7rbz - Revision history

OCA at 16:28, 18 October 2023

OCA — Wed, 18 Oct 2023 16:28:21 GMT

←Older revision		Revision as of 16:28, 18 October 2023
Line 3:		Line 3:
	<StructureSection load='7rbz' size='340' side='right'caption='[[7rbz]], [[Resolution\|resolution]] 1.65Å' scene=''>		<StructureSection load='7rbz' size='340' side='right'caption='[[7rbz]], [[Resolution\|resolution]] 1.65Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[7rbz]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7RBZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7RBZ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[7rbz]] 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=7RBZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7RBZ FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=4IJ:5~~-~~chloropyridin-3-yl+2~~,~~3-dihydro-1H-indole-4-carboxylate'>4IJ</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]] 1.65Å</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=4IJ:5-chloropyridin-3-yl+2,3-dihydro-1H-indole-4-carboxylate'>4IJ</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=7rbz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7rbz OCA], [https://pdbe.org/7rbz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7rbz RCSB], [https://www.ebi.ac.uk/pdbsum/7rbz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7rbz 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=7rbz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7rbz OCA], [https://pdbe.org/7rbz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7rbz RCSB], [https://www.ebi.ac.uk/pdbsum/7rbz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7rbz 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: Anson~~, B A]]~~	+	[[Category: Anson BA]]
-	~~[[Category: Structural genomic~~]]	+	[[Category: Ghosh AK]]
-	[[Category: Ghosh~~, A K~~]]	+	[[Category: Mesecar AD]]
-	[[Category: Mesecar~~, A D]]~~	+
-	~~[[Category: Covalent]]~~	+
-	~~[[Category: Covid-19]]~~	+
-	~~[[Category: Csgid]]~~	+
-	~~[[Category: Inhibitor]]~~	+
-	~~[[Category: Main]]~~	+
-	~~[[Category: Mpro]]~~	+
-	~~[[Category: Protease]]~~	+
-	~~[[Category: Sars-cov-2]]~~	+
-	~~[[Category: Viral protein~~]]	+

OCA at 15:55, 27 October 2021

OCA — Wed, 27 Oct 2021 15:55:28 GMT

←Older revision		Revision as of 15:55, 27 October 2021
Line 1:		Line 1:

	==X-ray Structure of SARS-CoV-2 main protease covalently modified by compound GRL-017-20==		==X-ray Structure of SARS-CoV-2 main protease covalently modified by compound GRL-017-20==
-	<StructureSection load='7rbz' size='340' side='right'caption='[[7rbz]]' scene=''>	+	<StructureSection load='7rbz' size='340' side='right'caption='[[7rbz]], [[Resolution\|resolution]] 1.65Å' 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=7RBZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7RBZ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[7rbz]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7RBZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7RBZ 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=7rbz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7rbz OCA], [https://pdbe.org/7rbz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7rbz RCSB], [https://www.ebi.ac.uk/pdbsum/7rbz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7rbz 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=4IJ:5-chloropyridin-3-yl+2,3-dihydro-1H-indole-4-carboxylate'>4IJ</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=7rbz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7rbz OCA], [https://pdbe.org/7rbz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7rbz RCSB], [https://www.ebi.ac.uk/pdbsum/7rbz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7rbz 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 ==
		+	Here, we report the synthesis, structure-activity relationship studies, enzyme inhibition, antiviral activity, and X-ray crystallographic studies of 5-chloropyridinyl indole carboxylate derivatives as a potent class of SARS-CoV-2 chymotrypsin-like protease inhibitors. Compound 1 exhibited a SARS-CoV-2 3CLpro inhibitory IC50 value of 250 nM and an antiviral EC50 value of 2.8 muM in VeroE6 cells. Remdesivir, an RNA-dependent RNA polymerase inhibitor, showed an antiviral EC50 value of 1.2 muM in the same assay. Compound 1 showed comparable antiviral activity with remdesivir in immunocytochemistry assays. Compound 7d with an N-allyl derivative showed the most potent enzyme inhibitory IC50 value of 73 nM. To obtain molecular insight into the binding properties of these molecules, X-ray crystal structures of compounds 2, 7b, and 9d-bound to SARS-CoV 3CLpro were determined, and their binding properties were compared.
		+
		+	Indole Chloropyridinyl Ester-Derived SARS-CoV-2 3CLpro Inhibitors: Enzyme Inhibition, Antiviral Efficacy, Structure-Activity Relationship, and X-ray Structural Studies.,Ghosh AK, Raghavaiah J, Shahabi D, Yadav M, Anson BJ, Lendy EK, Hattori SI, Higashi-Kuwata N, Mitsuya H, Mesecar AD J Med Chem. 2021 Sep 16. doi: 10.1021/acs.jmedchem.1c01214. PMID:34528437<ref>PMID:34528437</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 7rbz" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Anson BA]]	+	[[Category: SARS coronavirus main proteinase]]
-	[[Category: Ghosh AK]]	+	[[Category: Anson, B A]]
-	[[Category: Mesecar AD]]	+	[[Category: Structural genomic]]
		+	[[Category: Ghosh, A K]]
		+	[[Category: Mesecar, A D]]
		+	[[Category: Covalent]]
		+	[[Category: Covid-19]]
		+	[[Category: Csgid]]
		+	[[Category: Inhibitor]]
		+	[[Category: Main]]
		+	[[Category: Mpro]]
		+	[[Category: Protease]]
		+	[[Category: Sars-cov-2]]
		+	[[Category: Viral protein]]

OCA at 08:51, 29 September 2021

OCA — Wed, 29 Sep 2021 08:51:44 GMT

←Older revision		Revision as of 08:51, 29 September 2021
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry 7rbz is ON HOLD until Paper Publication~~	+	==X-ray Structure of SARS-CoV-2 main protease covalently modified by compound GRL-017-20==
-		+	<StructureSection load='7rbz' size='340' side='right'caption='[[7rbz]]' scene=''>
-	~~Authors: Mesecar, A.D., Anson, B.A., Ghosh, A.K., Center for Structural Genomics of Infectious Diseases (CSGID)~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7RBZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7RBZ FirstGlance]. <br>
-	~~Description:~~ X-ray Structure of SARS-CoV-2 main protease covalently modified by compound GRL-017-20	+	</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=7rbz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7rbz OCA], [https://pdbe.org/7rbz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7rbz RCSB], [https://www.ebi.ac.uk/pdbsum/7rbz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7rbz ProSAT]</span></td></tr>
-	[[~~Category~~: ~~Unreleased Structures~~]]	+	</table>
-	[[~~Category~~: ~~Mesecar~~, A.D]]	+	__TOC__
-	[[Category: ~~Ghosh, A.K~~]]	+	</StructureSection>
-	[[Category: ~~Center For Structural Genomics Of Infectious Diseases (Csgid)~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Anson, B.A~~]]	+	[[Category: Anson BA]]
		+	[[Category: Ghosh AK]]
		+	[[Category: Mesecar AD]]

OCA at 05:08, 11 August 2021

OCA — Wed, 11 Aug 2021 05:08:54 GMT

←Older revision		Revision as of 05:08, 11 August 2021
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors: Mesecar, A.D., Anson, B.A., Ghosh, A.K., Center for Structural Genomics of Infectious Diseases (CSGID)		Authors: Mesecar, A.D., Anson, B.A., Ghosh, A.K., Center for Structural Genomics of Infectious Diseases (CSGID)
Line 7:		Line 7:
	Description: X-ray Structure of SARS-CoV-2 main protease covalently modified by compound GRL-017-20		Description: X-ray Structure of SARS-CoV-2 main protease covalently modified by compound GRL-017-20
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: Ghosh, A.K]]
-	[[Category: Anson, B.A]]
	[[Category: Mesecar, A.D]]		[[Category: Mesecar, A.D]]
		+	[[Category: Ghosh, A.K]]
	[[Category: Center For Structural Genomics Of Infectious Diseases (Csgid)]]		[[Category: Center For Structural Genomics Of Infectious Diseases (Csgid)]]
		+	[[Category: Anson, B.A]]

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

OCA — Wed, 14 Jul 2021 08:56:56 GMT

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

←Older revision

Revision as of 08:56, 14 July 2021

OCA: New page: '''Unreleased structure''' The entry 7rbz is ON HOLD Authors: Mesecar, A.D., Anson, B.A., Ghosh, A.K., Center for Structural Genomics of Infectious Diseases (CSGID) Description: X-ray ...

OCA — Wed, 14 Jul 2021 08:56:55 GMT

New page: '''Unreleased structure''' The entry 7rbz is ON HOLD Authors: Mesecar, A.D., Anson, B.A., Ghosh, A.K., Center for Structural Genomics of Infectious Diseases (CSGID) Description: X-ray ...

New page

'''Unreleased structure'''

The entry 7rbz is ON HOLD

Authors: Mesecar, A.D., Anson, B.A., Ghosh, A.K., Center for Structural Genomics of Infectious Diseases (CSGID)

Description: X-ray Structure of SARS-CoV-2 main protease covalently modified by compound GRL-017-20
[[Category: Unreleased Structures]]
[[Category: Ghosh, A.K]]
[[Category: Anson, B.A]]
[[Category: Mesecar, A.D]]
[[Category: Center For Structural Genomics Of Infectious Diseases (Csgid)]]