4m4n: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
Line 3: Line 3:
<StructureSection load='4m4n' size='340' side='right'caption='[[4m4n]], [[Resolution|resolution]] 1.84&Aring;' scene=''>
<StructureSection load='4m4n' size='340' side='right'caption='[[4m4n]], [[Resolution|resolution]] 1.84&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4m4n]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspfu Aspfu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M4N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4M4N FirstGlance]. <br>
<table><tr><td colspan='2'>[[4m4n]] 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=4M4N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4M4N FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2xcy|2xcy]], [[2xzi|2xzi]], [[2xzj|2xzj]], [[2xzk|2xzk]], [[4m4u|4m4u]], [[4m4v|4m4v]]</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=4m4n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m4n OCA], [https://pdbe.org/4m4n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4m4n RCSB], [https://www.ebi.ac.uk/pdbsum/4m4n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4m4n ProSAT]</span></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AFUA_4G13800 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=330879 ASPFU])</td></tr>
<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>
<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=4m4n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m4n OCA], [http://pdbe.org/4m4n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4m4n RCSB], [http://www.ebi.ac.uk/pdbsum/4m4n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4m4n ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[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>
[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>  
 
==See Also==
*[[Sialidase|Sialidase]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Aspfu]]
[[Category: Aspergillus fumigatus Af293]]
[[Category: Exo-alpha-sialidase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Taylor, G L]]
[[Category: Taylor GL]]
[[Category: Telford, J C]]
[[Category: Telford JC]]
[[Category: Hydrolase]]
[[Category: Kdnase]]