7ar5

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<StructureSection load='7ar5' size='340' side='right'caption='[[7ar5]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
<StructureSection load='7ar5' size='340' side='right'caption='[[7ar5]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[7ar5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/2019-ncov 2019-ncov]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7AR5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7AR5 FirstGlance]. <br>
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7AR5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7AR5 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=DMS:DIMETHYL+SULFOXIDE'>DMS</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]] 1.4&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></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=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene></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;'>[[6ynq|6ynq]], [[6yt8|6yt8]], [[6yz6|6yz6]], [[7a1u|7a1u]], [[6yvf|6yvf]], [[7abu|7abu]], [[7adw|7adw]], [[7aga|7aga]], [[7af0|7af0]], [[7aha|7aha]], [[7aku|7aku]], [[7amj|7amj]], [[7aqi|7aqi]], [[7aph|7aph]], [[7aqe|7aqe]], [[7ap6|7ap6]], [[7aol|7aol]], [[7ak4|7ak4]], [[7ans|7ans]], [[7aqj|7aqj]]</div></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=7ar5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ar5 OCA], [https://pdbe.org/7ar5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ar5 RCSB], [https://www.ebi.ac.uk/pdbsum/7ar5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ar5 ProSAT]</span></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rep, 1a-1b ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2697049 2019-nCoV])</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=7ar5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ar5 OCA], [http://pdbe.org/7ar5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7ar5 RCSB], [http://www.ebi.ac.uk/pdbsum/7ar5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7ar5 ProSAT]</span></td></tr>
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</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/R1AB_SARS2 R1AB_SARS2]] Multifunctional protein involved in the transcription and replication of viral RNAs. Contains the proteinases responsible for the cleavages of the polyprotein.[UniProtKB:P0C6X7] Inhibits host translation by interacting with the 40S ribosomal subunit. The nsp1-40S ribosome complex further induces an endonucleolytic cleavage near the 5'UTR of host mRNAs, targeting them for degradation. Viral mRNAs are not susceptible to nsp1-mediated endonucleolytic RNA cleavage thanks to the presence of a 5'-end leader sequence and are therefore protected from degradation. By suppressing host gene expression, nsp1 facilitates efficient viral gene expression in infected cells and evasion from host immune response.[UniProtKB:P0C6X7] May play a role in the modulation of host cell survival signaling pathway by interacting with host PHB and PHB2. Indeed, these two proteins play a role in maintaining the functional integrity of the mitochondria and protecting cells from various stresses.[UniProtKB:P0C6X7] Responsible for the cleavages located at the N-terminus of the replicase polyprotein. In addition, PL-PRO possesses a deubiquitinating/deISGylating activity and processes both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains from cellular substrates. Participates together with nsp4 in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication. Antagonizes innate immune induction of type I interferon by blocking the phosphorylation, dimerization and subsequent nuclear translocation of host IRF3. Prevents also host NF-kappa-B signaling.[UniProtKB:P0C6X7] Participates in the assembly of virally-induced cytoplasmic double-membrane vesicles necessary for viral replication.[UniProtKB:P0C6X7] Cleaves the C-terminus of replicase polyprotein at 11 sites. Recognizes substrates containing the core sequence [ILMVF]-Q-|-[SGACN] (PubMed:32198291). Also able to bind an ADP-ribose-1''-phosphate (ADRP).[UniProtKB:P0C6X7]<ref>PMID:32198291</ref> Plays a role in the initial induction of autophagosomes from host reticulum endoplasmic. Later, limits the expansion of these phagosomes that are no longer able to deliver viral components to lysosomes.[UniProtKB:P0C6X7] Forms a hexadecamer with nsp8 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers.[UniProtKB:P0C6X7] Forms a hexadecamer with nsp7 (8 subunits of each) that may participate in viral replication by acting as a primase. Alternatively, may synthesize substantially longer products than oligonucleotide primers.[UniProtKB:P0C6X7] May participate in viral replication by acting as a ssRNA-binding protein.[UniProtKB:P0C6X7] Plays a pivotal role in viral transcription by stimulating both nsp14 3'-5' exoribonuclease and nsp16 2'-O-methyltransferase activities. Therefore plays an essential role in viral mRNAs cap methylation.[UniProtKB:P0C6X7] Responsible for replication and transcription of the viral RNA genome.[UniProtKB:P0C6X7] Multi-functional protein with a zinc-binding domain in N-terminus displaying RNA and DNA duplex-unwinding activities with 5' to 3' polarity. Activity of helicase is dependent on magnesium.[UniProtKB:P0C6X7] Enzyme possessing two different activities: an exoribonuclease activity acting on both ssRNA and dsRNA in a 3' to 5' direction and a N7-guanine methyltransferase activity. Acts as a proofreading exoribonuclease for RNA replication, thereby lowering The sensitivity of the virus to RNA mutagens.[UniProtKB:P0C6X7] Mn(2+)-dependent, uridylate-specific enzyme, which leaves 2'-3'-cyclic phosphates 5' to the cleaved bond.[UniProtKB:P0C6X7] Methyltransferase that mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs. N7-methyl guanosine cap is a prerequisite for binding of nsp16. Therefore plays an essential role in viral mRNAs cap methylation which is essential to evade immune system.[UniProtKB:P0C6X7]
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==See Also==
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== References ==
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*[[Virus protease 3D structures|Virus protease 3D structures]]
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: 2019-ncov]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Andaleeb, H]]
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[[Category: Alves Franca B]]
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[[Category: Awel, S]]
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[[Category: Andaleeb H]]
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[[Category: Beck, T]]
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[[Category: Awel S]]
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[[Category: Betzel, C]]
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[[Category: Beck T]]
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[[Category: Boger, J]]
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[[Category: Betzel C]]
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[[Category: Brehm, W]]
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[[Category: Boger J]]
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[[Category: Brognaro, H]]
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[[Category: Brehm W]]
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[[Category: Chapman, H N]]
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[[Category: Brognaro H]]
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[[Category: Chari, A]]
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[[Category: Chapman HN]]
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[[Category: Domaracky, M]]
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[[Category: Chari A]]
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[[Category: Doyle, J J]]
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[[Category: Domaracky M]]
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[[Category: Dunkel, I]]
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[[Category: Doyle JJ]]
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[[Category: Ehrt, C]]
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[[Category: Dunkel I]]
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[[Category: Ellinger, B]]
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[[Category: Ehrt C]]
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[[Category: Esperanza, G Pena]]
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[[Category: Ellinger B]]
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[[Category: Falke, S]]
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[[Category: Falke S]]
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[[Category: Feiler, C]]
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[[Category: Feiler C]]
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[[Category: Fischer, P]]
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[[Category: Fernandez Garcia Y]]
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[[Category: Fleckenstein, H]]
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[[Category: Fischer P]]
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[[Category: Franca, B Alves]]
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[[Category: Fleckenstein H]]
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[[Category: Galchenkova, M]]
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[[Category: Galchenkova M]]
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[[Category: Garcia, Y Fernandez]]
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[[Category: Gelisio L]]
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[[Category: Gelisio, L]]
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[[Category: Gevorkov Y]]
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[[Category: Gevorkov, Y]]
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[[Category: Ginn H]]
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[[Category: Ginn, H]]
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[[Category: Giseler H]]
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[[Category: Giseler, H]]
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[[Category: Gribbon P]]
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[[Category: Gribbon, P]]
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[[Category: Groessler M]]
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[[Category: Groessler, M]]
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[[Category: Guenther S]]
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[[Category: Guenther, S]]
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[[Category: Hakanpaeae J]]
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[[Category: Hakanpaeae, J]]
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[[Category: Han H]]
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[[Category: Han, H]]
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[[Category: Hennicke V]]
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[[Category: Hennicke, V]]
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[[Category: Hilgenfeld R]]
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[[Category: Hilgenfeld, R]]
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[[Category: Hinrichs W]]
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[[Category: Hinrichs, W]]
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[[Category: Knoska J]]
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[[Category: Knoska, J]]
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[[Category: Koua F]]
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[[Category: Koua, F]]
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[[Category: Kuzikov M]]
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[[Category: Kuzikov, M]]
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[[Category: Lane TJ]]
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[[Category: Lane, T J]]
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[[Category: Li C]]
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[[Category: Li, C]]
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[[Category: Lieske J]]
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[[Category: Lieske, J]]
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[[Category: Lorenzen K]]
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[[Category: Lorenzen, K]]
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[[Category: Meents A]]
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[[Category: Mashour, A Rahmani]]
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[[Category: Mehrabi P]]
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[[Category: Meents, A]]
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[[Category: Meier S]]
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[[Category: Mehrabi, P]]
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[[Category: Melo D]]
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[[Category: Meier, S]]
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[[Category: Meyer J]]
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[[Category: Melo, D]]
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[[Category: Noei H]]
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[[Category: Meyer, J]]
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[[Category: Norton-Baker B]]
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[[Category: Noei, H]]
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[[Category: Oberthuer D]]
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[[Category: Norton-Baker, B]]
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[[Category: Paulraj LX]]
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[[Category: Oberthuer, D]]
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[[Category: Pearson A]]
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[[Category: Paulraj, L X]]
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[[Category: Peck A]]
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[[Category: Pearson, A]]
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[[Category: Pena Esperanza G]]
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[[Category: Peck, A]]
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[[Category: Perbandt M]]
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[[Category: Perbandt, M]]
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[[Category: Pletzer-Zelgert J]]
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[[Category: Pletzer-Zelgert, J]]
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[[Category: Rahmani Mashour A]]
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[[Category: Rarey, M]]
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[[Category: Rarey M]]
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[[Category: Reinke, P]]
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[[Category: Reinke P]]
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[[Category: Saouane, S]]
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[[Category: Saouane S]]
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[[Category: Schmidt, C]]
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[[Category: Schmidt C]]
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[[Category: Schubert, R]]
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[[Category: Schubert R]]
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[[Category: Schulz, E C]]
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[[Category: Schulz EC]]
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[[Category: Schwinzer, M]]
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[[Category: Schwinzer M]]
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[[Category: Seychell, B]]
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[[Category: Seychell B]]
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[[Category: Tidow, H]]
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[[Category: Tidow H]]
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[[Category: Tolstikova, A]]
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[[Category: Tolstikova A]]
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[[Category: Trost, F]]
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[[Category: Trost F]]
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[[Category: Turk, D]]
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[[Category: Turk D]]
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[[Category: Ullah, N]]
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[[Category: Ullah N]]
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[[Category: Weiss, M]]
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[[Category: Weiss M]]
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[[Category: Werner, N]]
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[[Category: Werner N]]
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[[Category: White, T A]]
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[[Category: White TA]]
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[[Category: Wolf, M]]
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[[Category: Wolf M]]
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[[Category: Wollenhaupt, J]]
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[[Category: Wollenhaupt J]]
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[[Category: Yefanov, O]]
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[[Category: Yefanov O]]
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[[Category: Zaliani, A]]
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[[Category: Zaliani A]]
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[[Category: Zhang, L]]
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[[Category: Zhang L]]
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[[Category: Covid-19]]
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[[Category: Hydrolase]]
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[[Category: Mpro]]
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[[Category: Peptide binding protein]]
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[[Category: Sars-cov-2]]
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[[Category: Virus protease]]
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Current revision

Structure of apo SARS-CoV-2 Main Protease with small beta angle, space group C2.

PDB ID 7ar5

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

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