2hex: Difference between revisions
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<StructureSection load='2hex' size='340' side='right'caption='[[2hex]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='2hex' size='340' side='right'caption='[[2hex]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2hex]] is a 5 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2hex]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HEX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HEX FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2hex FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hex OCA], [https://pdbe.org/2hex PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hex RCSB], [https://www.ebi.ac.uk/pdbsum/2hex PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hex ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/BPT1_BOVIN BPT1_BOVIN]] Inhibits trypsin, kallikrein, chymotrypsin, and plasmin. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 14:08, 5 January 2022
DECAMERS OBSERVED IN THE CRYSTALS OF BOVINE PANCREATIC TRYPSIN INHIBITORDECAMERS OBSERVED IN THE CRYSTALS OF BOVINE PANCREATIC TRYPSIN INHIBITOR
Structural highlights
Function[BPT1_BOVIN] Inhibits trypsin, kallikrein, chymotrypsin, and plasmin. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe structure of bovine pancreatic trypsin inhibitor (BPTI) has been solved at 2.1 A resolution in a new crystal form (space group P6422 with unit-cell dimensions a = b = 95.0, c = 158.1 A). The asymmetric unit is a pentamer, but a decamer is created by application of crystallographic symmetry. The decamer of BPTI is only the fourth such assembly reported to date in the Protein Data Bank. Decamers observed in the crystals of bovine pancreatic trypsin inhibitor.,Lubkowski J, Wlodawer A Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):335-7. Epub 1999, Jan 1. PMID:10089443[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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