1mee: Difference between revisions

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 <StructureSection load='1mee' size='340' side='right'caption='[[1mee]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1mee]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_7061 Atcc 7061] and [http://en.wikipedia.org/wiki/Hirme Hirme]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MEE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MEE FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1mee]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_pumilus Bacillus pumilus] and [https://en.wikipedia.org/wiki/Hirudo_medicinalis Hirudo medicinalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MEE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MEE 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></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&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62, 3.4.21.63, 3.4.21.64, 3.4.21.65 and 3.4.21.67 3.4.21.62, 3.4.21.63, 3.4.21.64, 3.4.21.65 and 3.4.21.67] </span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=1mee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mee OCA], [http://pdbe.org/1mee PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mee RCSB], [http://www.ebi.ac.uk/pdbsum/1mee PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mee ProSAT]</span></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=1mee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mee OCA], [https://pdbe.org/1mee PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mee RCSB], [https://www.ebi.ac.uk/pdbsum/1mee PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mee ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/SUBT_BACPU SUBT_BACPU]] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides. [[http://www.uniprot.org/uniprot/ICIC_HIRME ICIC_HIRME]] Inhibits both elastase and cathepsin G.
+[https://www.uniprot.org/uniprot/SUBT_BACPU SUBT_BACPU] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides.
 == 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=1mee ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The alkaline proteinase from the mesophilic bacterium Bacillus mesentericus has been crystallized in a 1:1 complex with the inhibitor eglin-C from the medical leech. The crystals have cell dimensions of a = 43.0, b = 71.9, c = 48.3 A and beta = 110.0 degrees and are in the space group P2(1). Three-dimensional data to 2.0 A have been recorded on film from a single crystal. The orientation and position of the complex in the unit cell have been established using the refined coordinates of subtilisin Carlsberg and of eglin-C as independent models. The structure of the complex has been refined by restrained least-squares minimization. The crystallographic R factor (= sigma[magnitude of Fo - magnitude of Fc[/sigma magnitude of Fo) is 15.1% including two Ca2+ ions and 312 water molecules. The structure is discussed in terms of its physicochemical properties in solution and its relation to other Bacillus subtilisins.
-Complex between the subtilisin from a mesophilic bacterium and the leech inhibitor eglin-C.,Dauter Z, Betzel C, Genov N, Pipon N, Wilson KS Acta Crystallogr B. 1991 Oct 1;47 ( Pt 5):707-30. PMID:1793542<ref>PMID:1793542</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1mee" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Eglin|Eglin]]
-*[[Subtilisin|Subtilisin]]
+*[[Subtilisin 3D structures|Subtilisin 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Atcc 7061]]
+[[Category: Bacillus pumilus]]
-[[Category: Hirme]]
+[[Category: Hirudo medicinalis]]
-[[Category: Hydrolase]]
 [[Category: Large Structures]]
-[[Category: Betzel, C]]
+[[Category: Betzel C]]
-[[Category: Dauter, Z]]
+[[Category: Dauter Z]]
-[[Category: Wilson, K S]]
+[[Category: Wilson KS]]