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3o5w

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Current revision (16:54, 1 November 2023) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3o5w]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Viscum_album Viscum album]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O5W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O5W FirstGlance]. <br>
<table><tr><td colspan='2'>[[3o5w]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Viscum_album Viscum album]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O5W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O5W FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=H35:N-(FURAN-2-YLMETHYL)-7H-PURIN-6-AMINE'>H35</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.7&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1m2t|1m2t]], [[2r9k|2r9k]], [[3d7w|3d7w]]</div></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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=H35:N-(FURAN-2-YLMETHYL)-7H-PURIN-6-AMINE'>H35</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PRD_900017:triacetyl-beta-chitotriose'>PRD_900017</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/rRNA_N-glycosylase rRNA N-glycosylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.22 3.2.2.22] </span></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=3o5w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o5w OCA], [https://pdbe.org/3o5w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o5w RCSB], [https://www.ebi.ac.uk/pdbsum/3o5w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o5w 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=3o5w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o5w OCA], [https://pdbe.org/3o5w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o5w RCSB], [https://www.ebi.ac.uk/pdbsum/3o5w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o5w ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/ML1_VISAL ML1_VISAL]] The A chain is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits by removing adenine from position 4,324 of 28S rRNA. The B chain binds to cell receptors and probably facilitates the entry into the cell of the A chain; B chains are also responsible for cell agglutination (lectin activity). Inhibits growth of the human tumor cell line Molt4.<ref>PMID:15182350</ref> <ref>PMID:15001393</ref> <ref>PMID:1450445</ref>
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[https://www.uniprot.org/uniprot/ML1_VISAL ML1_VISAL] The A chain is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits by removing adenine from position 4,324 of 28S rRNA. The B chain binds to cell receptors and probably facilitates the entry into the cell of the A chain; B chains are also responsible for cell agglutination (lectin activity). Inhibits growth of the human tumor cell line Molt4.<ref>PMID:15182350</ref> <ref>PMID:15001393</ref> <ref>PMID:1450445</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Viscum album]]
[[Category: Viscum album]]
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[[Category: RRNA N-glycosylase]]
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[[Category: Barciszewski J]]
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[[Category: Barciszewski, J]]
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[[Category: Betzel C]]
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[[Category: Betzel, C]]
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[[Category: Malecki PH]]
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[[Category: Malecki, P H]]
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[[Category: Meyer A]]
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[[Category: Meyer, A]]
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[[Category: Rypniewski W]]
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[[Category: Rypniewski, W]]
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[[Category: Szymanski M]]
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[[Category: Szymanski, M]]
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[[Category: Active site]]
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[[Category: Cytokinin]]
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[[Category: Hydrolase]]
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[[Category: Kinetin]]
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[[Category: Microgravity]]
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[[Category: Ribosome inactivating protein]]
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Current revision

Binding of kinetin in the active site of mistletoe lectin I

PDB ID 3o5w

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