7mlg - Revision history

OCA at 16:14, 18 October 2023

2023-10-18T16:14:57Z

←Older revision		Revision as of 16:14, 18 October 2023
Line 3:		Line 3:
	<StructureSection load='7mlg' size='340' side='right'caption='[[7mlg]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='7mlg' size='340' side='right'caption='[[7mlg]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[7mlg]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7MLG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7MLG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[7mlg]] 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=7MLG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7MLG FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=ZJ1:(2R)-2~~-[~~(4-tert-butylphenyl)(ethanesulfonyl)amino~~]~~-N-cyclohexyl-~~2~~-(pyridin-3-yl)acetamide'>ZJ1</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]] 2.5Å</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='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZJ1:(2R)-2-[(4-tert-butylphenyl)(ethanesulfonyl)amino]-N-cyclohexyl-2-(pyridin-3-yl)acetamide'>ZJ1</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=7mlg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7mlg OCA], [https://pdbe.org/7mlg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7mlg RCSB], [https://www.ebi.ac.uk/pdbsum/7mlg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7mlg 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=7mlg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7mlg OCA], [https://pdbe.org/7mlg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7mlg RCSB], [https://www.ebi.ac.uk/pdbsum/7mlg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7mlg 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 24:		Line 24:
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~SARS~~ coronavirus ~~main proteinase~~]]	+	[[Category: Severe acute respiratory syndrome coronavirus 2]]
-	[[Category: Hennecker, C]]	+	[[Category: Hennecker C]]
-	[[Category: Huot, M]]	+	[[Category: Huot M]]
-	[[Category: Labarre, A]]	+	[[Category: Labarre A]]
-	[[Category: Miron~~, C E~~]]	+	[[Category: Miron CE]]
-	[[Category: Mittermaier~~, A K~~]]	+	[[Category: Mittermaier AK]]
-	[[Category: Moitessier, N]]	+	[[Category: Moitessier N]]
-	[[Category: Patrascu~~, M B~~]]	+	[[Category: Patrascu MB]]
-	[[Category: Pinus, S]]	+	[[Category: Pinus S]]
-	[[Category: Rueda~~, A M~~]]	+	[[Category: Rueda AM]]
-	[[Category: Schmeing~~, T M~~]]	+	[[Category: Schmeing TM]]
-	[[Category: Sharon, I]]	+	[[Category: Sharon I]]
-	[[Category: Stille, J]]	+	[[Category: Stille J]]
-	[[Category: Tjutrins, J]]	+	[[Category: Tjutrins J]]
-	[[Category: Venegas~~, F A~~]]	+	[[Category: Venegas FA]]
-	[[Category: Vlaho, D]]	+	[[Category: Vlaho D]]
-	[[Category: Wang, G]]	+	[[Category: Wang G]]
-	~~[[Category: Covalent inhibitor]]~~	+
-	~~[[Category: Hydrolase-inhibitor complex]]~~	+
-	~~[[Category: Sars-cov-2~~]]	+

OCA at 07:38, 19 January 2022

2022-01-19T07:38:23Z

←Older revision		Revision as of 07:38, 19 January 2022
Line 1:		Line 1:

	==Crystal Structure of SARS-CoV-2 Main Protease (3CLpro/Mpro) Covalently Bound to Compound C63==		==Crystal Structure of SARS-CoV-2 Main Protease (3CLpro/Mpro) Covalently Bound to Compound C63==
-	<StructureSection load='7mlg' size='340' side='right'caption='[[7mlg]]' scene=''>	+	<StructureSection load='7mlg' size='340' side='right'caption='[[7mlg]], [[Resolution\|resolution]] 2.50Å' 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=7MLG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7MLG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[7mlg]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7MLG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7MLG 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=7mlg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7mlg OCA], [https://pdbe.org/7mlg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7mlg RCSB], [https://www.ebi.ac.uk/pdbsum/7mlg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7mlg 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=ZJ1:(2R)-2-[(4-tert-butylphenyl)(ethanesulfonyl)amino]-N-cyclohexyl-2-(pyridin-3-yl)acetamide'>ZJ1</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=7mlg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7mlg OCA], [https://pdbe.org/7mlg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7mlg RCSB], [https://www.ebi.ac.uk/pdbsum/7mlg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7mlg 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 ==
		+	Severe diseases such as the ongoing COVID-19 pandemic, as well as the previous SARS and MERS outbreaks, are the result of coronavirus infections and have demonstrated the urgent need for antiviral drugs to combat these deadly viruses. Due to its essential role in viral replication and function, 3CL(pro) (main coronaviruses cysteine-protease) has been identified as a promising target for the development of antiviral drugs. Previously reported SARS-CoV 3CL(pro) non-covalent inhibitors were used as a starting point for the development of covalent inhibitors of SARS-CoV-2 3CL(pro). We report herein our efforts in the design and synthesis of submicromolar covalent inhibitors when the enzymatic activity of the viral protease was used as a screening platform.
		+
		+	Design, synthesis and in vitro evaluation of novel SARS-CoV-2 3CL(pro) covalent inhibitors.,Stille JK, Tjutrins J, Wang G, Venegas FA, Hennecker C, Rueda AM, Sharon I, Blaine N, Miron CE, Pinus S, Labarre A, Plescia J, Burai Patrascu M, Zhang X, Wahba AS, Vlaho D, Huot MJ, Schmeing TM, Mittermaier AK, Moitessier N Eur J Med Chem. 2021 Dec 11;229:114046. doi: 10.1016/j.ejmech.2021.114046. PMID:34995923<ref>PMID:34995923</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 7mlg" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Hennecker C]]	+	[[Category: SARS coronavirus main proteinase]]
-	[[Category: Huot M]]	+	[[Category: Hennecker, C]]
-	[[Category: Labarre A]]	+	[[Category: Huot, M]]
-	[[Category: Miron CE]]	+	[[Category: Labarre, A]]
-	[[Category: Mittermaier AK]]	+	[[Category: Miron, C E]]
-	[[Category: Moitessier N]]	+	[[Category: Mittermaier, A K]]
-	[[Category: Patrascu MB]]	+	[[Category: Moitessier, N]]
-	[[Category: Pinus S]]	+	[[Category: Patrascu, M B]]
-	[[Category: Rueda AM]]	+	[[Category: Pinus, S]]
-	[[Category: Schmeing TM]]	+	[[Category: Rueda, A M]]
-	[[Category: Sharon I]]	+	[[Category: Schmeing, T M]]
-	[[Category: Stille J]]	+	[[Category: Sharon, I]]
-	[[Category: Tjutrins J]]	+	[[Category: Stille, J]]
-	[[Category: Venegas FA]]	+	[[Category: Tjutrins, J]]
-	[[Category: Vlaho D]]	+	[[Category: Venegas, F A]]
-	[[Category: Wang G]]	+	[[Category: Vlaho, D]]
		+	[[Category: Wang, G]]
		+	[[Category: Covalent inhibitor]]
		+	[[Category: Hydrolase-inhibitor complex]]
		+	[[Category: Sars-cov-2]]

OCA at 15:26, 22 December 2021

2021-12-22T15:26:08Z

←Older revision		Revision as of 15:26, 22 December 2021
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 7mlg ~~is ON HOLD until Paper Publication~~	+	==Crystal Structure of SARS-CoV-2 Main Protease (3CLpro/Mpro) Covalently Bound to Compound C63==
-		+	<StructureSection load='7mlg' size='340' side='right'caption='[[7mlg]]' scene=''>
-	~~Authors~~: ~~Sharon, I~~.~~, Stille, J~~.~~, Tjutrins, J~~.~~, Wang, G~~.~~, Venegas, F~~.A.~~, Hennecker, C~~.~~, Rueda, A~~.M., ~~Miron, C~~.E.~~, Pinus, S~~., ~~Labarre, A~~., ~~Patrascu, M~~.B.~~, Vlaho, D~~., ~~Huot, M~~.~~, Mittermaier, A~~.K., ~~Moitessier, N~~.~~, Schmeing, T.M~~.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7MLG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7MLG FirstGlance]. <br>
-	~~Description: Crystal Structure of SARS-CoV-2 Main Protease (3CLpro~~/~~Mpro) Covalently Bound to Compound C63~~	+	</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=7mlg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7mlg OCA], [https://pdbe.org/7mlg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7mlg RCSB], [https://www.ebi.ac.uk/pdbsum/7mlg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7mlg ProSAT]</span></td></tr>
-	[[Category: ~~Unreleased~~ Structures]]	+	</table>
-	[[Category: ~~Pinus, S~~]]	+	__TOC__
-	[[Category: ~~Wang, G~~]]	+	</StructureSection>
-	[[Category: ~~Hennecker, C~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Labarre, A~~]]	+	[[Category: Hennecker C]]
-	[[Category: ~~Tjutrins, J~~]]	+	[[Category: Huot M]]
-	[[Category: ~~Stille, J~~]]	+	[[Category: Labarre A]]
-	[[Category: ~~Mittermaier, A.K~~]]	+	[[Category: Miron CE]]
-	[[Category: ~~Moitessier, N~~]]	+	[[Category: Mittermaier AK]]
-	[[Category: ~~Huot, M~~]]	+	[[Category: Moitessier N]]
-	[[Category: ~~Sharon, I~~]]	+	[[Category: Patrascu MB]]
-	[[Category: ~~Schmeing, T.M~~]]	+	[[Category: Pinus S]]
-	[[Category: ~~Miron, C.E~~]]	+	[[Category: Rueda AM]]
-	[[Category: ~~Vlaho, D~~]]	+	[[Category: Schmeing TM]]
-	[[Category: ~~Rueda, A.M~~]]	+	[[Category: Sharon I]]
-	[[Category: ~~Venegas, F.A~~]]	+	[[Category: Stille J]]
-	[[Category: ~~Patrascu, M.B~~]]	+	[[Category: Tjutrins J]]
		+	[[Category: Venegas FA]]
		+	[[Category: Vlaho D]]
		+	[[Category: Wang G]]

OCA at 08:10, 12 May 2021

2021-05-12T08:10:23Z

←Older revision		Revision as of 08:10, 12 May 2021
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors: Sharon, I., Stille, J., Tjutrins, J., Wang, G., Venegas, F.A., Hennecker, C., Rueda, A.M., Miron, C.E., Pinus, S., Labarre, A., Patrascu, M.B., Vlaho, D., Huot, M., Mittermaier, A.K., Moitessier, N., Schmeing, T.M.		Authors: Sharon, I., Stille, J., Tjutrins, J., Wang, G., Venegas, F.A., Hennecker, C., Rueda, A.M., Miron, C.E., Pinus, S., Labarre, A., Patrascu, M.B., Vlaho, D., Huot, M., Mittermaier, A.K., Moitessier, N., Schmeing, T.M.

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

2021-05-05T07:28:36Z

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

←Older revision

Revision as of 07:28, 5 May 2021

OCA: New page: '''Unreleased structure''' The entry 7mlg is ON HOLD Authors: Sharon, I., Stille, J., Tjutrins, J., Wang, G., Venegas, F.A., Hennecker, C., Rueda, A.M., Miron, C.E., Pinus, S., Labarre,...

2021-05-05T07:28:35Z

New page: '''Unreleased structure''' The entry 7mlg is ON HOLD Authors: Sharon, I., Stille, J., Tjutrins, J., Wang, G., Venegas, F.A., Hennecker, C., Rueda, A.M., Miron, C.E., Pinus, S., Labarre,...

New page

'''Unreleased structure'''

The entry 7mlg is ON HOLD

Authors: Sharon, I., Stille, J., Tjutrins, J., Wang, G., Venegas, F.A., Hennecker, C., Rueda, A.M., Miron, C.E., Pinus, S., Labarre, A., Patrascu, M.B., Vlaho, D., Huot, M., Mittermaier, A.K., Moitessier, N., Schmeing, T.M.

Description: Crystal Structure of SARS-CoV-2 Main Protease (3CLpro/Mpro) Covalently Bound to Compound C63
[[Category: Unreleased Structures]]
[[Category: Pinus, S]]
[[Category: Wang, G]]
[[Category: Hennecker, C]]
[[Category: Labarre, A]]
[[Category: Tjutrins, J]]
[[Category: Stille, J]]
[[Category: Mittermaier, A.K]]
[[Category: Moitessier, N]]
[[Category: Huot, M]]
[[Category: Sharon, I]]
[[Category: Schmeing, T.M]]
[[Category: Miron, C.E]]
[[Category: Vlaho, D]]
[[Category: Rueda, A.M]]
[[Category: Venegas, F.A]]
[[Category: Patrascu, M.B]]