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5v59

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==Crystal structure of catalytic fragment of human AlaRS in complex with Aze-SA==
==Crystal structure of catalytic fragment of human AlaRS in complex with Aze-SA==
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<StructureSection load='5v59' size='340' side='right' caption='[[5v59]], [[Resolution|resolution]] 2.03&Aring;' scene=''>
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<StructureSection load='5v59' size='340' side='right'caption='[[5v59]], [[Resolution|resolution]] 2.03&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5v59]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5V59 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5V59 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5v59]] 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=5V59 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5V59 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=8X1:5-O-{[(2S)-azetidine-2-carbonyl]sulfamoyl}adenosine'>8X1</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]] 2.03&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5v58|5v58]]</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=8X1:5-O-{[(2S)-azetidine-2-carbonyl]sulfamoyl}adenosine'>8X1</scene></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/Alanine--tRNA_ligase Alanine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.7 6.1.1.7] </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=5v59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v59 OCA], [https://pdbe.org/5v59 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5v59 RCSB], [https://www.ebi.ac.uk/pdbsum/5v59 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5v59 ProSAT]</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=5v59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5v59 OCA], [http://pdbe.org/5v59 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5v59 RCSB], [http://www.ebi.ac.uk/pdbsum/5v59 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5v59 ProSAT]</span></td></tr>
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</table>
</table>
== Disease ==
== Disease ==
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[[http://www.uniprot.org/uniprot/SYAC_HUMAN SYAC_HUMAN]] Autosomal dominant Charcot-Marie-Tooth disease type 2N. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry.
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[https://www.uniprot.org/uniprot/SYAC_HUMAN SYAC_HUMAN] Autosomal dominant Charcot-Marie-Tooth disease type 2N. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/SYAC_HUMAN SYAC_HUMAN]] Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain.[HAMAP-Rule:MF_03133]
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[https://www.uniprot.org/uniprot/SYAC_HUMAN SYAC_HUMAN] Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain.[HAMAP-Rule:MF_03133]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 5v59" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5v59" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Alanine--tRNA ligase]]
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[[Category: Homo sapiens]]
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[[Category: Schimmel, P]]
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[[Category: Large Structures]]
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[[Category: Song, Y]]
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[[Category: Schimmel P]]
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[[Category: Zhou, H]]
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[[Category: Song Y]]
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[[Category: Aminoacyl-trna synthetase]]
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[[Category: Zhou H]]
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[[Category: Ligase]]
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[[Category: Non-proteinogenic amino acid]]
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Current revision

Crystal structure of catalytic fragment of human AlaRS in complex with Aze-SA

PDB ID 5v59

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