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Structure paper

TitleUnexpected crucial role of residue 225 in serine proteases.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 96, Page 1852-1857, Year 1999
Publish dateJan 25, 1999 (structure data deposition date)
AuthorsGuinto, E.R. / Caccia, S. / Rose, T. / Futterer, K. / Waksman, G. / Di Cera, E.
External linksProc. Natl. Acad. Sci. USA / PubMed:10051558
MethodsX-ray diffraction
Resolution2.1 Å
Structure data

PDB-1b7x:
STRUCTURE OF HUMAN ALPHA-THROMBIN Y225I MUTANT BOUND TO D-PHE-PRO-ARG-CHLOROMETHYLKETONE
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-1thp:
STRUCTURE OF HUMAN ALPHA-THROMBIN Y225P MUTANT BOUND TO D-PHE-PRO-ARG-CHLOROMETHYLKETONE
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-2thf:
STRUCTURE OF HUMAN ALPHA-THROMBIN Y225F MUTANT BOUND TO D-PHE-PRO-ARG-CHLOROMETHYLKETONE
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-0G6:
D-phenylalanyl-N-[(2S,3S)-6-{[amino(iminio)methyl]amino}-1-chloro-2-hydroxyhexan-3-yl]-L-prolinamide

ChemComp-NA:
Unknown entry

Source
  • homo sapiens (human)
KeywordsHYDROLASE/HYDROLASE INHIBITOR / SERINE PROTEASE / HYDROLASE-HYDROLASE INHIBITOR COMPLEX / FPRCK

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