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8ibm
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Sulfate bound form of PET-degrading cutinase Cut190 with thermostability-improving mutations of S226P/R228S/Q138A/D250C-E296C/Q123H/N202H and S176A inactivation== | |
| - | + | <StructureSection load='8ibm' size='340' side='right'caption='[[8ibm]], [[Resolution|resolution]] 2.20Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[8ibm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomonospora_viridis Saccharomonospora viridis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8IBM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8IBM FirstGlance]. <br> | |
| - | + | </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=SO4:SULFATE+ION'>SO4</scene></td></tr> | |
| - | [[Category: | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8ibm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ibm OCA], [https://pdbe.org/8ibm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ibm RCSB], [https://www.ebi.ac.uk/pdbsum/8ibm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ibm ProSAT]</span></td></tr> |
| - | [[Category: | + | </table> |
| - | [[Category: | + | == Function == |
| - | [[Category: Kamiya | + | [https://www.uniprot.org/uniprot/W0TJ64_9PSEU W0TJ64_9PSEU] |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Saccharomonospora viridis]] | ||
| + | [[Category: Emori M]] | ||
| + | [[Category: Kamiya N]] | ||
| + | [[Category: Numoto N]] | ||
| + | [[Category: Oda M]] | ||
Current revision
Sulfate bound form of PET-degrading cutinase Cut190 with thermostability-improving mutations of S226P/R228S/Q138A/D250C-E296C/Q123H/N202H and S176A inactivation
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