4y3o - Revision history

OCA at 09:03, 20 March 2024

OCA — Wed, 20 Mar 2024 09:03:15 GMT

←Older revision		Revision as of 09:03, 20 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4y3o]] is a 4 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=4Y3O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Y3O FirstGlance]. <br>		<table><tr><td colspan='2'>[[4y3o]] is a 4 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=4Y3O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Y3O FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</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]] 2.2Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</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=4y3o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y3o OCA], [https://pdbe.org/4y3o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4y3o RCSB], [https://www.ebi.ac.uk/pdbsum/4y3o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4y3o 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=4y3o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y3o OCA], [https://pdbe.org/4y3o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4y3o RCSB], [https://www.ebi.ac.uk/pdbsum/4y3o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4y3o ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/RIOX1_HUMAN RIOX1_HUMAN] Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase. Specifically demethylates 'Lys-4' (H3K4me) and 'Lys-36' (H3K36me) of histone H3, thereby playing a central role in histone code. Preferentially demethylates trimethylated H3 'Lys-4' (H3K4me3) and monomethylated H3 'Lys-4' (H3K4me1) residues, while it has weaker activity for dimethylated H3 'Lys-36' (H3K36me2). Also catalyzes the hydroxylation of 60S ribosomal protein L8 on 'His-216'. Acts as a regulator of osteoblast differentiation via its interaction with SP7/OSX by demethylating H3K4me and H3K36me, thereby inhibiting SP7/OSX-mediated promoter activation (By similarity). May also play a role in ribosome biogenesis and in the replication or remodeling of certain heterochromatic region. Participates in MYC-induced transcriptional activation.<ref>PMID:14742713</ref> <ref>PMID:17308053</ref> <ref>PMID:23103944</ref>		[https://www.uniprot.org/uniprot/RIOX1_HUMAN RIOX1_HUMAN] Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase. Specifically demethylates 'Lys-4' (H3K4me) and 'Lys-36' (H3K36me) of histone H3, thereby playing a central role in histone code. Preferentially demethylates trimethylated H3 'Lys-4' (H3K4me3) and monomethylated H3 'Lys-4' (H3K4me1) residues, while it has weaker activity for dimethylated H3 'Lys-36' (H3K36me2). Also catalyzes the hydroxylation of 60S ribosomal protein L8 on 'His-216'. Acts as a regulator of osteoblast differentiation via its interaction with SP7/OSX by demethylating H3K4me and H3K36me, thereby inhibiting SP7/OSX-mediated promoter activation (By similarity). May also play a role in ribosome biogenesis and in the replication or remodeling of certain heterochromatic region. Participates in MYC-induced transcriptional activation.<ref>PMID:14742713</ref> <ref>PMID:17308053</ref> <ref>PMID:23103944</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The JmjC domain-containing proteins belong to a large family of oxygenases possessing distinct substrate specificities which are involved in the regulation of different biological processes, such as gene transcription, RNA processing and translation. Nucleolar protein 66 (NO66) is a JmjC domain-containing protein which has been reported to be a histone demethylase and a ribosome protein 8 (Rpl8) hydroxylase. The present biochemical study confirmed the hydroxylase activity of NO66 and showed that oligomerization is required for NO66 to efficiently catalyze the hydroxylation of Rpl8. The structures of NO66(176-C) complexed with Rpl8(204-224) in a tetrameric form and of the mutant protein M2 in a dimeric form were solved. Based on the results of structural and biochemical analyses, the consensus sequence motif NHXH recognized by NO66 was confirmed. Several potential substrates of NO66 were found by a BLAST search according to the consensus sequence motif. When binding to substrate, the relative positions of each subunit in the NO66 tetramer shift. Oligomerization may facilitate the motion of each subunit in the NO66 tetramer and affect the catalytic activity.
-
-	Structure of the JmjC domain-containing protein NO66 complexed with ribosomal protein Rpl8.,Wang C, Zhang Q, Hang T, Tao Y, Ma X, Wu M, Zhang X, Zang J Acta Crystallogr D Biol Crystallogr. 2015 Sep 1;71(Pt 9):1955-64. doi:, 10.1107/S1399004715012948. Epub 2015 Aug 28. PMID:26327385<ref>PMID:26327385</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4y3o" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 18:05, 26 April 2023

OCA — Wed, 26 Apr 2023 18:05:18 GMT

←Older revision		Revision as of 18:05, 26 April 2023
Line 3:		Line 3:
	<StructureSection load='4y3o' size='340' side='right'caption='[[4y3o]], [[Resolution\|resolution]] 2.20Å' scene=''>		<StructureSection load='4y3o' size='340' side='right'caption='[[4y3o]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4y3o]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y3O OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4Y3O FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4y3o]] is a 4 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=4Y3O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Y3O FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4y33\|4y33]], [[4y4r\|4y4r]]</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=4y3o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y3o OCA], [https://pdbe.org/4y3o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4y3o RCSB], [https://www.ebi.ac.uk/pdbsum/4y3o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4y3o ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">NO66, C14orf169, MAPJD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4y3o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y3o OCA], [~~http~~://pdbe.org/4y3o PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4y3o RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4y3o PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4y3o ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/~~NO66_HUMAN NO66_HUMAN]~~] Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase. Specifically demethylates 'Lys-4' (H3K4me) and 'Lys-36' (H3K36me) of histone H3, thereby playing a central role in histone code. Preferentially demethylates trimethylated H3 'Lys-4' (H3K4me3) and monomethylated H3 'Lys-4' (H3K4me1) residues, while it has weaker activity for dimethylated H3 'Lys-36' (H3K36me2). Also catalyzes the hydroxylation of 60S ribosomal protein L8 on 'His-216'. Acts as a regulator of osteoblast differentiation via its interaction with SP7/OSX by demethylating H3K4me and H3K36me, thereby inhibiting SP7/OSX-mediated promoter activation (By similarity). May also play a role in ribosome biogenesis and in the replication or remodeling of certain heterochromatic region. Participates in MYC-induced transcriptional activation.<ref>PMID:14742713</ref> <ref>PMID:17308053</ref> <ref>PMID:23103944</ref>	+	[https://www.uniprot.org/uniprot/RIOX1_HUMAN RIOX1_HUMAN] Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase. Specifically demethylates 'Lys-4' (H3K4me) and 'Lys-36' (H3K36me) of histone H3, thereby playing a central role in histone code. Preferentially demethylates trimethylated H3 'Lys-4' (H3K4me3) and monomethylated H3 'Lys-4' (H3K4me1) residues, while it has weaker activity for dimethylated H3 'Lys-36' (H3K36me2). Also catalyzes the hydroxylation of 60S ribosomal protein L8 on 'His-216'. Acts as a regulator of osteoblast differentiation via its interaction with SP7/OSX by demethylating H3K4me and H3K36me, thereby inhibiting SP7/OSX-mediated promoter activation (By similarity). May also play a role in ribosome biogenesis and in the replication or remodeling of certain heterochromatic region. Participates in MYC-induced transcriptional activation.<ref>PMID:14742713</ref> <ref>PMID:17308053</ref> <ref>PMID:23103944</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 24:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Wang, C]]	+	[[Category: Wang C]]
-	[[Category: Zang, J]]	+	[[Category: Zang J]]
-	[[Category: Zhang, Q]]	+	[[Category: Zhang Q]]
-	~~[[Category: Jmjc-domain]]~~	+
-	~~[[Category: Oxidoreductase-peptide complex]]~~	+
-	~~[[Category: Quaternary compound structure]]~~	+
-	~~[[Category: Ribosomal oxygenase~~]]	+

OCA at 00:27, 6 June 2019

OCA — Thu, 06 Jun 2019 00:27:12 GMT

←Older revision		Revision as of 00:27, 6 June 2019
Line 1:		Line 1:
		+
	==Crystal structure of Ribosomal oxygenase NO66 in complex with substrate Rpl8 peptide and Ni(II) and cofactor N-oxalyglycine==		==Crystal structure of Ribosomal oxygenase NO66 in complex with substrate Rpl8 peptide and Ni(II) and cofactor N-oxalyglycine==
-	<StructureSection load='4y3o' size='340' side='right' caption='[[4y3o]], [[Resolution\|resolution]] 2.20Å' scene=''>	+	<StructureSection load='4y3o' size='340' side='right'caption='[[4y3o]], [[Resolution\|resolution]] 2.20Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4y3o]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y3O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Y3O FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4y3o]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y3O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Y3O FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4y33\|4y33]], [[4y4r\|4y4r]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4y33\|4y33]], [[4y4r\|4y4r]]</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4y3o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y3o OCA], [http://pdbe.org/4y3o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4y3o RCSB], [http://www.ebi.ac.uk/pdbsum/4y3o PDBsum]</span></td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">NO66, C14orf169, MAPJD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4y3o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y3o OCA], [http://pdbe.org/4y3o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4y3o RCSB], [http://www.ebi.ac.uk/pdbsum/4y3o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4y3o ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 22:		Line 24:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Wang, C]]		[[Category: Wang, C]]
	[[Category: Zang, J]]		[[Category: Zang, J]]

OCA at 13:45, 7 October 2015

OCA — Wed, 07 Oct 2015 13:45:59 GMT

←Older revision		Revision as of 13:45, 7 October 2015
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==Crystal structure of Ribosomal oxygenase NO66 in complex with substrate Rpl8 peptide and Ni(II) and cofactor N-oxalyglycine==
		+	<StructureSection load='4y3o' size='340' side='right' caption='[[4y3o]], [[Resolution\|resolution]] 2.20Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4y3o]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y3O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Y3O FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4y33\|4y33]], [[4y4r\|4y4r]]</td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4y3o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y3o OCA], [http://pdbe.org/4y3o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4y3o RCSB], [http://www.ebi.ac.uk/pdbsum/4y3o PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/NO66_HUMAN NO66_HUMAN]] Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase. Specifically demethylates 'Lys-4' (H3K4me) and 'Lys-36' (H3K36me) of histone H3, thereby playing a central role in histone code. Preferentially demethylates trimethylated H3 'Lys-4' (H3K4me3) and monomethylated H3 'Lys-4' (H3K4me1) residues, while it has weaker activity for dimethylated H3 'Lys-36' (H3K36me2). Also catalyzes the hydroxylation of 60S ribosomal protein L8 on 'His-216'. Acts as a regulator of osteoblast differentiation via its interaction with SP7/OSX by demethylating H3K4me and H3K36me, thereby inhibiting SP7/OSX-mediated promoter activation (By similarity). May also play a role in ribosome biogenesis and in the replication or remodeling of certain heterochromatic region. Participates in MYC-induced transcriptional activation.<ref>PMID:14742713</ref> <ref>PMID:17308053</ref> <ref>PMID:23103944</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The JmjC domain-containing proteins belong to a large family of oxygenases possessing distinct substrate specificities which are involved in the regulation of different biological processes, such as gene transcription, RNA processing and translation. Nucleolar protein 66 (NO66) is a JmjC domain-containing protein which has been reported to be a histone demethylase and a ribosome protein 8 (Rpl8) hydroxylase. The present biochemical study confirmed the hydroxylase activity of NO66 and showed that oligomerization is required for NO66 to efficiently catalyze the hydroxylation of Rpl8. The structures of NO66(176-C) complexed with Rpl8(204-224) in a tetrameric form and of the mutant protein M2 in a dimeric form were solved. Based on the results of structural and biochemical analyses, the consensus sequence motif NHXH recognized by NO66 was confirmed. Several potential substrates of NO66 were found by a BLAST search according to the consensus sequence motif. When binding to substrate, the relative positions of each subunit in the NO66 tetramer shift. Oligomerization may facilitate the motion of each subunit in the NO66 tetramer and affect the catalytic activity.

-	~~The entry 4y3o is ON HOLD until Feb~~ 10 ~~2017~~	+	Structure of the JmjC domain-containing protein NO66 complexed with ribosomal protein Rpl8.,Wang C, Zhang Q, Hang T, Tao Y, Ma X, Wu M, Zhang X, Zang J Acta Crystallogr D Biol Crystallogr. 2015 Sep 1;71(Pt 9):1955-64. doi:, 10.1107/S1399004715012948. Epub 2015 Aug 28. PMID:26327385<ref>PMID:26327385</ref>

-	~~Authors: Wang~~, C.~~, Zhang, Q~~.~~, Zang, J~~.	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description~~:	+	<div class="pdbe-citations 4y3o" style="background-color:#fffaf0;"></div>
-	[[Category: ~~Unreleased Structures~~]]	+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Wang, C]]
	[[Category: Zang, J]]		[[Category: Zang, J]]
-	[[Category: Wang, C]]
	[[Category: Zhang, Q]]		[[Category: Zhang, Q]]
		+	[[Category: Jmjc-domain]]
		+	[[Category: Oxidoreductase-peptide complex]]
		+	[[Category: Quaternary compound structure]]
		+	[[Category: Ribosomal oxygenase]]

OCA at 10:41, 15 April 2015

OCA — Wed, 15 Apr 2015 10:41:34 GMT

←Older revision		Revision as of 10:41, 15 April 2015
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4y3o is ON HOLD	+	The entry 4y3o is ON HOLD until Feb 10 2017

	Authors: Wang, C., Zhang, Q., Zang, J.		Authors: Wang, C., Zhang, Q., Zang, J.

OCA at 10:03, 4 March 2015

OCA — Wed, 04 Mar 2015 10:03:55 GMT

←Older revision		Revision as of 10:03, 4 March 2015
Line 3:		Line 3:
	The entry 4y3o is ON HOLD		The entry 4y3o is ON HOLD

-	Authors: ~~Chengliang~~ Wang, ~~Qiongdi~~ Zhang, ~~Jianye~~ Zang	+	Authors: Wang, C., Zhang, Q., Zang, J.

	Description:		Description:
	[[Category: Unreleased Structures]]		[[Category: Unreleased Structures]]
-	[[Category: ~~Chengliang~~ Wang, ~~Qiongdi~~ Zhang, ~~Jianye Zang~~]]	+	[[Category: Zang, J]]
		+	[[Category: Wang, C]]
		+	[[Category: Zhang, Q]]

OCA: Protected "4y3o" [edit=sysop:move=sysop]

OCA — Wed, 18 Feb 2015 11:59:47 GMT

Protected "4y3o" [edit=sysop:move=sysop]

←Older revision

Revision as of 11:59, 18 February 2015

OCA: New page: '''Unreleased structure''' The entry 4y3o is ON HOLD Authors: Chengliang Wang, Qiongdi Zhang, Jianye Zang Description: Category: Unreleased Structures [[Category: Chengliang Wang,...

OCA — Wed, 18 Feb 2015 11:59:46 GMT

New page: '''Unreleased structure''' The entry 4y3o is ON HOLD Authors: Chengliang Wang, Qiongdi Zhang, Jianye Zang Description: Category: Unreleased Structures [[Category: Chengliang Wang,...

New page

'''Unreleased structure'''

The entry 4y3o is ON HOLD

Authors: Chengliang Wang, Qiongdi Zhang, Jianye Zang

Description:
[[Category: Unreleased Structures]]
[[Category: Chengliang Wang, Qiongdi Zhang, Jianye Zang]]