7syf - Revision history

OCA at 13:06, 1 March 2024

OCA — Fri, 01 Mar 2024 13:06:21 GMT

←Older revision		Revision as of 13:06, 1 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[7syf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7SYF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SYF FirstGlance]. <br>		<table><tr><td colspan='2'>[[7syf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7SYF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SYF 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=7syf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7syf OCA], [https://pdbe.org/7syf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7syf RCSB], [https://www.ebi.ac.uk/pdbsum/7syf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7syf ProSAT]</span></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution\|Resolution]] 4.2Å</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=7syf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7syf OCA], [https://pdbe.org/7syf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7syf RCSB], [https://www.ebi.ac.uk/pdbsum/7syf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7syf ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/D9IEF7_BPT4 D9IEF7_BPT4]~~] [~~[https://www.uniprot.org/uniprot/PREX1_HUMAN PREX1_HUMAN]] Functions as a RAC guanine nucleotide exchange factor (GEF), which activates the Rac proteins by exchanging bound GDP for free GTP. Its activity is synergistically activated by phosphatidylinositol 3,4,5-trisphosphate and the beta gamma subunits of heterotrimeric G protein. May function downstream of heterotrimeric G proteins in neutrophils.	+	[https://www.uniprot.org/uniprot/D9IEF7_BPT4 D9IEF7_BPT4] [https://www.uniprot.org/uniprot/PREX1_HUMAN PREX1_HUMAN] Functions as a RAC guanine nucleotide exchange factor (GEF), which activates the Rac proteins by exchanging bound GDP for free GTP. Its activity is synergistically activated by phosphatidylinositol 3,4,5-trisphosphate and the beta gamma subunits of heterotrimeric G protein. May function downstream of heterotrimeric G proteins in neutrophils.
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	P-Rex (PI(3,4,5)P3-dependent Rac exchanger) guanine nucleotide exchange factors potently activate Rho GTPases. P-Rex guanine nucleotide exchange factors are autoinhibited, synergistically activated by Gbetagamma and PI(3,4,5)P3 binding and dysregulated in cancer. Here, we use X-ray crystallography, cryogenic electron microscopy and crosslinking mass spectrometry to determine the structural basis of human P-Rex1 autoinhibition. P-Rex1 has a bipartite structure of N- and C-terminal modules connected by a C-terminal four-helix bundle that binds the N-terminal Pleckstrin homology (PH) domain. In the N-terminal module, the Dbl homology (DH) domain catalytic surface is occluded by the compact arrangement of the DH-PH-DEP1 domains. Structural analysis reveals a remarkable conformational transition to release autoinhibition, requiring a 126 degrees opening of the DH domain hinge helix. The off-axis position of Gbetagamma and PI(3,4,5)P3 binding sites further suggests a counter-rotation of the P-Rex1 halves by 90 degrees facilitates PH domain uncoupling from the four-helix bundle, releasing the autoinhibited DH domain to drive Rho GTPase signaling.	+
-		+
-	Structure of the metastatic factor P-Rex1 reveals a two-layered autoinhibitory mechanism.,Chang YG, Lupton CJ, Bayly-Jones C, Keen AC, D'Andrea L, Lucato CM, Steele JR, Venugopal H, Schittenhelm RB, Whisstock JC, Halls ML, Ellisdon AM Nat Struct Mol Biol. 2022 Jul 21. pii: 10.1038/s41594-022-00804-9. doi:, 10.1038/s41594-022-00804-9. PMID:35864164<ref>PMID:35864164</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 7syf" style="background-color:#fffaf0;"></div>~~	+
-	~~== References ==~~	+
-	~~<references/>~~	+
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 03:53, 8 September 2022

OCA — Thu, 08 Sep 2022 03:53:31 GMT

←Older revision		Revision as of 03:53, 8 September 2022
Line 1:		Line 1:

	==Reconstruction of full-length Prex-1 (PtdIns(3,4,5)P3-dependent Rac Exchanger 1)==		==Reconstruction of full-length Prex-1 (PtdIns(3,4,5)P3-dependent Rac Exchanger 1)==
-	<StructureSection load='7syf' size='340' side='right'caption='[[7syf]]' scene=''>	+	<StructureSection load='7syf' size='340' side='right'caption='[[7syf]], [[Resolution\|resolution]] 4.20Å' 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=7SYF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SYF FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[7syf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7SYF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SYF 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=7syf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7syf OCA], [https://pdbe.org/7syf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7syf RCSB], [https://www.ebi.ac.uk/pdbsum/7syf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7syf ProSAT]</span></td></tr>		</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=7syf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7syf OCA], [https://pdbe.org/7syf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7syf RCSB], [https://www.ebi.ac.uk/pdbsum/7syf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7syf ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[https://www.uniprot.org/uniprot/D9IEF7_BPT4 D9IEF7_BPT4]] [[https://www.uniprot.org/uniprot/PREX1_HUMAN PREX1_HUMAN]] Functions as a RAC guanine nucleotide exchange factor (GEF), which activates the Rac proteins by exchanging bound GDP for free GTP. Its activity is synergistically activated by phosphatidylinositol 3,4,5-trisphosphate and the beta gamma subunits of heterotrimeric G protein. May function downstream of heterotrimeric G proteins in neutrophils.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	P-Rex (PI(3,4,5)P3-dependent Rac exchanger) guanine nucleotide exchange factors potently activate Rho GTPases. P-Rex guanine nucleotide exchange factors are autoinhibited, synergistically activated by Gbetagamma and PI(3,4,5)P3 binding and dysregulated in cancer. Here, we use X-ray crystallography, cryogenic electron microscopy and crosslinking mass spectrometry to determine the structural basis of human P-Rex1 autoinhibition. P-Rex1 has a bipartite structure of N- and C-terminal modules connected by a C-terminal four-helix bundle that binds the N-terminal Pleckstrin homology (PH) domain. In the N-terminal module, the Dbl homology (DH) domain catalytic surface is occluded by the compact arrangement of the DH-PH-DEP1 domains. Structural analysis reveals a remarkable conformational transition to release autoinhibition, requiring a 126 degrees opening of the DH domain hinge helix. The off-axis position of Gbetagamma and PI(3,4,5)P3 binding sites further suggests a counter-rotation of the P-Rex1 halves by 90 degrees facilitates PH domain uncoupling from the four-helix bundle, releasing the autoinhibited DH domain to drive Rho GTPase signaling.
		+
		+	Structure of the metastatic factor P-Rex1 reveals a two-layered autoinhibitory mechanism.,Chang YG, Lupton CJ, Bayly-Jones C, Keen AC, D'Andrea L, Lucato CM, Steele JR, Venugopal H, Schittenhelm RB, Whisstock JC, Halls ML, Ellisdon AM Nat Struct Mol Biol. 2022 Jul 21. pii: 10.1038/s41594-022-00804-9. doi:, 10.1038/s41594-022-00804-9. PMID:35864164<ref>PMID:35864164</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 7syf" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Bayly-Jones C]]		[[Category: Bayly-Jones C]]
	[[Category: Ellisdon AM]]		[[Category: Ellisdon AM]]
	[[Category: Lupton CJ]]		[[Category: Lupton CJ]]

OCA at 11:08, 31 August 2022

OCA — Wed, 31 Aug 2022 11:08:17 GMT

←Older revision		Revision as of 11:08, 31 August 2022
Line 1:		Line 1:

	==Reconstruction of full-length Prex-1 (PtdIns(3,4,5)P3-dependent Rac Exchanger 1)==		==Reconstruction of full-length Prex-1 (PtdIns(3,4,5)P3-dependent Rac Exchanger 1)==
-	<StructureSection load='7syf' size='340' side='right'caption='[[7syf]]~~, [[Resolution\|resolution]] 4.20Å~~' scene=''>	+	<StructureSection load='7syf' size='340' side='right'caption='[[7syf]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>~~[[7syf]] is a 1 chain structure.~~ Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7SYF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SYF FirstGlance]. <br>	+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7SYF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SYF FirstGlance]. <br>
-	</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span></td></tr>	+	</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=7syf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7syf OCA], [https://pdbe.org/7syf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7syf RCSB], [https://www.ebi.ac.uk/pdbsum/7syf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7syf 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=7syf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7syf OCA], [https://pdbe.org/7syf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7syf RCSB], [https://www.ebi.ac.uk/pdbsum/7syf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7syf ProSAT]</span></td></tr>	+
	</table>		</table>
-	== Function ==
-	[[https://www.uniprot.org/uniprot/PREX1_HUMAN PREX1_HUMAN]] Functions as a RAC guanine nucleotide exchange factor (GEF), which activates the Rac proteins by exchanging bound GDP for free GTP. Its activity is synergistically activated by phosphatidylinositol 3,4,5-trisphosphate and the beta gamma subunits of heterotrimeric G protein. May function downstream of heterotrimeric G proteins in neutrophils.
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	P-Rex (PI(3,4,5)P3-dependent Rac exchanger) guanine nucleotide exchange factors potently activate Rho GTPases. P-Rex guanine nucleotide exchange factors are autoinhibited, synergistically activated by Gbetagamma and PI(3,4,5)P3 binding and dysregulated in cancer. Here, we use X-ray crystallography, cryogenic electron microscopy and crosslinking mass spectrometry to determine the structural basis of human P-Rex1 autoinhibition. P-Rex1 has a bipartite structure of N- and C-terminal modules connected by a C-terminal four-helix bundle that binds the N-terminal Pleckstrin homology (PH) domain. In the N-terminal module, the Dbl homology (DH) domain catalytic surface is occluded by the compact arrangement of the DH-PH-DEP1 domains. Structural analysis reveals a remarkable conformational transition to release autoinhibition, requiring a 126 degrees opening of the DH domain hinge helix. The off-axis position of Gbetagamma and PI(3,4,5)P3 binding sites further suggests a counter-rotation of the P-Rex1 halves by 90 degrees facilitates PH domain uncoupling from the four-helix bundle, releasing the autoinhibited DH domain to drive Rho GTPase signaling.
-
-	Structure of the metastatic factor P-Rex1 reveals a two-layered autoinhibitory mechanism.,Chang YG, Lupton CJ, Bayly-Jones C, Keen AC, D'Andrea L, Lucato CM, Steele JR, Venugopal H, Schittenhelm RB, Whisstock JC, Halls ML, Ellisdon AM Nat Struct Mol Biol. 2022 Jul 21. pii: 10.1038/s41594-022-00804-9. doi:, 10.1038/s41594-022-00804-9. PMID:35864164<ref>PMID:35864164</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 7syf" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Lysozyme]]~~	+	[[Category: Bayly-Jones C]]
-	[[Category: Bayly-Jones, C]]	+	[[Category: Ellisdon AM]]
-	[[Category: Ellisdon~~, A M~~]]	+	[[Category: Lupton CJ]]
-	[[Category: Lupton~~, C J]]~~	+
-	~~[[Category: Guanine nucleotide exchange factor]]~~	+
-	~~[[Category: Metastasis]]~~	+
-	~~[[Category: Oncoprotein]]~~	+
-	~~[[Category: Plasma membrane]]~~	+
-	~~[[Category: Rho gtpase signalling~~]]	+

OCA at 05:02, 3 August 2022

OCA — Wed, 03 Aug 2022 05:02:00 GMT

←Older revision		Revision as of 05:02, 3 August 2022
Line 1:		Line 1:

	==Reconstruction of full-length Prex-1 (PtdIns(3,4,5)P3-dependent Rac Exchanger 1)==		==Reconstruction of full-length Prex-1 (PtdIns(3,4,5)P3-dependent Rac Exchanger 1)==
-	<StructureSection load='7syf' size='340' side='right'caption='[[7syf]]' scene=''>	+	<StructureSection load='7syf' size='340' side='right'caption='[[7syf]], [[Resolution\|resolution]] 4.20Å' 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=7SYF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SYF FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[7syf]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7SYF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SYF 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=7syf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7syf OCA], [https://pdbe.org/7syf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7syf RCSB], [https://www.ebi.ac.uk/pdbsum/7syf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7syf ProSAT]</span></td></tr>	+	</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </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=7syf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7syf OCA], [https://pdbe.org/7syf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7syf RCSB], [https://www.ebi.ac.uk/pdbsum/7syf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7syf ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[https://www.uniprot.org/uniprot/PREX1_HUMAN PREX1_HUMAN]] Functions as a RAC guanine nucleotide exchange factor (GEF), which activates the Rac proteins by exchanging bound GDP for free GTP. Its activity is synergistically activated by phosphatidylinositol 3,4,5-trisphosphate and the beta gamma subunits of heterotrimeric G protein. May function downstream of heterotrimeric G proteins in neutrophils.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	P-Rex (PI(3,4,5)P3-dependent Rac exchanger) guanine nucleotide exchange factors potently activate Rho GTPases. P-Rex guanine nucleotide exchange factors are autoinhibited, synergistically activated by Gbetagamma and PI(3,4,5)P3 binding and dysregulated in cancer. Here, we use X-ray crystallography, cryogenic electron microscopy and crosslinking mass spectrometry to determine the structural basis of human P-Rex1 autoinhibition. P-Rex1 has a bipartite structure of N- and C-terminal modules connected by a C-terminal four-helix bundle that binds the N-terminal Pleckstrin homology (PH) domain. In the N-terminal module, the Dbl homology (DH) domain catalytic surface is occluded by the compact arrangement of the DH-PH-DEP1 domains. Structural analysis reveals a remarkable conformational transition to release autoinhibition, requiring a 126 degrees opening of the DH domain hinge helix. The off-axis position of Gbetagamma and PI(3,4,5)P3 binding sites further suggests a counter-rotation of the P-Rex1 halves by 90 degrees facilitates PH domain uncoupling from the four-helix bundle, releasing the autoinhibited DH domain to drive Rho GTPase signaling.
		+
		+	Structure of the metastatic factor P-Rex1 reveals a two-layered autoinhibitory mechanism.,Chang YG, Lupton CJ, Bayly-Jones C, Keen AC, D'Andrea L, Lucato CM, Steele JR, Venugopal H, Schittenhelm RB, Whisstock JC, Halls ML, Ellisdon AM Nat Struct Mol Biol. 2022 Jul 21. pii: 10.1038/s41594-022-00804-9. doi:, 10.1038/s41594-022-00804-9. PMID:35864164<ref>PMID:35864164</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 7syf" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Bayly-Jones C]]	+	[[Category: Lysozyme]]
-	[[Category: Ellisdon AM]]	+	[[Category: Bayly-Jones, C]]
-	[[Category: Lupton CJ]]	+	[[Category: Ellisdon, A M]]
		+	[[Category: Lupton, C J]]
		+	[[Category: Guanine nucleotide exchange factor]]
		+	[[Category: Metastasis]]
		+	[[Category: Oncoprotein]]
		+	[[Category: Plasma membrane]]
		+	[[Category: Rho gtpase signalling]]

OCA at 18:04, 27 July 2022

OCA — Wed, 27 Jul 2022 18:04:39 GMT

←Older revision		Revision as of 18:04, 27 July 2022
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 7syf is ~~ON HOLD until Paper Publication~~	+	==Reconstruction of full-length Prex-1 (PtdIns(3,4,5)P3-dependent Rac Exchanger 1)==
-		+	<StructureSection load='7syf' size='340' side='right'caption='[[7syf]]' scene=''>
-	~~Authors~~:	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7SYF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SYF FirstGlance]. <br>
-	~~Description~~:	+	</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=7syf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7syf OCA], [https://pdbe.org/7syf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7syf RCSB], [https://www.ebi.ac.uk/pdbsum/7syf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7syf ProSAT]</span></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	</table>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Bayly-Jones C]]
		+	[[Category: Ellisdon AM]]
		+	[[Category: Lupton CJ]]

OCA at 09:17, 5 January 2022

OCA — Wed, 05 Jan 2022 09:17:38 GMT

←Older revision		Revision as of 09:17, 5 January 2022
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors:		Authors:

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

OCA — Wed, 01 Dec 2021 05:15:53 GMT

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

←Older revision

Revision as of 05:15, 1 December 2021

OCA: New page: '''Unreleased structure''' The entry 7syf is ON HOLD Authors: Description: Category: Unreleased Structures

OCA — Wed, 01 Dec 2021 05:15:52 GMT

New page: '''Unreleased structure''' The entry 7syf is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 7syf is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]