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1sel
From Proteopedia
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| - | {{STRUCTURE_1sel| PDB=1sel | SCENE= }} | ||
| - | ===CRYSTAL STRUCTURE OF SELENOSUBTILISIN AT 2.0-ANGSTROMS RESOLUTION=== | ||
| - | {{ABSTRACT_PUBMED_8512925}} | ||
| - | == | + | ==CRYSTAL STRUCTURE OF SELENOSUBTILISIN AT 2.0-ANGSTROMS RESOLUTION== |
| - | [[http://www.uniprot.org/uniprot/ | + | <StructureSection load='1sel' size='340' side='right'caption='[[1sel]], [[Resolution|resolution]] 2.00Å' scene=''> |
| - | + | == Structural highlights == | |
| - | == | + | <table><tr><td colspan='2'>[[1sel]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SEL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SEL 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]] 2Å</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=SE7:2-AMINO-3-SELENINO-PROPIONIC+ACID'>SE7</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=1sel FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sel OCA], [https://pdbe.org/1sel PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sel RCSB], [https://www.ebi.ac.uk/pdbsum/1sel PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sel ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == 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 == | ||
| + | [[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/se/1sel_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=1sel ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
==See Also== | ==See Also== | ||
| - | *[[Subtilisin|Subtilisin]] | + | *[[Subtilisin 3D structures|Subtilisin 3D structures]] |
| - | + | == References == | |
| - | == | + | <references/> |
| - | + | __TOC__ | |
| - | [[Category: Bacillus | + | </StructureSection> |
| - | [[Category: Hilvert | + | [[Category: Bacillus subtilis]] |
| - | [[Category: Hogle | + | [[Category: Large Structures]] |
| - | [[Category: Syed | + | [[Category: Hilvert D]] |
| + | [[Category: Hogle JM]] | ||
| + | [[Category: Syed R]] | ||
Current revision
CRYSTAL STRUCTURE OF SELENOSUBTILISIN AT 2.0-ANGSTROMS RESOLUTION
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