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1sud

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[[Image:1sud.jpg|left|200px]]
 
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{{Structure
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==CALCIUM-INDEPENDENT SUBTILISIN BY DESIGN==
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|PDB= 1sud |SIZE=350|CAPTION= <scene name='initialview01'>1sud</scene>, resolution 1.9&Aring;
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<StructureSection load='1sud' size='340' side='right'caption='[[1sud]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=ACN:ACETONE'>ACN</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CYA:TWO+OXYGEN+ATOMS+BOUND+TO+SG+OF+CYS'>CYA</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>
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<table><tr><td colspan='2'>[[1sud]] 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=1SUD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SUD FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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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]] 1.9&#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=ACN:ACETONE'>ACN</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
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|DOMAIN=
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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=1sud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sud OCA], [https://pdbe.org/1sud PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sud RCSB], [https://www.ebi.ac.uk/pdbsum/1sud PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sud ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1sud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sud OCA], [http://www.ebi.ac.uk/pdbsum/1sud PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1sud RCSB]</span>
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== Function ==
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}}
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[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>
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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/su/1sud_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=1sud ConSurf].
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<div style="clear:both"></div>
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'''CALCIUM-INDEPENDENT SUBTILISIN BY DESIGN'''
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==See Also==
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*[[Subtilisin 3D structures|Subtilisin 3D structures]]
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== References ==
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==Overview==
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<references/>
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A version of subtilisin BPN' lacking the high affinity calcium site (site A) has been produced through genetic engineering methods, and its crystal structure refined at 1.8 A resolution. This protein and the corresponding version containing the calcium A site are described and compared. The deletion of residues 75-83 was made in the context of four site-specific replacements previously shown to stabilize subtilisin. The helix that in wild type is interrupted by the calcium binding loop, is continuous in the deletion mutant, with normal geometry. A few residues adjacent to the loop, principally those that were involved in calcium coordination, are repositioned and/or destabilized by the deletion. Because refolding is greatly facilitated by the absence of the Ca-loop, this protein offers a new vehicle for analysis and dissection of the folding reaction. This is among the largest internal changes to a protein to be described at atomic resolution.
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__TOC__
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</StructureSection>
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==About this Structure==
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1SUD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SUD OCA].
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==Reference==
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Calcium-independent subtilisin by design., Gallagher T, Bryan P, Gilliland GL, Proteins. 1993 Jun;16(2):205-13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8332608 8332608]
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[[Category: Bacillus amyloliquefaciens]]
[[Category: Bacillus amyloliquefaciens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Subtilisin]]
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[[Category: Bryan P]]
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[[Category: Bryan, P.]]
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[[Category: Gallagher T]]
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[[Category: Gallagher, T.]]
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[[Category: Gilliland GL]]
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[[Category: Gilliland, G L.]]
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[[Category: hydrolase(serine proteinase)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:47:05 2008''
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CALCIUM-INDEPENDENT SUBTILISIN BY DESIGN

PDB ID 1sud

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