5jpo

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Current revision (19:01, 20 September 2023) (edit) (undo)
 
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<StructureSection load='5jpo' size='340' side='right'caption='[[5jpo]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='5jpo' size='340' side='right'caption='[[5jpo]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5jpo]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JPO OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5JPO FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5jpo]] is a 5 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=5JPO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JPO 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></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]] 1.998&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EEF1G, EF1G, PRO1608 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), EEF1D, EF1D ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5jpo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jpo OCA], [http://pdbe.org/5jpo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jpo RCSB], [http://www.ebi.ac.uk/pdbsum/5jpo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jpo 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=5jpo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jpo OCA], [https://pdbe.org/5jpo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jpo RCSB], [https://www.ebi.ac.uk/pdbsum/5jpo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jpo ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/EF1G_HUMAN EF1G_HUMAN]] Probably plays a role in anchoring the complex to other cellular components. [[http://www.uniprot.org/uniprot/EF1D_HUMAN EF1D_HUMAN]] Isoform 1: EF-1-beta and EF-1-delta stimulate the exchange of GDP bound to EF-1-alpha to GTP, regenerating EF-1-alpha for another round of transfer of aminoacyl-tRNAs to the ribosome. Isoform 2: Regulates induction of heat-shock-responsive genes through association with heat shock transcription factors and direct DNA-binding at heat shock promoter elements (HSE).
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[https://www.uniprot.org/uniprot/EF1G_HUMAN EF1G_HUMAN] Probably plays a role in anchoring the complex to other cellular components.
==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Choi, Y S]]
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[[Category: Choi YS]]
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[[Category: Kang, B S]]
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[[Category: Kang BS]]
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[[Category: Eef1b]]
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[[Category: Elongation factor 1b]]
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[[Category: Translation]]
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Current revision

Complex structure of human elongation factor 1B gamma GST-liked domain and delta N-terminal domain

PDB ID 5jpo

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