2v5d
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2v5d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Clostridium_perfringens Clostridium perfringens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V5D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2V5D FirstGlance]. <br> | <table><tr><td colspan='2'>[[2v5d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Clostridium_perfringens Clostridium perfringens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V5D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2V5D FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2j62|2j62]], [[2jh2|2jh2]], [[2v5c|2v5c]], [[2vur|2vur]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2j62|2j62]], [[2jh2|2jh2]], [[2v5c|2v5c]], [[2vur|2vur]]</td></tr> |
| - | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-N-acetylhexosaminidase Beta-N-acetylhexosaminidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.52 3.2.1.52] </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-N-acetylhexosaminidase Beta-N-acetylhexosaminidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.52 3.2.1.52] </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=2v5d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v5d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2v5d RCSB], [http://www.ebi.ac.uk/pdbsum/2v5d 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=2v5d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v5d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2v5d RCSB], [http://www.ebi.ac.uk/pdbsum/2v5d PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/OGA_CLOP1 OGA_CLOP1]] Biological function unknown. Capable of hydrolyzing the glycosidic link of O-GlcNAcylated proteins. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Beta-N-acetylhexosaminidase]] | [[Category: Beta-N-acetylhexosaminidase]] | ||
[[Category: Clostridium perfringens]] | [[Category: Clostridium perfringens]] | ||
| - | [[Category: Adams, J J | + | [[Category: Adams, J J]] |
| - | [[Category: Boraston, A B | + | [[Category: Boraston, A B]] |
| - | [[Category: Czjzek, M | + | [[Category: Czjzek, M]] |
| - | [[Category: Ficko-Blean, E | + | [[Category: Ficko-Blean, E]] |
| - | [[Category: Gregg, K J | + | [[Category: Gregg, K J]] |
| - | [[Category: Hehemann, J H | + | [[Category: Hehemann, J H]] |
| - | [[Category: Smith, S J | + | [[Category: Smith, S J]] |
[[Category: Carbohydrate binding module]] | [[Category: Carbohydrate binding module]] | ||
[[Category: Cbm32]] | [[Category: Cbm32]] | ||
Revision as of 04:26, 25 December 2014
STRUCTURE OF A FAMILY 84 GLYCOSIDE HYDROLASE AND A FAMILY 32 CARBOHYDRATE-BINDING MODULE IN TANDEM FROM CLOSTRIDIUM PERFRINGENS.
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Categories: Beta-N-acetylhexosaminidase | Clostridium perfringens | Adams, J J | Boraston, A B | Czjzek, M | Ficko-Blean, E | Gregg, K J | Hehemann, J H | Smith, S J | Carbohydrate binding module | Cbm32 | Clostridium perfringen | Family 32 carbohydrate binding module | Family 84 glycoside hydrolase | Gh84 | Gh84c | Glycosidase | Hydrolase
