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4ba0
From Proteopedia
(Difference between revisions)
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==Crystal Structure of Agd31B, alpha-transglucosylase, complexed with 5F-alpha-GlcF== | ==Crystal Structure of Agd31B, alpha-transglucosylase, complexed with 5F-alpha-GlcF== | ||
<StructureSection load='4ba0' size='340' side='right' caption='[[4ba0]], [[Resolution|resolution]] 1.85Å' scene=''> | <StructureSection load='4ba0' size='340' side='right' caption='[[4ba0]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4ba0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[4ba0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"cellvibrio_cellulosa"_nagy_et_al._2002 "cellvibrio cellulosa" nagy et al. 2002]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BA0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BA0 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5GF:5-FLUORO-BETA-D-GLUCOPYRANOSE'>5GF</scene>, <scene name='pdbligand=ARG:ARGININE'>ARG</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5GF:5-FLUORO-BETA-D-GLUCOPYRANOSE'>5GF</scene>, <scene name='pdbligand=ARG:ARGININE'>ARG</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4b9y|4b9y]], [[4b9z|4b9z]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4b9y|4b9y]], [[4b9z|4b9z]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-glucosidase Alpha-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.20 3.2.1.20] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-glucosidase Alpha-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.20 3.2.1.20] </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=4ba0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ba0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ba0 RCSB], [http://www.ebi.ac.uk/pdbsum/4ba0 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=4ba0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ba0 OCA], [http://pdbe.org/4ba0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ba0 RCSB], [http://www.ebi.ac.uk/pdbsum/4ba0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ba0 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[http://www.uniprot.org/uniprot/ | + | [[http://www.uniprot.org/uniprot/OL4AG_CELJU OL4AG_CELJU]] Alpha-transglucosylase that specifically transfers single glucosyl units from alpha(1->4)-glucans to the non-reducing terminal 4-OH of glucose and alpha(1->4)- and alpha(1->6)-linked glucosyl residues. Acts on amylose, amylopectin, glycogen and maltooligosaccharides, with the highest activity with maltotriose as a donor, and also accepts maltose. Does not act as a hydrolase: weak hydrolysis activity is only observed on the disaccharide maltose.<ref>PMID:23132856</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 4ba0" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Cellvibrio cellulosa nagy et al. 2002]] | ||
[[Category: Alpha-glucosidase]] | [[Category: Alpha-glucosidase]] | ||
| - | [[Category: Cellvibrio japonicus]] | ||
[[Category: Brumer, H]] | [[Category: Brumer, H]] | ||
[[Category: Davies, G J]] | [[Category: Davies, G J]] | ||
Revision as of 20:40, 4 August 2016
Crystal Structure of Agd31B, alpha-transglucosylase, complexed with 5F-alpha-GlcF
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