1jqp: Difference between revisions

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 <StructureSection load='1jqp' size='340' side='right'caption='[[1jqp]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1jqp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JQP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JQP FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1jqp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JQP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JQP FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Dipeptidyl-peptidase_I Dipeptidyl-peptidase I], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.14.1 3.4.14.1] </span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <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'>[https://proteopedia.org/fgij/fg.htm?mol=1jqp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jqp OCA], [https://pdbe.org/1jqp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jqp RCSB], [https://www.ebi.ac.uk/pdbsum/1jqp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jqp ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/CATC_RAT CATC_RAT]] Thiol protease. Has dipeptidylpeptidase activity. Can act as both an exopeptidase and endopeptidase (By similarity).
+[https://www.uniprot.org/uniprot/CATC_RAT CATC_RAT] Thiol protease. Has dipeptidylpeptidase activity. Can act as both an exopeptidase and endopeptidase (By similarity).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 </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=1jqp ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The crystal structure of mature dipeptidyl peptidase I reveals insight into the unique tetrameric structure, substrate binding and activation of this atypical papain family peptidase. Each subunit is composed of three peptides. The heavy and light chains form the catalytic domain, which adopts the papain fold. The residual pro-part forms a beta-barrel with the carboxylate group of Asp1 pointing towards the substrate amino-terminus. The tetrameric structure appears to stabilize the association of the two domains and encloses a 12700 A3 spherical cavity. The tetramer contains six chloride ions, one buried in each S2 pocket and two at subunit interfaces.
-Tetrameric dipeptidyl peptidase I directs substrate specificity by use of the residual pro-part domain.,Olsen JG, Kadziola A, Lauritzen C, Pedersen J, Larsen S, Dahl SW FEBS Lett. 2001 Oct 12;506(3):201-6. PMID:11602245<ref>PMID:11602245</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1jqp" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Cathepsin 3D structures|Cathepsin 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Buffalo rat]]
-[[Category: Dipeptidyl-peptidase I]]
 [[Category: Large Structures]]
-[[Category: Dahl, S W]]
+[[Category: Rattus norvegicus]]
-[[Category: Kadziola, A]]
+[[Category: Dahl SW]]
-[[Category: Larsen, S]]
+[[Category: Kadziola A]]
-[[Category: Lauritzen, C]]
+[[Category: Larsen S]]
-[[Category: Olsen, J G]]
+[[Category: Lauritzen C]]
-[[Category: Pedersen, J]]
+[[Category: Olsen JG]]
-[[Category: Cathepsin c]]
+[[Category: Pedersen J]]
-[[Category: Chloride]]
-[[Category: Cysteine protease]]
-[[Category: Dpp i]]
-[[Category: Hydrolase]]
-[[Category: Papain]]
-[[Category: Tetramer]]