7wo3 - Revision history

OCA at 17:42, 29 November 2023

2023-11-29T17:42:57Z

←Older revision		Revision as of 17:42, 29 November 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[7wo3]] 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=7WO3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WO3 FirstGlance]. <br>		<table><tr><td colspan='2'>[[7wo3]] 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=7WO3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WO3 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=59S:(2S)-2-[[(2S)-2-[[(E)-3-(4-methoxyphenyl)prop-2-enoyl]amino]-3-methyl-butanoyl]amino]-4-methyl-N-[(2S)-1-oxidanylidene-3-[(3S)-2-oxidanylidenepiperidin-3-yl]propan-2-yl]pentanamide'>59S</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]] 2.01Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=59S:(2S)-2-[[(2S)-2-[[(E)-3-(4-methoxyphenyl)prop-2-enoyl]amino]-3-methyl-butanoyl]amino]-4-methyl-N-[(2S)-1-oxidanylidene-3-[(3S)-2-oxidanylidenepiperidin-3-yl]propan-2-yl]pentanamide'>59S</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=7wo3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wo3 OCA], [https://pdbe.org/7wo3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wo3 RCSB], [https://www.ebi.ac.uk/pdbsum/7wo3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wo3 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=7wo3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wo3 OCA], [https://pdbe.org/7wo3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wo3 RCSB], [https://www.ebi.ac.uk/pdbsum/7wo3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wo3 ProSAT]</span></td></tr>
	</table>		</table>

OCA at 17:12, 26 April 2023

2023-04-26T17:12:13Z

←Older revision		Revision as of 17:12, 26 April 2023
Line 3:		Line 3:
	<StructureSection load='7wo3' size='340' side='right'caption='[[7wo3]], [[Resolution\|resolution]] 2.01Å' scene=''>		<StructureSection load='7wo3' size='340' side='right'caption='[[7wo3]], [[Resolution\|resolution]] 2.01Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[7wo3]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7WO3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WO3 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[7wo3]] 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=7WO3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WO3 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=59S:(2S)-2-[[(2S)-2-[[(E)-3-(4-methoxyphenyl)prop-2-enoyl]amino]-3-methyl-butanoyl]amino]-4-methyl-N-[(2S)-1-oxidanylidene-3-[(3S)-2-oxidanylidenepiperidin-3-yl]propan-2-yl]pentanamide'>59S</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=59S:(2S)-2-[[(2S)-2-[[(E)-3-(4-methoxyphenyl)prop-2-enoyl]amino]-3-methyl-butanoyl]amino]-4-methyl-N-[(2S)-1-oxidanylidene-3-[(3S)-2-oxidanylidenepiperidin-3-yl]propan-2-yl]pentanamide'>59S</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/SARS_coronavirus_main_proteinase SARS coronavirus main proteinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.69 3.4.22.69] </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=7wo3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wo3 OCA], [https://pdbe.org/7wo3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wo3 RCSB], [https://www.ebi.ac.uk/pdbsum/7wo3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wo3 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=7wo3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wo3 OCA], [https://pdbe.org/7wo3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wo3 RCSB], [https://www.ebi.ac.uk/pdbsum/7wo3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wo3 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/~~R1A_SARS2 R1A_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]. Also able to bind an ADP-ribose-1''-phosphate (ADRP).[UniProtKB:P0C6X7] 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]	+	[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 ==
		+	As the etiological agent for the coronavirus disease 2019, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) challenges the ongoing efforts of vaccine development and drug design. Due to the accumulating cases of breakthrough infections, there are urgent needs for broad-spectrum antiviral medicines. Here, we designed and examined five new tetrapeptidomimetic anti-SARS-CoV-2 inhibitors targeting the 3C-Like protease (3CL(Pro)), which is highly conserved among coronaviruses and essential for viral replications. We significantly improved the efficacy of a ketoamide lead compound based on high-resolution co-crystal structures, all-atom simulations, and binding energy calculations. The inhibitors successfully engaged the catalytic dyad histidine residue (H41) of 3CLPro as designed, and they exhibited nanomolar inhibitory capacity as well as mitigated the viral loads of SARS-CoV-2 in cellular assays. As a widely applicable design principle, our results revealed that the potencies of 3CL(Pro)-specific drug candidates were determined by the interplay between 3CL(Pro) H41 residue and the peptidomimetic inhibitors.
		+
		+	Discovery of SARS-CoV-2 3CL(Pro) Peptidomimetic Inhibitors through the Catalytic Dyad Histidine-Specific Protein-Ligand Interactions.,Wang Y, Xu B, Ma S, Wang H, Shang L, Zhu C, Ye S Int J Mol Sci. 2022 Feb 21;23(4):2392. doi: 10.3390/ijms23042392. PMID:35216507<ref>PMID:35216507</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 7wo3" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~SARS~~ coronavirus ~~main proteinase~~]]	+	[[Category: Severe acute respiratory syndrome coronavirus 2]]
-	[[Category: Wang, Y]]	+	[[Category: Wang Y]]
-	[[Category: Ye, S]]	+	[[Category: Ye S]]
-	~~[[Category: Sars-cov-2 3clpro]]~~	+
-	~~[[Category: Viral protein~~]]	+

OCA at 11:58, 27 April 2022

2022-04-27T11:58:19Z

←Older revision		Revision as of 11:58, 27 April 2022
Line 1:		Line 1:

	==SARS-CoV-2 3CLpro==		==SARS-CoV-2 3CLpro==
-	<StructureSection load='7wo3' size='340' side='right'caption='[[7wo3]]' scene=''>	+	<StructureSection load='7wo3' size='340' side='right'caption='[[7wo3]], [[Resolution\|resolution]] 2.01Å' 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=7WO3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WO3 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[7wo3]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7WO3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WO3 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=7wo3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wo3 OCA], [https://pdbe.org/7wo3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wo3 RCSB], [https://www.ebi.ac.uk/pdbsum/7wo3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wo3 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=59S:(2S)-2-[[(2S)-2-[[(E)-3-(4-methoxyphenyl)prop-2-enoyl]amino]-3-methyl-butanoyl]amino]-4-methyl-N-[(2S)-1-oxidanylidene-3-[(3S)-2-oxidanylidenepiperidin-3-yl]propan-2-yl]pentanamide'>59S</scene></td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/SARS_coronavirus_main_proteinase SARS coronavirus main proteinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.69 3.4.22.69] </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=7wo3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wo3 OCA], [https://pdbe.org/7wo3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wo3 RCSB], [https://www.ebi.ac.uk/pdbsum/7wo3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wo3 ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[https://www.uniprot.org/uniprot/R1A_SARS2 R1A_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]. Also able to bind an ADP-ribose-1''-phosphate (ADRP).[UniProtKB:P0C6X7] 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]
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Wang Y]]	+	[[Category: SARS coronavirus main proteinase]]
-	[[Category: Ye S]]	+	[[Category: Wang, Y]]
		+	[[Category: Ye, S]]
		+	[[Category: Sars-cov-2 3clpro]]
		+	[[Category: Viral protein]]

OCA at 09:49, 13 April 2022

2022-04-13T09:49:32Z

←Older revision		Revision as of 09:49, 13 April 2022
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 7wo3 ~~is ON HOLD until Paper Publication~~	+	==SARS-CoV-2 3CLpro==
-		+	<StructureSection load='7wo3' size='340' side='right'caption='[[7wo3]]' scene=''>
-	~~Authors~~: ~~Wang~~, Y., Ye, S.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7WO3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WO3 FirstGlance]. <br>
-	~~Description~~: ~~SARS~~-~~CoV-2 3CLpro~~	+	</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=7wo3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wo3 OCA], [https://pdbe.org/7wo3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wo3 RCSB], [https://www.ebi.ac.uk/pdbsum/7wo3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wo3 ProSAT]</span></td></tr>
-	[[Category: ~~Unreleased~~ Structures]]	+	</table>
-	[[Category: Wang, Y]]	+	__TOC__
-	[[Category: Ye, S]]	+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Wang Y]]
		+	[[Category: Ye S]]

OCA at 05:01, 9 March 2022

2022-03-09T05:01:21Z

←Older revision		Revision as of 05:01, 9 March 2022
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 7wo3 is ON HOLD	+	The entry 7wo3 is ON HOLD until Paper Publication

	Authors: Wang, Y., Ye, S.		Authors: Wang, Y., Ye, S.
Line 7:		Line 7:
	Description: SARS-CoV-2 3CLpro		Description: SARS-CoV-2 3CLpro
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: Ye, S]]
	[[Category: Wang, Y]]		[[Category: Wang, Y]]
		+	[[Category: Ye, S]]

OCA at 06:26, 9 February 2022

2022-02-09T06:26:44Z

←Older revision		Revision as of 06:26, 9 February 2022
Line 3:		Line 3:
	The entry 7wo3 is ON HOLD		The entry 7wo3 is ON HOLD

-	Authors: ~~Yaxin~~, W., ~~Sheng~~, Y.	+	Authors: Wang, Y., Ye, S.

	Description: SARS-CoV-2 3CLpro		Description: SARS-CoV-2 3CLpro
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: ~~Yaxin~~, W]]	+	[[Category: Ye, S]]
-	[[Category: ~~Sheng~~, Y]]	+	[[Category: Wang, Y]]

OCA: Protected "7wo3" [edit=sysop:move=sysop]

2022-01-27T05:48:37Z

Protected "7wo3" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:48, 27 January 2022

OCA: New page: '''Unreleased structure''' The entry 7wo3 is ON HOLD Authors: Yaxin, W., Sheng, Y. Description: SARS-CoV-2 3CLpro Category: Unreleased Structures Category: Yaxin, W [[Category:...

2022-01-27T05:48:36Z

New page: '''Unreleased structure''' The entry 7wo3 is ON HOLD Authors: Yaxin, W., Sheng, Y. Description: SARS-CoV-2 3CLpro Category: Unreleased Structures Category: Yaxin, W [[Category:...

New page

'''Unreleased structure'''

The entry 7wo3 is ON HOLD

Authors: Yaxin, W., Sheng, Y.

Description: SARS-CoV-2 3CLpro
[[Category: Unreleased Structures]]
[[Category: Yaxin, W]]
[[Category: Sheng, Y]]