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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1azz|1azz]], [[1ecy|1ecy]], [[1fi8|1fi8]], [[1id5|1id5]], [[1ifg|1ifg]], [[1slu|1slu]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1azz|1azz]], [[1ecy|1ecy]], [[1fi8|1fi8]], [[1id5|1id5]], [[1ifg|1ifg]], [[1slu|1slu]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Chymotrypsin Chymotrypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.1 3.4.21.1] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Chymotrypsin Chymotrypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.1 3.4.21.1] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n8o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n8o OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1n8o RCSB], [http://www.ebi.ac.uk/pdbsum/1n8o PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n8o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n8o OCA], [http://pdbe.org/1n8o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1n8o RCSB], [http://www.ebi.ac.uk/pdbsum/1n8o PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
Revision as of 17:20, 10 September 2015
Crystal structure of a complex between bovine chymotrypsin and ecotinCrystal structure of a complex between bovine chymotrypsin and ecotin
Structural highlights
Function[ECOT_ECOLI] General inhibitor of pancreatic serine proteases: inhibits chymotrypsin, trypsin, elastases, factor X, kallikrein as well as a variety of other proteases. The strength of inhibition does not appear to be correlated with a particular protease specificity.[HAMAP-Rule:MF_00706] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also |
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