6dwq: Difference between revisions
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<StructureSection load='6dwq' size='340' side='right'caption='[[6dwq]], [[Resolution|resolution]] 1.27Å' scene=''> | <StructureSection load='6dwq' size='340' side='right'caption='[[6dwq]], [[Resolution|resolution]] 1.27Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6dwq]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6dwq]] 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=6DWQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6DWQ 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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.27Å</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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=OSE:O-SULFO-L-SERINE'>OSE</scene>, <scene name='pdbligand=P5U:O-[(4-cyanophenyl)sulfonyl]-L-serine'>P5U</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=6dwq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dwq OCA], [https://pdbe.org/6dwq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6dwq RCSB], [https://www.ebi.ac.uk/pdbsum/6dwq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6dwq ProSAT]</span></td></tr> | ||
</table> | </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> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bacillus licheniformis]] | [[Category: Bacillus licheniformis]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Eaton | [[Category: Eaton CN]] | ||
[[Category: Luo | [[Category: Luo M]] | ||
[[Category: Phillips-Piro | [[Category: Phillips-Piro CM]] | ||
Latest revision as of 06:15, 11 October 2023
Subtilisin serine protease modified with the protease inhibitor cyanobenzylsulfonylfluoride
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