7oru - Revision history

OCA at 12:55, 1 February 2024

2024-02-01T12:55:15Z

← Older revision		Revision as of 12:55, 1 February 2024
Line 3:		Line 3:
	<StructureSection load='7oru' size='340' side='right'caption='[[7oru]], [[Resolution\|resolution]] 1.67Å' scene=''>		<StructureSection load='7oru' size='340' side='right'caption='[[7oru]], [[Resolution\|resolution]] 1.67Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[7oru]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ORU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ORU FirstGlance]. <br>		<table><tr><td colspan='2'>[[7oru]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Severe_acute_respiratory_syndrome_coronavirus_2 Severe acute respiratory syndrome coronavirus 2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ORU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ORU FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2AQ:QUINOLIN-2-AMINE'>2AQ</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.67Å</td></tr>
			<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2AQ:QUINOLIN-2-AMINE'>2AQ</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7oru FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7oru OCA], [https://pdbe.org/7oru PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7oru RCSB], [https://www.ebi.ac.uk/pdbsum/7oru PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7oru ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7oru FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7oru OCA], [https://pdbe.org/7oru PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7oru RCSB], [https://www.ebi.ac.uk/pdbsum/7oru PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7oru ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://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]		[https://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]
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 26:		Line 27:
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Dong, D]]		[[Category: Severe acute respiratory syndrome coronavirus 2]]
	[[Category: Fisher~~, S Z~~]]		[[Category: Dong D]]
	[[Category: Knecht, W]]		[[Category: Fisher SZ]]
	[[Category: Kozielski, F]]		[[Category: Knecht W]]
	[[Category: Krojer, T]]		[[Category: Kozielski F]]
	[[Category: Lou, J]]		[[Category: Krojer T]]
	[[Category: Nyblom, M]]		[[Category: Lou J]]
	[[Category: Rogstam, A]]		[[Category: Nyblom M]]
	[[Category: Sele, C]]		[[Category: Rogstam A]]
	[[Category: Shi, X]]		[[Category: Sele C]]
	[[Category: Talibov~~, V O~~]]		[[Category: Shi X]]
	[[Category: Wang, Q]]		[[Category: Talibov VO]]
	~~[[Category: Complex]]~~		[[Category: Wang Q]]
	~~[[Category: Fragment]]~~
	~~[[Category: Small molecule]]~~
	~~[[Category: Viral protein~~]]

OCA at 08:41, 23 February 2022

2022-02-23T08:41:53Z

← Older revision		Revision as of 08:41, 23 February 2022
Line 1:		Line 1:

	==Non-structural protein 10 (nsp10) from SARS CoV-2 in complex with fragment VT00221==		==Non-structural protein 10 (nsp10) from SARS CoV-2 in complex with fragment VT00221==
	<StructureSection load='7oru' size='340' side='right'caption='[[7oru]]' scene=''>		<StructureSection load='7oru' size='340' side='right'caption='[[7oru]], [[Resolution\|resolution]] 1.67Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ORU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ORU FirstGlance]. <br>		<table><tr><td colspan='2'>[[7oru]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ORU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ORU FirstGlance]. <br>
	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7oru FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7oru OCA], [https://pdbe.org/7oru PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7oru RCSB], [https://www.ebi.ac.uk/pdbsum/7oru PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7oru ProSAT]</span></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2AQ:QUINOLIN-2-AMINE'>2AQ</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
			<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7oru FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7oru OCA], [https://pdbe.org/7oru PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7oru RCSB], [https://www.ebi.ac.uk/pdbsum/7oru PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7oru ProSAT]</span></td></tr>
	</table>		</table>
			== Function ==
			[[https://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]
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Since the emergence of SARS-CoV-2 in 2019, Covid-19 has developed into a serious threat to our health, social and economic systems. Although vaccines have been developed in a tour-de-force and are now increasingly available, repurposing of existing drugs has been less successful. There is a clear need to develop new drugs against SARS-CoV-2 that can also be used against future coronavirus infections. Non-structural protein 10 (nsp10) is a conserved stimulator of two enzymes crucial for viral replication, nsp14 and nsp16, exhibiting exoribonuclease and methyltransferase activities. Interfering with RNA proofreading or RNA cap formation represents intervention strategies to inhibit replication. We applied fragment-based screening using nano differential scanning fluorometry and X-ray crystallography to identify ligands targeting SARS-CoV-2 nsp10. We identified four fragments located in two distinct sites: one can be modelled to where it would be located in the nsp14-nsp10 complex interface and the other in the nsp16-nsp10 complex interface. Microscale thermophoresis (MST) experiments were used to quantify fragment affinities for nsp10. Additionally, we showed by MST that the interaction by nsp14 and 10 is weak and thereby that complex formation could be disrupted by small molecules. The fragments will serve as starting points for the development of more potent analogues using fragment growing techniques and structure-based drug design.

			Identification of fragments binding to SARS-CoV-2 nsp10 reveals ligand-binding sites in conserved interfaces between nsp10 and nsp14/nsp16.,Kozielski F, Sele C, Talibov VO, Lou J, Dong D, Wang Q, Shi X, Nyblom M, Rogstam A, Krojer T, Fisher Z, Knecht W RSC Chem Biol. 2021 Oct 6;3(1):44-55. doi: 10.1039/d1cb00135c. eCollection 2022, Jan 5. PMID:35128408<ref>PMID:35128408</ref>

			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
			<div class="pdbe-citations 7oru" style="background-color:#fffaf0;"></div>

			==See Also==
			*[[Nonstructural protein 3D structures\|Nonstructural protein 3D structures]]
			== References ==
			<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Dong D]]		[[Category: Dong, D]]
	[[Category: Fisher SZ]]		[[Category: Fisher, S Z]]
	[[Category: Knecht W]]		[[Category: Knecht, W]]
	[[Category: Kozielski F]]		[[Category: Kozielski, F]]
	[[Category: Krojer T]]		[[Category: Krojer, T]]
	[[Category: Lou J]]		[[Category: Lou, J]]
	[[Category: Nyblom M]]		[[Category: Nyblom, M]]
	[[Category: Rogstam A]]		[[Category: Rogstam, A]]
	[[Category: Sele C]]		[[Category: Sele, C]]
	[[Category: Shi X]]		[[Category: Shi, X]]
	[[Category: Talibov VO]]		[[Category: Talibov, V O]]
	[[Category: Wang Q]]		[[Category: Wang, Q]]
			[[Category: Complex]]
			[[Category: Fragment]]
			[[Category: Small molecule]]
			[[Category: Viral protein]]

OCA at 16:30, 20 October 2021

2021-10-20T16:30:45Z

← Older revision		Revision as of 16:30, 20 October 2021
Line 1:		Line 1:
	~~'''Unreleased structure'''~~

	~~The entry~~ 7oru is ~~ON HOLD until Paper Publication~~		==Non-structural protein 10 (nsp10) from SARS CoV-2 in complex with fragment VT00221==
			<StructureSection load='7oru' size='340' side='right'caption='[[7oru]]' scene=''>
	~~Authors~~: ~~Talibov, V~~.O., ~~Kozielski, F~~.~~, Sele, C~~.~~, Lou, J~~., ~~Dong, D~~., ~~Wang, Q~~.~~, Shi, X~~.~~, Nyblom, M~~., ~~Rogstam, A~~.~~, Krojer, T~~.~~, Knecht, W~~., ~~Fisher, S~~.Z.		== Structural highlights ==
			<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ORU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ORU FirstGlance]. <br>
	~~Description: Non-structural protein 10 (nsp10) from SARS CoV-2 in complex with fragment VT00221~~		</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7oru FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7oru OCA], [https://pdbe.org/7oru PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7oru RCSB], [https://www.ebi.ac.uk/pdbsum/7oru PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7oru ProSAT]</span></td></tr>
	[[Category: ~~Unreleased~~ Structures]]		</table>
	[[Category: ~~Talibov, V.O~~]]		__TOC__
	[[Category: ~~Shi, X~~]]		</StructureSection>
	[[Category: ~~Rogstam, A~~]]		[[Category: Large Structures]]
	[[Category: ~~Dong, D~~]]		[[Category: Dong D]]
	[[Category: ~~Fisher, S.Z~~]]		[[Category: Fisher SZ]]
	[[Category: ~~Knecht, W~~]]		[[Category: Knecht W]]
	[[Category: ~~Sele, C~~]]		[[Category: Kozielski F]]
	[[Category: ~~Nyblom, M~~]]		[[Category: Krojer T]]
	[[Category: ~~Lou, J~~]]		[[Category: Lou J]]
	[[Category: ~~Kozielski, F~~]]		[[Category: Nyblom M]]
	[[Category: ~~Wang, Q~~]]		[[Category: Rogstam A]]
	[[Category: ~~Krojer, T~~]]		[[Category: Sele C]]
			[[Category: Shi X]]
			[[Category: Talibov VO]]
			[[Category: Wang Q]]

OCA at 06:20, 25 June 2021

2021-06-25T06:20:15Z

← Older revision		Revision as of 06:20, 25 June 2021
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 7oru is ON HOLD		The entry 7oru is ON HOLD until Paper Publication

	Authors: Talibov, V.O., Kozielski, F., Sele, C., Lou, J., Dong, D., Wang, Q., Shi, X., Nyblom, M., Rogstam, A., Krojer, T., Knecht, W., Fisher, S.Z.		Authors: Talibov, V.O., Kozielski, F., Sele, C., Lou, J., Dong, D., Wang, Q., Shi, X., Nyblom, M., Rogstam, A., Krojer, T., Knecht, W., Fisher, S.Z.
Line 7:		Line 7:
	Description: Non-structural protein 10 (nsp10) from SARS CoV-2 in complex with fragment VT00221		Description: Non-structural protein 10 (nsp10) from SARS CoV-2 in complex with fragment VT00221
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
	~~[[Category: Nyblom, M]]~~
	~~[[Category: Lou, J]]~~
	~~[[Category: Kozielski, F]]~~
	[[Category: Talibov, V.O]]		[[Category: Talibov, V.O]]
	~~[[Category: Wang, Q]]~~
	[[Category: Shi, X]]		[[Category: Shi, X]]
	[[Category: Rogstam, A]]		[[Category: Rogstam, A]]
	~~[[Category: Krojer, T]]~~
	[[Category: Dong, D]]		[[Category: Dong, D]]
	[[Category: Fisher, S.Z]]		[[Category: Fisher, S.Z]]
	[[Category: Knecht, W]]		[[Category: Knecht, W]]
	[[Category: Sele, C]]		[[Category: Sele, C]]
			[[Category: Nyblom, M]]
			[[Category: Lou, J]]
			[[Category: Kozielski, F]]
			[[Category: Wang, Q]]
			[[Category: Krojer, T]]

OCA: Protected "7oru" [edit=sysop:move=sysop]

2021-06-17T13:50:45Z

Protected "7oru" [edit=sysop:move=sysop]

← Older revision	Revision as of 13:50, 17 June 2021
(No difference)

OCA: New page: '''Unreleased structure''' The entry 7oru is ON HOLD Authors: Talibov, V.O., Kozielski, F., Sele, C., Lou, J., Dong, D., Wang, Q., Shi, X., Nyblom, M., Rogstam, A., Krojer, T., Knecht, ...

2021-06-17T13:50:44Z

New page: '''Unreleased structure''' The entry 7oru is ON HOLD Authors: Talibov, V.O., Kozielski, F., Sele, C., Lou, J., Dong, D., Wang, Q., Shi, X., Nyblom, M., Rogstam, A., Krojer, T., Knecht, ...

New page

'''Unreleased structure'''

The entry 7oru is ON HOLD

Authors: Talibov, V.O., Kozielski, F., Sele, C., Lou, J., Dong, D., Wang, Q., Shi, X., Nyblom, M., Rogstam, A., Krojer, T., Knecht, W., Fisher, S.Z.

Description: Non-structural protein 10 (nsp10) from SARS CoV-2 in complex with fragment VT00221
[[Category: Unreleased Structures]]
[[Category: Nyblom, M]]
[[Category: Lou, J]]
[[Category: Kozielski, F]]
[[Category: Talibov, V.O]]
[[Category: Wang, Q]]
[[Category: Shi, X]]
[[Category: Rogstam, A]]
[[Category: Krojer, T]]
[[Category: Dong, D]]
[[Category: Fisher, S.Z]]
[[Category: Knecht, W]]
[[Category: Sele, C]]