1bh6: Difference between revisions

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-[[Image:1bh6.gif|left|200px]]<br />
-<applet load="1bh6" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1bh6, resolution 1.75&Aring;" />
-'''SUBTILISIN DY IN COMPLEX WITH THE SYNTHETIC INHIBITOR N-BENZYLOXYCARBONYL-ALA-PRO-PHE-CHLOROMETHYL KETONE'''<br />
-==Overview==
+==SUBTILISIN DY IN COMPLEX WITH THE SYNTHETIC INHIBITOR N-BENZYLOXYCARBONYL-ALA-PRO-PHE-CHLOROMETHYL KETONE==
-The crystal structure of subtilisin DY inhibited by, N-benzyloxycarbonyl-Ala-Pro-Phe-chloromethyl ketone has been solved by, molecular replacement with subtilisin Carlsberg as the starting model. The, model has been refined to a crystallographic R factor (= sigma absolute, value [(absolute value Fo) - (absolute value Fc)] / sigma (absolute value, of Fo) of 15.1% using X-ray diffraction data to 0.175 nm resolution., Subtilisin DY is an alkaline proteinase from the X-irradiated Japanese, strain DY of Bacillus licheniformis, which normally produces subtilisin, Carlsberg. It has very similar properties to subtilisin Carlsberg, with a, slightly enhanced resistance to heat and guanidine hydrochloride-induced, denaturation, in spite of the fact that the sequences of the two enzymes, differ in 31 positions out of 274 residues. The close similarity in, overall three-dimensional structure of subtilisins DY and Carlsberg and, also their physicochemical properties, such as activity and stability, shows that nature aided by X-irradiation for rapid 'evolution' is able to, accommodate considerable changes in sequence without substantial changes, in property.
+<StructureSection load='1bh6' size='340' side='right'caption='[[1bh6]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1bh6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BH6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BH6 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1BH:N-BENZYLOXYCARBONYL-ALA-PRO-3-AMINO-4-PHENYL-BUTAN-2-OL'>1BH</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=1bh6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bh6 OCA], [https://pdbe.org/1bh6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bh6 RCSB], [https://www.ebi.ac.uk/pdbsum/1bh6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bh6 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/SUBD_BACLI SUBD_BACLI] 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]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bh/1bh6_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1bh6 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The crystal structure of subtilisin DY inhibited by N-benzyloxycarbonyl-Ala-Pro-Phe-chloromethyl ketone has been solved by molecular replacement with subtilisin Carlsberg as the starting model. The model has been refined to a crystallographic R factor (= sigma absolute value [(absolute value Fo) - (absolute value Fc)] / sigma (absolute value of Fo) of 15.1% using X-ray diffraction data to 0.175 nm resolution. Subtilisin DY is an alkaline proteinase from the X-irradiated Japanese strain DY of Bacillus licheniformis, which normally produces subtilisin Carlsberg. It has very similar properties to subtilisin Carlsberg, with a slightly enhanced resistance to heat and guanidine hydrochloride-induced denaturation, in spite of the fact that the sequences of the two enzymes differ in 31 positions out of 274 residues. The close similarity in overall three-dimensional structure of subtilisins DY and Carlsberg and also their physicochemical properties, such as activity and stability, shows that nature aided by X-irradiation for rapid 'evolution' is able to accommodate considerable changes in sequence without substantial changes in property.
-==About this Structure==
+Crystal structure of subtilisin DY, a random mutant of subtilisin Carlsberg.,Eschenburg S, Genov N, Peters K, Fittkau S, Stoeva S, Wilson KS, Betzel C Eur J Biochem. 1998 Oct 15;257(2):309-18. PMID:9826175<ref>PMID:9826175</ref>
-BH6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis] with CA, NA and 1BH as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62] Structure known Active Site: ACT. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BH6 OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-Crystal structure of subtilisin DY, a random mutant of subtilisin Carlsberg., Eschenburg S, Genov N, Peters K, Fittkau S, Stoeva S, Wilson KS, Betzel C, Eur J Biochem. 1998 Oct 15;257(2):309-18. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9826175 9826175]
+</div>
+<div class="pdbe-citations 1bh6" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Subtilisin 3D structures|Subtilisin 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Bacillus licheniformis]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Subtilisin]]
+[[Category: Betzel C]]
-[[Category: Betzel, C.]]
+[[Category: Eschenburg S]]
-[[Category: Eschenburg, S.]]
+[[Category: Genov N]]
-[[Category: Genov, N.]]
+[[Category: Wilson KS]]
-[[Category: Wilson, K.S.]]
-[[Category: 1BH]]
-[[Category: CA]]
-[[Category: NA]]
-[[Category: hydrolase]]
-[[Category: protein degradation]]
-[[Category: subtilisin]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov  5 15:54:33 2007''