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2f28
From Proteopedia
(Difference between revisions)
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<StructureSection load='2f28' size='340' side='right'caption='[[2f28]], [[Resolution|resolution]] 1.67Å' scene=''> | <StructureSection load='2f28' size='340' side='right'caption='[[2f28]], [[Resolution|resolution]] 1.67Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2f28]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2f28]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F28 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F28 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1snt|1snt]], [[1so7|1so7]], [[1vcu|1vcu]], [[2f0z|2f0z]], [[2f10|2f10]], [[2f11|2f11]], [[2f12|2f12]], [[2f13|2f13]], [[2f24|2f24]], [[2f25|2f25]], [[2f26|2f26]], [[2f27|2f27]], [[2f29|2f29]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1snt|1snt]], [[1so7|1so7]], [[1vcu|1vcu]], [[2f0z|2f0z]], [[2f10|2f10]], [[2f11|2f11]], [[2f12|2f12]], [[2f13|2f13]], [[2f24|2f24]], [[2f25|2f25]], [[2f26|2f26]], [[2f27|2f27]], [[2f29|2f29]]</div></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Exo-alpha-sialidase Exo-alpha-sialidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.18 3.2.1.18] </span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2f28 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f28 OCA], [https://pdbe.org/2f28 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f28 RCSB], [https://www.ebi.ac.uk/pdbsum/2f28 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f28 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/NEUR2_HUMAN NEUR2_HUMAN]] Hydrolyzes sialylated compounds. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2f28 ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2f28 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Neuraminidase 3D structures|Neuraminidase 3D structures]] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 06:58, 10 November 2021
Crystal Structure of the Human Sialidase Neu2 Q116E Mutant
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Categories: Exo-alpha-sialidase | Human | Large Structures | Chavas, L M.G | Fusi, P | Kato, R | Monti, E | Tettamanti, G | Tringali, C | Venerando, B | Wakatsuki, S | Drug design | Ganglioside | Hydrolase | Neuraminidase | Sialidase
