5xfc
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Serial femtosecond X-ray structure of a stem domain of human O-mannose beta-1,2-N-acetylglucosaminyltransferase solved by Se-SAD using XFEL (refined against 13,000 patterns)== | |
| - | + | <StructureSection load='5xfc' size='340' side='right' caption='[[5xfc]], [[Resolution|resolution]] 1.40Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5xfc]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XFC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XFC FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MBE:4-NITROPHENYL-BETA-D-MANNOPYRANOSIDE'>MBE</scene></td></tr> | |
| - | [[Category: | + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5xfd|5xfd]]</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=5xfc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xfc OCA], [http://pdbe.org/5xfc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xfc RCSB], [http://www.ebi.ac.uk/pdbsum/5xfc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xfc ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
| + | [[http://www.uniprot.org/uniprot/PMGT1_HUMAN PMGT1_HUMAN]] Walker-Warburg syndrome;Autosomal recessive limb-girdle muscular dystrophy type 2O;Congenital muscular dystrophy with cerebellar involvement;Muscle-eye-brain disease. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/PMGT1_HUMAN PMGT1_HUMAN]] Participates in O-mannosyl glycosylation. May be responsible for the synthesis of the GlcNAc(beta1-2)Man(alpha1-)O-Ser/Thr moiety on alpha-dystroglycan and other O-mannosylated proteins. Is specific for alpha linked terminal mannose and does not have MGAT3, MGAT4, MGAT5, MGAT7 or MGAT8 activity.<ref>PMID:11709191</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Fumiaki, Y]] | ||
[[Category: Kato, R]] | [[Category: Kato, R]] | ||
[[Category: Kuwabara, N]] | [[Category: Kuwabara, N]] | ||
[[Category: Manya, H]] | [[Category: Manya, H]] | ||
| - | [[Category: | + | [[Category: Carbohydrate-binding domain]] |
| + | [[Category: Glycosyltransferase]] | ||
| + | [[Category: Sugar binding protein]] | ||
Revision as of 15:01, 5 September 2017
Serial femtosecond X-ray structure of a stem domain of human O-mannose beta-1,2-N-acetylglucosaminyltransferase solved by Se-SAD using XFEL (refined against 13,000 patterns)
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