4awd
From Proteopedia
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==Crystal structure of the beta-porphyranase BpGH16B (BACPLE_01689) from the human gut bacterium Bacteroides plebeius== | ==Crystal structure of the beta-porphyranase BpGH16B (BACPLE_01689) from the human gut bacterium Bacteroides plebeius== | ||
<StructureSection load='4awd' size='340' side='right' caption='[[4awd]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='4awd' size='340' side='right' caption='[[4awd]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
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</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=GOL:GLYCEROL'>GOL</scene></td></tr> | </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=GOL:GLYCEROL'>GOL</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-porphyranase Beta-porphyranase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.178 3.2.1.178] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-porphyranase Beta-porphyranase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.178 3.2.1.178] </span></td></tr> | ||
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4awd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4awd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4awd RCSB], [http://www.ebi.ac.uk/pdbsum/4awd PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4awd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4awd OCA], [http://pdbe.org/4awd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4awd RCSB], [http://www.ebi.ac.uk/pdbsum/4awd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4awd ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[http://www.uniprot.org/uniprot/ | + | [[http://www.uniprot.org/uniprot/PORB_BACPM PORB_BACPM]] Cleaves the sulfated polysaccharide porphyran at the (1->4) linkages between beta-D-galactopyranose and alpha-L-galactopyranose-6-sulfate, forming mostly the disaccharide alpha-L-galactopyranose-6-sulfate-(1->3)-beta-D-galactose. Some longer oligosaccharides of even number of residues are also observed. Inactive on the non-sulfated agarose portion of the porphyran backbone.<ref>PMID:23150581</ref> |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
| + | <div class="pdbe-citations 4awd" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 09:40, 11 August 2016
Crystal structure of the beta-porphyranase BpGH16B (BACPLE_01689) from the human gut bacterium Bacteroides plebeius
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