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1qx1

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==Golgi alpha-mannosidase II D341N mutant complex with 2-F-mannosyl-F==
==Golgi alpha-mannosidase II D341N mutant complex with 2-F-mannosyl-F==
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<StructureSection load='1qx1' size='340' side='right' caption='[[1qx1]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
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<StructureSection load='1qx1' size='340' side='right'caption='[[1qx1]], [[Resolution|resolution]] 1.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1qx1]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QX1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QX1 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1qx1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QX1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QX1 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=FMF:2-DEOXY-2-FLUOROHEXOPYRANOSYL+FLUORIDE'>FMF</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.3&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1qwn|1qwn]], [[1qwu|1qwu]], [[1ps3|1ps3]], [[1hty|1hty]], [[1hww|1hww]], [[1hxk|1hxk]]</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=FMF:2-DEOXY-2-FLUOROHEXOPYRANOSYL+FLUORIDE'>FMF</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ALPHA-MAN-II OR GMII OR CG18474/CG18802/CG8139 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</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=1qx1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qx1 OCA], [https://pdbe.org/1qx1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qx1 RCSB], [https://www.ebi.ac.uk/pdbsum/1qx1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qx1 ProSAT]</span></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/Mannosyl-oligosaccharide_1,3-1,6-alpha-mannosidase Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.114 3.2.1.114] </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=1qx1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qx1 OCA], [http://pdbe.org/1qx1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qx1 RCSB], [http://www.ebi.ac.uk/pdbsum/1qx1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qx1 ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/MAN2_DROME MAN2_DROME]] Catalyzes the first committed step in the biosynthesis of complex N-glycans. It controls conversion of high mannose to complex N-glycans; the final hydrolytic step in the N-glycan maturation pathway (By similarity).
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[https://www.uniprot.org/uniprot/MAN2_DROME MAN2_DROME] Catalyzes the first committed step in the biosynthesis of complex N-glycans. It controls conversion of high mannose to complex N-glycans; the final hydrolytic step in the N-glycan maturation pathway (By similarity).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</div>
</div>
<div class="pdbe-citations 1qx1" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 1qx1" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Mannosidase 3D structures|Mannosidase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Drome]]
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[[Category: Drosophila melanogaster]]
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[[Category: Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase]]
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[[Category: Large Structures]]
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[[Category: Kuntz, D A]]
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[[Category: Kuntz DA]]
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[[Category: Numao, S]]
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[[Category: Numao S]]
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[[Category: Rose, D R]]
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[[Category: Rose DR]]
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[[Category: Withers, S G]]
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[[Category: Withers SG]]
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[[Category: Covalent catalytic intermediate]]
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[[Category: Glycosyl hydrolase family 38]]
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[[Category: Hydrolase]]
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Current revision

Golgi alpha-mannosidase II D341N mutant complex with 2-F-mannosyl-F

PDB ID 1qx1

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