3ty9

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==Crystal Structure of C. Thermocellum PNKP Ligase Domain AMP-Adenylate==
==Crystal Structure of C. Thermocellum PNKP Ligase Domain AMP-Adenylate==
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<StructureSection load='3ty9' size='340' side='right' caption='[[3ty9]], [[Resolution|resolution]] 3.12&Aring;' scene=''>
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<StructureSection load='3ty9' size='340' side='right'caption='[[3ty9]], [[Resolution|resolution]] 3.12&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3ty9]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Clostridium_thermocellum Clostridium thermocellum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TY9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TY9 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3ty9]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Acetivibrio_thermocellus_ATCC_27405 Acetivibrio thermocellus ATCC 27405]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TY9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TY9 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene><br>
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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]] 3.12&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ty5|3ty5]], [[3ty8|3ty8]]</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=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene></td></tr>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Cthe_2768 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1515 Clostridium thermocellum])</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=3ty9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ty9 OCA], [https://pdbe.org/3ty9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ty9 RCSB], [https://www.ebi.ac.uk/pdbsum/3ty9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ty9 ProSAT]</span></td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RNA_ligase_(ATP) RNA ligase (ATP)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.5.1.3 6.5.1.3] </span></td></tr>
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</table>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ty9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ty9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ty9 RCSB], [http://www.ebi.ac.uk/pdbsum/3ty9 PDBsum]</span></td></tr>
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== Function ==
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<table>
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[https://www.uniprot.org/uniprot/A3DJ38_ACET2 A3DJ38_ACET2]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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The adenylyltransferase domain of bacterial Pnkp defines a unique RNA ligase family.,Smith P, Wang LK, Nair PA, Shuman S Proc Natl Acad Sci U S A. 2012 Feb 14;109(7):2296-301. Epub 2012 Jan 27. PMID:22308407<ref>PMID:22308407</ref>
The adenylyltransferase domain of bacterial Pnkp defines a unique RNA ligase family.,Smith P, Wang LK, Nair PA, Shuman S Proc Natl Acad Sci U S A. 2012 Feb 14;109(7):2296-301. Epub 2012 Jan 27. PMID:22308407<ref>PMID:22308407</ref>
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 3ty9" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Clostridium thermocellum]]
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[[Category: Acetivibrio thermocellus ATCC 27405]]
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[[Category: Shuman, S.]]
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[[Category: Large Structures]]
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[[Category: Smith, P.]]
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[[Category: Shuman S]]
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[[Category: Wang, L.]]
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[[Category: Smith P]]
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[[Category: Adenylyltransferase]]
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[[Category: Wang L]]
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[[Category: Dna ligase/mrna capping enzyme]]
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[[Category: Hen1]]
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[[Category: Rna ligase]]
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[[Category: Transferase]]
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Current revision

Crystal Structure of C. Thermocellum PNKP Ligase Domain AMP-Adenylate

PDB ID 3ty9

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