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Structure paper

TitleThe linker connecting the two kringles plays a key role in prothrombin activation.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 111, Page 7630-7635, Year 2014
Publish dateDec 12, 2013 (structure data deposition date)
AuthorsPozzi, N. / Chen, Z. / Pelc, L.A. / Shropshire, D.B. / Di Cera, E.
External linksProc. Natl. Acad. Sci. USA / PubMed:24821807
MethodsX-ray diffraction
Resolution2.807 - 3.38 Å
Structure data

PDB-4nzq:
Crystal structure of Ca2+-free prothrombin deletion mutant residues 146-167
Method: X-RAY DIFFRACTION / Resolution: 2.807 Å

PDB-4o03:
Crystal structure of Ca2+ bound prothrombin deletion mutant residues 146-167
Method: X-RAY DIFFRACTION / Resolution: 3.38 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-CA:
Unknown entry

Source
  • homo sapiens (human)
KeywordsHYDROLASE / PROTHROMBIN / KRINGLE / SERINE PROTEASE / COAGULATION

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