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Structure paper

TitleHow the Linker Connecting the Two Kringles Influences Activation and Conformational Plasticity of Prothrombin.
Journal, issue, pagesJ. Biol. Chem., Vol. 291, Page 6071-6082, Year 2016
Publish dateOct 21, 2015 (structure data deposition date)
AuthorsPozzi, N. / Chen, Z. / Di Cera, E.
External linksJ. Biol. Chem. / PubMed:26763231
MethodsX-ray diffraction
Resolution2.2 - 3.214 Å
Structure data

PDB-5edk:
Crystal structure of prothrombin deletion mutant residues 146-167 ( Form II ).
Method: X-RAY DIFFRACTION / Resolution: 3.214 Å

PDB-5edm:
Crystal structure of prothrombin deletion mutant residues 154-167 ( Form I )
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

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

ChemComp-MG:
Unknown entry

ChemComp-SO4:
SULFATE ION

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsHYDROLASE / prothrombin / kringle / Protease / coagulation factor / enzyme mechanism / kinetics / structure-function

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