4m4u

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==Structural evaluation D84A mutant of the aspergillus fumigatus kdnase (sialidase)==
==Structural evaluation D84A mutant of the aspergillus fumigatus kdnase (sialidase)==
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<StructureSection load='4m4u' size='340' side='right' caption='[[4m4u]], [[Resolution|resolution]] 1.84&Aring;' scene=''>
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<StructureSection load='4m4u' size='340' side='right'caption='[[4m4u]], [[Resolution|resolution]] 1.84&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4m4u]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M4U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4M4U FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4m4u]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_fumigatus_Af293 Aspergillus fumigatus Af293]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M4U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4M4U FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NO2:NITRITE+ION'>NO2</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 1.84&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2xcy|2xcy]], [[2xzi|2xzi]], [[2xzj|2xzj]], [[2xzk|2xzk]], [[4m4n|4m4n]], [[4m4v|4m4v]]</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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NO2:NITRITE+ION'>NO2</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Exo-alpha-sialidase Exo-alpha-sialidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.18 3.2.1.18] </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=4m4u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m4u OCA], [https://pdbe.org/4m4u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4m4u RCSB], [https://www.ebi.ac.uk/pdbsum/4m4u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4m4u ProSAT]</span></td></tr>
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<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=4m4u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m4u OCA], [http://pdbe.org/4m4u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4m4u RCSB], [http://www.ebi.ac.uk/pdbsum/4m4u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4m4u ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/SIA_ASPFU SIA_ASPFU]] Sialidase is able to release sialic acid from a wide variety of natural substrates including bovine salivary mucin, colominic acid, bovine fetuin, a serum glycoprotein containing both alpha-2-6 and alpha-2-3-linkages in a ratio of about 3:2, and glycoproteins and glycolipids from thermally denatured human lung epithelial cells. Does not show any trans-sialidase activity since it is able to remove terminal sialic acid residues but is unable to catalyze their transfer to the acceptor substrate. 2-keto-3-deoxynononic acid (KDN) is the preferred substrate and A.fumigatus can utilize KDN as a sole carbon source.<ref>PMID:20652740</ref>
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[https://www.uniprot.org/uniprot/SIA_ASPFU SIA_ASPFU] Sialidase is able to release sialic acid from a wide variety of natural substrates including bovine salivary mucin, colominic acid, bovine fetuin, a serum glycoprotein containing both alpha-2-6 and alpha-2-3-linkages in a ratio of about 3:2, and glycoproteins and glycolipids from thermally denatured human lung epithelial cells. Does not show any trans-sialidase activity since it is able to remove terminal sialic acid residues but is unable to catalyze their transfer to the acceptor substrate. 2-keto-3-deoxynononic acid (KDN) is the preferred substrate and A.fumigatus can utilize KDN as a sole carbon source.<ref>PMID:20652740</ref>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Exo-alpha-sialidase]]
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[[Category: Aspergillus fumigatus Af293]]
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[[Category: Taylor, G L]]
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[[Category: Large Structures]]
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[[Category: Telford, J C]]
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[[Category: Taylor GL]]
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[[Category: Hydrolase]]
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[[Category: Telford JC]]
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[[Category: Kdnase]]
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Current revision

Structural evaluation D84A mutant of the aspergillus fumigatus kdnase (sialidase)

PDB ID 4m4u

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