagulation Factor XI in Complex with Benzamidine (S434A-T475A-K505 Mutant)
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

PDB-1zhr:
Crystal Structure of the Catalytic Domain of Coagulation Factor XI in Complex with Benzamidine (S434A-T475A-C482S-K437A Mutant)
Method: X-RAY DIFFRACTION / Resolution: 1.73 Å

Chemicals

ChemComp-BEN:
BENZAMIDINE

ChemComp-GSH:
GLUTATHIONE

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsHYDROLASE / BLOOD CLOTTING / Factor XI; benzamidine

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