1uhb

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[[Image:1uhb.jpg|left|200px]]
 
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{{Structure
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==Crystal structure of porcine alpha trypsin bound with auto catalyticaly produced native peptide at 2.15 A resolution==
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|PDB= 1uhb |SIZE=350|CAPTION= <scene name='initialview01'>1uhb</scene>, resolution 2.15&Aring;
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<StructureSection load='1uhb' size='340' side='right'caption='[[1uhb]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene> and <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
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<table><tr><td colspan='2'>[[1uhb]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UHB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UHB FirstGlance]. <br>
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|ACTIVITY= [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]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1uhb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uhb OCA], [https://pdbe.org/1uhb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uhb RCSB], [https://www.ebi.ac.uk/pdbsum/1uhb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uhb ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TRYP_PIG TRYP_PIG]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/uh/1uhb_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1uhb ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Trypsin, a serine protease enzyme plays a pivotal role in digestion and is autocatalytic. The crystal structure of a complex formed between porcine trypsin and an auto catalytically produced peptide is reported here. This complex shows a reduction in enzyme activity as compared to native beta-trypsin. The nonapeptide has a lysine, which is recognized by Asp 189 at the specificity pocket. The auto catalytically produced native nonapeptide is bound at the active site cleft like other trypsin inhibitors but the important interactions with the oxyanion hole are absent. The peptide covers only a part of the active site cleft and hence the enzyme activity is reduced rather than being inhibited.
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'''Crystal structure of porcine alpha trypsin bound with auto catalyticaly produced native peptide at 2.15 A resolution'''
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Trypsin activity reduced by an autocatalytically produced nonapeptide.,Ibrahim BS, Shamaladevi N, Pattabhi V J Biomol Struct Dyn. 2004 Jun;21(6):737-44. PMID:15106996<ref>PMID:15106996</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1uhb" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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Trypsin, a serine protease enzyme plays a pivotal role in digestion and is autocatalytic. The crystal structure of a complex formed between porcine trypsin and an auto catalytically produced peptide is reported here. This complex shows a reduction in enzyme activity as compared to native beta-trypsin. The nonapeptide has a lysine, which is recognized by Asp 189 at the specificity pocket. The auto catalytically produced native nonapeptide is bound at the active site cleft like other trypsin inhibitors but the important interactions with the oxyanion hole are absent. The peptide covers only a part of the active site cleft and hence the enzyme activity is reduced rather than being inhibited.
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*[[Trypsin 3D structures|Trypsin 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1UHB is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UHB OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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Trypsin activity reduced by an autocatalytically produced nonapeptide., Ibrahim BS, Shamaladevi N, Pattabhi V, J Biomol Struct Dyn. 2004 Jun;21(6):737-44. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15106996 15106996]
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[[Category: Protein complex]]
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[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
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[[Category: Trypsin]]
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[[Category: Pattabhi V]]
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[[Category: Ibrahim, B Syed.]]
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[[Category: Shamaladevi N]]
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[[Category: Pattabhi, V.]]
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[[Category: Syed Ibrahim B]]
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[[Category: Shamaladevi, N.]]
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[[Category: ACT]]
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[[Category: CA]]
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[[Category: hydrolase]]
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[[Category: peptide trypsin complex]]
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[[Category: serine protease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:32:00 2008''
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Current revision

Crystal structure of porcine alpha trypsin bound with auto catalyticaly produced native peptide at 2.15 A resolution

PDB ID 1uhb

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