1scb: Difference between revisions
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<StructureSection load='1scb' size='340' side='right'caption='[[1scb]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='1scb' size='340' side='right'caption='[[1scb]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1scb]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1scb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"clostridium_licheniforme"_weigmann_1898 "clostridium licheniforme" weigmann 1898]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SCB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SCB 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>, <scene name='pdbligand=CCN:ACETONITRILE'>CCN</scene></td></tr> | </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=CCN:ACETONITRILE'>CCN</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1scb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1scb OCA], [https://pdbe.org/1scb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1scb RCSB], [https://www.ebi.ac.uk/pdbsum/1scb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1scb ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/SUBT_BACLI SUBT_BACLI]] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
*[[Subtilisin|Subtilisin]] | *[[Subtilisin 3D structures|Subtilisin 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 10:29, 22 September 2021
ENZYME CRYSTAL STRUCTURE IN A NEAT ORGANIC SOLVENTENZYME CRYSTAL STRUCTURE IN A NEAT ORGANIC SOLVENT
Structural highlights
Function[SUBT_BACLI] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystal structure of the serine protease subtilisin Carlsberg in anhydrous acetonitrile was determined at 2.3 A resolution. It was found to be essentially identical to the three-dimensional structure of the enzyme in water; the differences observed were smaller than those between two independently determined structures in aqueous solution. The hydrogen bond system of the catalytic triad is intact in acetonitrile. The majority (99 of 119) of enzyme-bound, structural water molecules have such a great affinity to subtilisin that they are not displaced even in anhydrous acetonitrile. Of the 12 enzyme-bound acetonitrile molecules, 4 displace water molecules and 8 bind where no water had been observed before. One-third of all subtilisin-bound acetonitrile molecules reside in the active center, occupying the same region (P1, P2, and P3 binding sites) as the specific protein inhibitor eglin c. Enzyme crystal structure in a neat organic solvent.,Fitzpatrick PA, Steinmetz AC, Ringe D, Klibanov AM Proc Natl Acad Sci U S A. 1993 Sep 15;90(18):8653-7. PMID:8378343[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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