5ggn
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of N-terminal domain of human protein O-mannose beta-1,2-N-acetylglucosaminyltransferase in complex with GlcNAc-beta-pNP== | |
| - | + | <StructureSection load='5ggn' size='340' side='right' caption='[[5ggn]], [[Resolution|resolution]] 1.21Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5ggn]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GGN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GGN FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LEC:N-[(2S,3R,4R,5S,6R)-4,5-DIHYDROXY-6-(HYDROXYMETHYL)-2-(4-NITROPHENOXY)OXAN-3-YL]ETHANAMIDE'>LEC</scene></td></tr> | |
| - | [[Category: | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ggf|5ggf]], [[5ggg|5ggg]], [[5ggi|5ggi]], [[5ggj|5ggj]], [[5ggk|5ggk]], [[5ggl|5ggl]], [[5ggo|5ggo]], [[5ggp|5ggp]]</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=5ggn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ggn OCA], [http://pdbe.org/5ggn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ggn RCSB], [http://www.ebi.ac.uk/pdbsum/5ggn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ggn 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: Kato, R]] | ||
[[Category: Kuwabara, N]] | [[Category: Kuwabara, N]] | ||
| - | [[Category: Kato, R]] | ||
[[Category: Senda, T]] | [[Category: Senda, T]] | ||
| + | [[Category: Alpha-dystroglycan]] | ||
| + | [[Category: Glycosyltransferease]] | ||
| + | [[Category: O-mannosylation]] | ||
| + | [[Category: Sugar binding protein]] | ||
Revision as of 16:25, 10 August 2016
Crystal structure of N-terminal domain of human protein O-mannose beta-1,2-N-acetylglucosaminyltransferase in complex with GlcNAc-beta-pNP
| |||||||||||
