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1sup

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SUBTILISIN BPN' AT 1.6 ANGSTROMS RESOLUTION: ANALYSIS OF DISCRETE DISORDER AND COMPARISON OF CRYSTAL FORMS

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-[[Image:1sup.jpg|left|200px]]<br /><applet load="1sup" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1sup, resolution 1.6&Aring;" />
-'''SUBTILISIN BPN' AT 1.6 ANGSTROMS RESOLUTION: ANALYSIS OF DISCRETE DISORDER AND COMPARISON OF CRYSTAL FORMS'''<br />
-==Overview==
+==SUBTILISIN BPN' AT 1.6 ANGSTROMS RESOLUTION: ANALYSIS OF DISCRETE DISORDER AND COMPARISON OF CRYSTAL FORMS==
-The three-dimensional structure of the serine protease subtilisin BPN', (SBT) has been refined at 1.6 A resolution in space group C2 to a final R, value of 0.17. 17 regions of discrete disorder have been identified and, analyzed. Two of these are dual-conformation peptide units; the remainder, involve alternate rotamers of side chains either alone or in small, clusters. The structure is compared with previously reported, high-resolution models of SBT in two other space groups, P2(1)2(1)2(1) and, P2(1). Apart from the surface, there are no significant variations in, structure among the three crystal forms. Structural variations observed at, the protein surface occur predominantly in regions of protein-protein, contact. The crystal packing arrangements in the three space groups are, compared.
+<StructureSection load='1sup' size='340' side='right'caption='[[1sup]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1sup]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SUP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SUP 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]] 1.6&#8491;</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>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PMS:PHENYLMETHANESULFONIC+ACID'>PMS</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=1sup FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sup OCA], [https://pdbe.org/1sup PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sup RCSB], [https://www.ebi.ac.uk/pdbsum/1sup PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sup ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/SUBT_BACAM SUBT_BACAM] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides. Has a high substrate specificity to fibrin.<ref>PMID:12524032</ref>
+== 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/su/1sup_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=1sup ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-SUP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens] with CA, NA and PMS 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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SUP OCA].
+*[[Subtilisin 3D structures|Subtilisin 3D structures]]
+== References ==
-==Reference==
+<references/>
-Subtilisin BPN' at 1.6 A resolution: analysis for discrete disorder and comparison of crystal forms., Gallagher T, Oliver J, Bott R, Betzel C, Gilliland GL, Acta Crystallogr D Biol Crystallogr. 1996 Nov 1;52(Pt 6):1125-35. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15299573 15299573]
+__TOC__
+</StructureSection>
 [[Category: Bacillus amyloliquefaciens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Subtilisin]]
+[[Category: Betzel C]]
-[[Category: Betzel, C.]]
+[[Category: Gallagher DT]]
-[[Category: Gallagher, D.T.]]
+[[Category: Gilliland GL]]
-[[Category: Gilliland, G.L.]]
+[[Category: Oliver JD]]
-[[Category: Oliver, J.D.]]
-[[Category: CA]]
-[[Category: NA]]
-[[Category: PMS]]
-[[Category: hydrolase (serine protease)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 02:41:12 2007''

1sup

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SUBTILISIN BPN' AT 1.6 ANGSTROMS RESOLUTION: ANALYSIS OF DISCRETE DISORDER AND COMPARISON OF CRYSTAL FORMS

Structural highlights

Function

Evolutionary Conservation

See Also

References

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