5aqe
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 5aqe is ON HOLD Authors: Sharma, M., Diaz-Rodriguez, A., Offen, W.A., Palm-Espling, M.E., Pordea, A., Wormald, M.R., Mcdonough, M., Davies, G.J., Da...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Cooperative bio-metallic selectivity in a tailored protease enables creation of a C-C cross-coupling Heckase== | |
| + | <StructureSection load='5aqe' size='340' side='right'caption='[[5aqe]], [[Resolution|resolution]] 1.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5aqe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lederbergia_lenta Lederbergia lenta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AQE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AQE 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]] 1.1Å</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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=VOD:(4-VINYLPHENYL)METHANESULFONIC+ACID'>VOD</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=5aqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aqe OCA], [https://pdbe.org/5aqe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5aqe RCSB], [https://www.ebi.ac.uk/pdbsum/5aqe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5aqe ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/SUBS_LEDLE SUBS_LEDLE] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides. | ||
| - | + | ==See Also== | |
| - | + | *[[Subtilisin 3D structures|Subtilisin 3D structures]] | |
| - | + | __TOC__ | |
| - | [[Category: | + | </StructureSection> |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Lederbergia lenta]] |
| - | [[Category: | + | [[Category: Davies GJ]] |
| - | [[Category: | + | [[Category: Davis BG]] |
| - | [[Category: | + | [[Category: Diaz-Rodriguez A]] |
| - | [[Category: Palm-Espling | + | [[Category: Mcdonough M]] |
| - | [[Category: | + | [[Category: Offen WA]] |
| - | [[Category: | + | [[Category: Palm-Espling ME]] |
| - | [[Category: | + | [[Category: Pordea A]] |
| + | [[Category: Sharma M]] | ||
| + | [[Category: Wormald MR]] | ||
Current revision
Cooperative bio-metallic selectivity in a tailored protease enables creation of a C-C cross-coupling Heckase
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