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1A0H

THE X-RAY CRYSTAL STRUCTURE OF PPACK-MEIZOTHROMBIN DESF1: KRINGLE/THROMBIN AND CARBOHYDRATE/KRINGLE/THROMBIN INTERACTIONS AND LOCATION OF THE LINKER CHAIN

Summary for 1A0H
Entry DOI10.2210/pdb1a0h/pdb
Related PRD IDPRD_000020
DescriptorMEIZOTHROMBIN, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, D-phenylalanyl-N-[(2S,3S)-6-{[amino(iminio)methyl]amino}-1-chloro-2-hydroxyhexan-3-yl]-L-prolinamide, ... (5 entities in total)
Functional Keywordsserine protease, coagulation, thrombin, prothrombin, meizothrombin, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
Biological sourceBos taurus (cattle)
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Total number of polymer chains4
Total formula weight97038.29
Authors
Martin, P.D.,Malkowski, M.G.,Box, J.,Esmon, C.T.,Edwards, B.F.P. (deposition date: 1997-11-30, release date: 1998-06-17, Last modification date: 2024-11-13)
Primary citationMartin, P.D.,Malkowski, M.G.,Box, J.,Esmon, C.T.,Edwards, B.F.
New insights into the regulation of the blood clotting cascade derived from the X-ray crystal structure of bovine meizothrombin des F1 in complex with PPACK.
Structure, 5:1681-1693, 1997
Cited by
PubMed Abstract: The conversion of prothrombin to thrombin by factor Xa is the penultimate step in the blood clotting cascade. In vivo, where the conversion occurs primarily on activated platelets in association with factor Va and Ca2+ ions, meizothrombin is the major intermediate of the two step reaction. Meizothrombin rapidly loses the fragment 1 domain (F1) by autolysis to become meizothrombin des F1 (mzTBN-F1). The physiological properties of mzTBN-F1 differ dramatically from those of thrombin due to the presence of prothrombin fragment 2 (F2), which remains covalently attached to the activated thrombin domain in mzTBN-F1.
PubMed: 9438869
DOI: 10.1016/S0969-2126(97)00314-6
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.2 Å)
Structure validation

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건을2025-06-18부터공개중

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