3eju: Difference between revisions

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'''Unreleased structure'''


The entry 3eju is ON HOLD
==Golgi alpha-Mannosidase II in complex with 5-substituted swainsonine analog:(5S)-5-[2'-oxo-2'-(4-tert-butylphenyl)ethyl]-swainsonine==
<StructureSection load='3eju' size='340' side='right'caption='[[3eju]], [[Resolution|resolution]] 1.32&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3eju]] 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=3EJU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EJU 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]] 1.32&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HN7:1-(4-TERT-BUTYLPHENYL)-2-[(1S,2R,5S,8R,8AR)-1,2,8-TRIHYDROXYOCTAHYDROINDOLIZIN-5-YL]ETHANONE'>HN7</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=3eju FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eju OCA], [https://pdbe.org/3eju PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3eju RCSB], [https://www.ebi.ac.uk/pdbsum/3eju PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3eju ProSAT]</span></td></tr>
</table>
== Function ==
[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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ej/3eju_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3eju ConSurf].
<div style="clear:both"></div>


Authors: Kuntz, D.A., Shea, K., Rose, D.R.
==See Also==
 
*[[Mannosidase 3D structures|Mannosidase 3D structures]]
Description: Golgi alpha-Mannosidase II in complex with 5-substituted swainsonine analog:(5S)-5-[2'-oxo-2'-(4-tert-butylphenyl)ethyl]-swainsonine
__TOC__
 
</StructureSection>
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Oct  1 21:13:24 2008''
[[Category: Drosophila melanogaster]]
[[Category: Large Structures]]
[[Category: Kuntz DA]]
[[Category: Rose DR]]
[[Category: Shea K]]

Latest revision as of 09:36, 3 April 2024

Golgi alpha-Mannosidase II in complex with 5-substituted swainsonine analog:(5S)-5-[2'-oxo-2'-(4-tert-butylphenyl)ethyl]-swainsonineGolgi alpha-Mannosidase II in complex with 5-substituted swainsonine analog:(5S)-5-[2'-oxo-2'-(4-tert-butylphenyl)ethyl]-swainsonine

Structural highlights

3eju is a 1 chain structure with sequence from Drosophila melanogaster. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.32Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

3eju, resolution 1.32Å

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