3ioi: Difference between revisions

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<StructureSection load='3ioi' size='340' side='right'caption='[[3ioi]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
<StructureSection load='3ioi' size='340' side='right'caption='[[3ioi]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3ioi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IOI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IOI FirstGlance]. <br>
<table><tr><td colspan='2'>[[3ioi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IOI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IOI FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1GW:5-(2-FORMYLTHIEN-5-YL)-URIDINE-5-DIPHOSPHATE-ALPHA-D-GALACTOSE'>1GW</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.45&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3ioh|3ioh]], [[3ioj|3ioj]], [[1lz0|1lz0]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1GW:5-(2-FORMYLTHIEN-5-YL)-URIDINE-5-DIPHOSPHATE-ALPHA-D-GALACTOSE'>1GW</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ABO ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3ioi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ioi OCA], [https://pdbe.org/3ioi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ioi RCSB], [https://www.ebi.ac.uk/pdbsum/3ioi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ioi ProSAT]</span></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=3ioi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ioi OCA], [https://pdbe.org/3ioi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ioi RCSB], [https://www.ebi.ac.uk/pdbsum/3ioi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ioi ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/BGAT_HUMAN BGAT_HUMAN]] This protein is the basis of the ABO blood group system. The histo-blood group ABO involves three carbohydrate antigens: A, B, and H. A, B, and AB individuals express a glycosyltransferase activity that converts the H antigen to the A antigen (by addition of UDP-GalNAc) or to the B antigen (by addition of UDP-Gal), whereas O individuals lack such activity.  
[https://www.uniprot.org/uniprot/BGAT_HUMAN BGAT_HUMAN] This protein is the basis of the ABO blood group system. The histo-blood group ABO involves three carbohydrate antigens: A, B, and H. A, B, and AB individuals express a glycosyltransferase activity that converts the H antigen to the A antigen (by addition of UDP-GalNAc) or to the B antigen (by addition of UDP-Gal), whereas O individuals lack such activity.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Jorgensen, R]]
[[Category: Jorgensen R]]
[[Category: Palcic, M M]]
[[Category: Palcic MM]]
[[Category: Pesnot, T]]
[[Category: Pesnot T]]
[[Category: Wagner, G K]]
[[Category: Wagner GK]]
[[Category: Abo]]
[[Category: Blood group antigen]]
[[Category: Cisab mutant]]
[[Category: Glycoprotein]]
[[Category: Glycosyltransferase]]
[[Category: Golgi apparatus]]
[[Category: Gta]]
[[Category: Inhibitor]]
[[Category: Manganese]]
[[Category: Membrane]]
[[Category: Metal-binding]]
[[Category: Polymorphism]]
[[Category: Rossmann fold]]
[[Category: Secreted]]
[[Category: Semi-closed conformation]]
[[Category: Signal-anchor]]
[[Category: Transferase]]
[[Category: Transmembrane]]

Latest revision as of 07:54, 6 September 2023

Crystal structure of the Fucosylgalactoside alpha N-acetylgalactosaminyltransferase (GTA, cisAB mutant L266G, G268A) in complex with a novel UDP-Gal derived inhibitor (1GW)

3ioi, resolution 1.45Å

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