3wie
From Proteopedia
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<StructureSection load='3wie' size='340' side='right' caption='[[3wie]], [[Resolution|resolution]] 2.33Å' scene=''> | <StructureSection load='3wie' size='340' side='right' caption='[[3wie]], [[Resolution|resolution]] 2.33Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3wie]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WIE OCA]. <br> | + | <table><tr><td colspan='2'>[[3wie]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WIE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WIE FirstGlance]. <br> |
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=DN4:[[(2R,3R,4R,5R)-5-(6-AMINOPURIN-9-YL)-3-OXIDANYL-4-PHOSPHONOOXY-OXOLAN-2-YL]METHOXY-OXIDANYL-PHOSPHORYL]+[(2R,3S,4R,5R)-5-(3-CARBOXYPYRIDIN-1-IUM-1-YL)-3,4-BIS(OXIDANYL)OXOLAN-2-YL]METHYL+PHOSPHATE'>DN4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=DN4:[[(2R,3R,4R,5R)-5-(6-AMINOPURIN-9-YL)-3-OXIDANYL-4-PHOSPHONOOXY-OXOLAN-2-YL]METHOXY-OXIDANYL-PHOSPHORYL]+[(2R,3S,4R,5R)-5-(3-CARBOXYPYRIDIN-1-IUM-1-YL)-3,4-BIS(OXIDANYL)OXOLAN-2-YL]METHYL+PHOSPHATE'>DN4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wic|3wic]], [[3wid|3wid]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wic|3wic]], [[3wid|3wid]]</td></tr> |
| - | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucose_1-dehydrogenase Glucose 1-dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.47 1.1.1.47] </span></td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3wie FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wie OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wie RCSB], [http://www.ebi.ac.uk/pdbsum/3wie 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=3wie FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wie OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wie RCSB], [http://www.ebi.ac.uk/pdbsum/3wie PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/Q979W2_THEVO Q979W2_THEVO]] Catalyzes the NAD(P)(+)-dependent oxidation of D-glucose to D-gluconate via gluconolactone. Can utilize both NAD(+) and NADP(+) as electron acceptor. Is involved in the degradation of glucose through a non-phosphorylative variant of the Entner-Doudoroff pathway (By similarity).[HAMAP-Rule:MF_02127] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Glucose 1-dehydrogenase]] | [[Category: Glucose 1-dehydrogenase]] | ||
| - | [[Category: Kanoh, Y | + | [[Category: Kanoh, Y]] |
| - | [[Category: Ohshima, T | + | [[Category: Ohshima, T]] |
| - | [[Category: Sakuraba, H | + | [[Category: Sakuraba, H]] |
| - | [[Category: Yoneda, K | + | [[Category: Yoneda, K]] |
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
[[Category: Rossmann fold]] | [[Category: Rossmann fold]] | ||
Revision as of 21:47, 24 December 2014
Structure of a glucose dehydrogenase T277F mutant in complex with D-glucose and NAADP
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