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1scd
From Proteopedia
(Difference between revisions)
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<StructureSection load='1scd' size='340' side='right'caption='[[1scd]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='1scd' size='340' side='right'caption='[[1scd]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1scd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1scd]] 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=1SCD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SCD FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| - | <tr id=' | + | <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'>[https://proteopedia.org/fgij/fg.htm?mol=1scd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1scd OCA], [https://pdbe.org/1scd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1scd RCSB], [https://www.ebi.ac.uk/pdbsum/1scd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1scd 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=1scd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1scd OCA], [https://pdbe.org/1scd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1scd RCSB], [https://www.ebi.ac.uk/pdbsum/1scd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1scd ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/SUBC_BACLI SUBC_BACLI] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides (Ref.4, PubMed:11109488). Shows high specificity for aromatic and hydrophobic amino acids in the P1 substrate position (PubMed:11109488). May play an important role in the degradation of feather keratin (PubMed:11109488).<ref>PMID:11109488</ref> <ref>PMID:4967581</ref> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[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=1scd ConSurf]. | </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=1scd ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The crystal structure of subtilisin Carlsberg lightly cross-linked with glutaraldehyde was solved in aqueous solution by X-ray crystallography at 2.3 A resolution. It was found to be virtually identical to the recently determined (Fitzpatrick, P.A., Steinmetz, A.C.U., Ringe, D.A. & Klibanov, A.M. (1993) Proc. Natl. Acad. Sci. USA 90, 8653) structure of the cross-linked enzyme in anhydrous acetonitrile. The latter structure was found to be significantly more rigid than in water, as reflected by their average B factors. The numbers of subtilisin-bound water molecules in the two structures are similar (114 and 99 in water and in acetonitrile, respectively), but the locations of some half of these bound waters are distinct. | ||
| - | |||
| - | X-ray crystal structure of cross-linked subtilisin Carlsberg in water vs. acetonitrile.,Fitzpatrick PA, Ringe D, Klibanov AM Biochem Biophys Res Commun. 1994 Jan 28;198(2):675-81. PMID:8297378<ref>PMID:8297378</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1scd" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Bacillus licheniformis]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | + | [[Category: Fitzpatrick PA]] | |
| - | [[Category: Fitzpatrick | + | [[Category: Klibanov AM]] |
| - | [[Category: Klibanov | + | [[Category: Ringe D]] |
| - | [[Category: Ringe | + | |
| - | + | ||
Current revision
X-RAY CRYSTAL STRUCTURE OF CROSS-LINKED SUBTILISM CARLSBERG IN WATER VS. ACETONITRILE
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