1tx7: Difference between revisions
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<StructureSection load='1tx7' size='340' side='right'caption='[[1tx7]], [[Resolution|resolution]] 1.75Å' scene=''> | <StructureSection load='1tx7' size='340' side='right'caption='[[1tx7]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1tx7]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1tx7]] is a 1 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=1TX7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TX7 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4CM:(4-CARBAMIMIDOYLPHENYL)-METHYL-PHOSPHINIC+ACID'>4CM</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4CM:(4-CARBAMIMIDOYLPHENYL)-METHYL-PHOSPHINIC+ACID'>4CM</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] </span></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=1tx7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tx7 OCA], [https://pdbe.org/1tx7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tx7 RCSB], [https://www.ebi.ac.uk/pdbsum/1tx7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tx7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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==See Also== | ==See Also== | ||
*[[Trypsin|Trypsin]] | *[[Trypsin 3D structures|Trypsin 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 16:17, 13 October 2021
Bovine Trypsin complexed with p-amidinophenylmethylphosphinic acid (AMPA)Bovine Trypsin complexed with p-amidinophenylmethylphosphinic acid (AMPA)
Structural highlights
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 PubMedp-amidinophenylmethylphosphinic acid (AMPA) was designed, synthesized and crystallized in complex with trypsin to study interactions with the oxyanion hole at the S1 site. In comparison to benzamidine, AMPA shows improved activity, which the crystal structure demonstrates to result from hydrogen bonds between the negatively charged phosphinic acid group and the catalytic residues at the oxyanion hole. An oxyanion-hole selective serine protease inhibitor in complex with trypsin.,Cui J, Marankan F, Fu W, Crich D, Mesecar A, Johnson ME Bioorg Med Chem. 2002 Jan;10(1):41-6. PMID:11738605[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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