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3tpi
From Proteopedia
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| - | [[Image:3tpi.png|left|200px]] | ||
| - | + | ==THE GEOMETRY OF THE REACTIVE SITE AND OF THE PEPTIDE GROUPS IN TRYPSIN, TRYPSINOGEN AND ITS COMPLEXES WITH INHIBITORS== | |
| - | + | <StructureSection load='3tpi' size='340' side='right' caption='[[3tpi]], [[Resolution|resolution]] 1.90Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3tpi]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1tpi 1tpi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TPI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TPI FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ILE:ISOLEUCINE'>ILE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=VAL:VALINE'>VAL</scene></td></tr> | |
| - | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3tpi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tpi OCA], [http://pdbe.org/3tpi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3tpi RCSB], [http://www.ebi.ac.uk/pdbsum/3tpi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3tpi ProSAT]</span></td></tr> |
| - | [[3tpi]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1tpi 1tpi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TPI OCA]. | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/BPT1_BOVIN BPT1_BOVIN]] Inhibits trypsin, kallikrein, chymotrypsin, and plasmin. | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tp/3tpi_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3tpi ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
==See Also== | ==See Also== | ||
*[[Basic Pancreatic Trypsin Inhibitor|Basic Pancreatic Trypsin Inhibitor]] | *[[Basic Pancreatic Trypsin Inhibitor|Basic Pancreatic Trypsin Inhibitor]] | ||
*[[Trypsin|Trypsin]] | *[[Trypsin|Trypsin]] | ||
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Trypsin]] | [[Category: Trypsin]] | ||
| - | [[Category: Bode, W | + | [[Category: Bode, W]] |
| - | [[Category: Deisenhofer, J | + | [[Category: Deisenhofer, J]] |
| - | [[Category: Huber, R | + | [[Category: Huber, R]] |
| - | [[Category: Schwager, P | + | [[Category: Schwager, P]] |
[[Category: Hydrolase-hydrolase inhibitor complex]] | [[Category: Hydrolase-hydrolase inhibitor complex]] | ||
Current revision
THE GEOMETRY OF THE REACTIVE SITE AND OF THE PEPTIDE GROUPS IN TRYPSIN, TRYPSINOGEN AND ITS COMPLEXES WITH INHIBITORS
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