4m4v
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structural evaluation R171L mutant of the aspergillus fumigatus kdnase (sialidase)== | |
| - | + | <StructureSection load='4m4v' size='340' side='right'caption='[[4m4v]], [[Resolution|resolution]] 1.84Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4m4v]] 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=4M4V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4M4V FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.84Å</td></tr> | |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DAN:2-DEOXY-2,3-DEHYDRO-N-ACETYL-NEURAMINIC+ACID'>DAN</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></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=4m4v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m4v OCA], [https://pdbe.org/4m4v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4m4v RCSB], [https://www.ebi.ac.uk/pdbsum/4m4v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4m4v ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [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/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Aspergillus fumigatus Af293]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Taylor GL]] | ||
| + | [[Category: Telford JC]] | ||
Current revision
Structural evaluation R171L mutant of the aspergillus fumigatus kdnase (sialidase)
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