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1bfk
From Proteopedia
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==CRYSTAL STRUCTURE OF SUBTILISIN CARLSBERG IN 40% ACETONITRILE== | ==CRYSTAL STRUCTURE OF SUBTILISIN CARLSBERG IN 40% ACETONITRILE== | ||
| - | <StructureSection load='1bfk' size='340' side='right' caption='[[1bfk]], [[Resolution|resolution]] 2.30Å' scene=''> | + | <StructureSection load='1bfk' size='340' side='right'caption='[[1bfk]], [[Resolution|resolution]] 2.30Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1bfk]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1bfk]] 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=1BFK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BFK 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>, <scene name='pdbligand=CCN:ACETONITRILE'>CCN</scene></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=1bfk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bfk OCA], [https://pdbe.org/1bfk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bfk RCSB], [https://www.ebi.ac.uk/pdbsum/1bfk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bfk 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]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bf/1bfk_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bf/1bfk_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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==See Also== | ==See Also== | ||
| - | *[[Subtilisin|Subtilisin]] | + | *[[Subtilisin 3D structures|Subtilisin 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Bacillus licheniformis]] | [[Category: Bacillus licheniformis]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Klibanov | + | [[Category: Klibanov AM]] |
| - | [[Category: Schmitke | + | [[Category: Schmitke JL]] |
| - | [[Category: Stern | + | [[Category: Stern LJ]] |
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Current revision
CRYSTAL STRUCTURE OF SUBTILISIN CARLSBERG IN 40% ACETONITRILE
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