6nya

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<StructureSection load='6nya' size='340' side='right'caption='[[6nya]], [[Resolution|resolution]] 2.06&Aring;' scene=''>
<StructureSection load='6nya' size='340' side='right'caption='[[6nya]], [[Resolution|resolution]] 2.06&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6nya]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NYA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6NYA FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6nya]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C] and [https://en.wikipedia.org/wiki/Triticum_aestivum Triticum aestivum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6NYA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6NYA 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=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.065&#8491;</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/E1_ubiquitin-activating_enzyme E1 ubiquitin-activating enzyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.2.1.45 6.2.1.45] </span></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=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=6nya FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nya OCA], [http://pdbe.org/6nya PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6nya RCSB], [http://www.ebi.ac.uk/pdbsum/6nya PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6nya ProSAT]</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=6nya FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6nya OCA], [https://pdbe.org/6nya PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6nya RCSB], [https://www.ebi.ac.uk/pdbsum/6nya PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6nya ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/UBA1_YEAST UBA1_YEAST]] Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding an ubiquitin-E1 thioester and free AMP. [[http://www.uniprot.org/uniprot/UBC3_YEAST UBC3_YEAST]] Catalyzes the covalent attachment of ubiquitin to other proteins. Capable, in vitro, to ubiquitinate histone H2A. Mediates the initiation of DNA replication (transition of G1 to S phase in cell cycle). Essential component of the E3 ubiquitin ligase complex SCF (SKP1-CUL1-F-box protein), which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Involved in the regulation of methionine biosynthesis genes and in the degradation of CDC6 together with CDC4 and CDC53.
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[https://www.uniprot.org/uniprot/UBA1_YEAST UBA1_YEAST] Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding an ubiquitin-E1 thioester and free AMP.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
<div class="pdbe-citations 6nya" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 6nya" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[3D structures of Ubiquitin activating enzyme|3D structures of Ubiquitin activating enzyme]]
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*[[3D structures of ubiquitin|3D structures of ubiquitin]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: E1 ubiquitin-activating enzyme]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Atkison, J H]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Olsen, S K]]
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[[Category: Triticum aestivum]]
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[[Category: Williams, K M]]
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[[Category: Atkison JH]]
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[[Category: Adenylation]]
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[[Category: Olsen SK]]
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[[Category: Atp-binding]]
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[[Category: Williams KM]]
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[[Category: Conformational change]]
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[[Category: Ligase]]
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[[Category: Ligase-transferase complex]]
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[[Category: Thioester]]
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[[Category: Thioester transfer]]
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[[Category: Transthioesterification]]
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[[Category: Ubiquitin e2-binding]]
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[[Category: Ubiquitination]]
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Current revision

Crystal Structure of ubiquitin E1 (Uba1) in complex with Ubc3 (Cdc34) and ubiquitin

PDB ID 6nya

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