4ba0

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Current revision (11:46, 20 December 2023) (edit) (undo)
 
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<StructureSection load='4ba0' size='340' side='right'caption='[[4ba0]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
<StructureSection load='4ba0' size='340' side='right'caption='[[4ba0]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4ba0]] is a 1 chain structure. 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 [https://proteopedia.org/fgij/fg.htm?mol=4BA0 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4ba0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cellvibrio_japonicus Cellvibrio japonicus]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4BA0 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4b9y|4b9y]], [[4b9z|4b9z]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Alpha-glucosidase Alpha-glucosidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.20 3.2.1.20] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ba0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ba0 OCA], [https://pdbe.org/4ba0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ba0 RCSB], [https://www.ebi.ac.uk/pdbsum/4ba0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ba0 ProSAT]</span></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=4ba0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ba0 OCA], [https://pdbe.org/4ba0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ba0 RCSB], [https://www.ebi.ac.uk/pdbsum/4ba0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ba0 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://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>
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[https://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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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Alpha-glucosidase]]
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[[Category: Cellvibrio japonicus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Brumer, H]]
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[[Category: Brumer H]]
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[[Category: Davies, G J]]
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[[Category: Davies GJ]]
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[[Category: Hemsworth, G R]]
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[[Category: Hemsworth GR]]
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[[Category: Izumi, A]]
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[[Category: Izumi A]]
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[[Category: Larsbrink, J]]
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[[Category: Larsbrink J]]
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[[Category: Hydrolase]]
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Current revision

Crystal Structure of Agd31B, alpha-transglucosylase, complexed with 5F-alpha-GlcF

PDB ID 4ba0

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