5lwv - Revision history

OCA at 18:54, 18 October 2023

OCA — Wed, 18 Oct 2023 18:54:08 GMT

←Older revision		Revision as of 18:54, 18 October 2023
Line 3:		Line 3:
	<StructureSection load='5lwv' size='340' side='right'caption='[[5lwv]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='5lwv' size='340' side='right'caption='[[5lwv]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5lwv]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LWV OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5LWV FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5lwv]] 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=5LWV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LWV FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</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]] 1.9Å</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein_O-GlcNAc_transferase Protein O-GlcNAc transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.255 2.4.1.255] </span></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=5lwv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lwv OCA], [~~http~~://pdbe.org/5lwv PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5lwv RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5lwv PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5lwv 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=5lwv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lwv OCA], [https://pdbe.org/5lwv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lwv RCSB], [https://www.ebi.ac.uk/pdbsum/5lwv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lwv ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/HCFC1_HUMAN HCFC1_HUMAN]] X-linked nonsyndromic intellectual deficit. Mental retardation, X-linked 3 (MRX3) [MIM:[~~http~~://omim.org/entry/309541 309541]]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptative behavior and manifested during the developmental period. Intellectual deficiency is the only primary symptom of non-syndromic X-linked mental retardation, while syndromic mental retardation presents with associated physical, neurological and/or psychiatric manifestations. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:23000143</ref>	+	[https://www.uniprot.org/uniprot/OGT1_HUMAN OGT1_HUMAN] Regulation of OGT activity and altered O-GlcNAcylations are implicated in diabetes and Alzheimer disease. O-GlcNAcylation of AKT1 affects insulin signaling and, possibly diabetes. Reduced O-GlcNAcylations and resulting increased phosphorylations of MAPT/TAU are observed in Alzheimer disease (AD) brain cerebrum.[https://www.uniprot.org/uniprot/HCFC1_HUMAN HCFC1_HUMAN] X-linked nonsyndromic intellectual deficit. Mental retardation, X-linked 3 (MRX3) [MIM:[https://omim.org/entry/309541 309541]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptative behavior and manifested during the developmental period. Intellectual deficiency is the only primary symptom of non-syndromic X-linked mental retardation, while syndromic mental retardation presents with associated physical, neurological and/or psychiatric manifestations. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:23000143</ref>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/HCFC1_HUMAN HCFC1_HUMAN]] Involved in control of the cell cycle. Also antagonizes transactivation by ZBTB17 and GABP2; represses ZBTB17 activation of the p15(INK4b) promoter and inhibits its ability to recruit p300. Coactivator for EGR2 and GABP2. Tethers the chromatin modifying Set1/Ash2 histone H3 'Lys-4' methyltransferase (H3K4me) and Sin3 histone deacetylase (HDAC) complexes (involved in the activation and repression of transcription, respectively) together. Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the regulation of the transcriptional activity of RRM1. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. In case of human herpes simplex virus (HSV) infection, HCFC1 forms a multiprotein-DNA complex with the viral transactivator protein VP16 and POU2F1 thereby enabling the transcription of the viral immediate early genes.<ref>PMID:10920196</ref> <ref>PMID:9990006</ref> <ref>PMID:10675337</ref> <ref>PMID:10629049</ref> <ref>PMID:10779346</ref> <ref>PMID:12244100</ref> <ref>PMID:14532282</ref> <ref>PMID:12670868</ref> <ref>PMID:15190068</ref> <ref>PMID:16624878</ref> <ref>PMID:17578910</ref> <ref>PMID:20018852</ref> <ref>PMID:20200153</ref>	+	[https://www.uniprot.org/uniprot/OGT1_HUMAN OGT1_HUMAN] Catalyzes the transfer of a single N-acetylglucosamine from UDP-GlcNAc to a serine or threonine residue in cytoplasmic and nuclear proteins resulting in their modification with a beta-linked N-acetylglucosamine (O-GlcNAc). Glycosylates a large and diverse number of proteins including histone H2B, AKT1, PFKL, KMT2E/MLL5, MAPT/TAU and HCFC1. Can regulate their cellular processes via cross-talk between glycosylation and phosphorylation or by affecting proteolytic processing. Involved in insulin resistance in muscle and adipocyte cells via glycosylating insulin signaling components and inhibiting the 'Thr-308' phosphorylation of AKT1, enhancing IRS1 phosphorylation and attenuating insulin signaling. Involved in glycolysis regulation by mediating glycosylation of 6-phosphofructokinase PFKL, inhibiting its activity. Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the regulation of the transcriptional activity of RRM1. Plays a key role in chromatin structure by mediating O-GlcNAcylation of 'Ser-112' of histone H2B: recruited to CpG-rich transcription start sites of active genes via its interaction with TET proteins (TET1, TET2 or TET3). As part of the NSL complex indirectly involved in acetylation of nucleosomal histone H4 on several lysine residues.<ref>PMID:12150998</ref> <ref>PMID:18288188</ref> <ref>PMID:19451179</ref> <ref>PMID:19377461</ref> <ref>PMID:20018852</ref> <ref>PMID:20018868</ref> <ref>PMID:20200153</ref> <ref>PMID:20824293</ref> <ref>PMID:21285374</ref> <ref>PMID:22121020</ref> <ref>PMID:22923583</ref> <ref>PMID:23353889</ref> <ref>PMID:23222540</ref> <ref>PMID:15361863</ref> <ref>PMID:21240259</ref> Isoform 2: the mitochondrial isoform (mOGT) is cytotoxic and triggers apoptosis in several cell types including INS1, an insulinoma cell line.<ref>PMID:12150998</ref> <ref>PMID:18288188</ref> <ref>PMID:19451179</ref> <ref>PMID:19377461</ref> <ref>PMID:20018852</ref> <ref>PMID:20018868</ref> <ref>PMID:20200153</ref> <ref>PMID:20824293</ref> <ref>PMID:21285374</ref> <ref>PMID:22121020</ref> <ref>PMID:22923583</ref> <ref>PMID:23353889</ref> <ref>PMID:23222540</ref> <ref>PMID:15361863</ref> <ref>PMID:21240259</ref> [https://www.uniprot.org/uniprot/HCFC1_HUMAN HCFC1_HUMAN] Involved in control of the cell cycle. Also antagonizes transactivation by ZBTB17 and GABP2; represses ZBTB17 activation of the p15(INK4b) promoter and inhibits its ability to recruit p300. Coactivator for EGR2 and GABP2. Tethers the chromatin modifying Set1/Ash2 histone H3 'Lys-4' methyltransferase (H3K4me) and Sin3 histone deacetylase (HDAC) complexes (involved in the activation and repression of transcription, respectively) together. Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the regulation of the transcriptional activity of RRM1. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. In case of human herpes simplex virus (HSV) infection, HCFC1 forms a multiprotein-DNA complex with the viral transactivator protein VP16 and POU2F1 thereby enabling the transcription of the viral immediate early genes.<ref>PMID:10920196</ref> <ref>PMID:9990006</ref> <ref>PMID:10675337</ref> <ref>PMID:10629049</ref> <ref>PMID:10779346</ref> <ref>PMID:12244100</ref> <ref>PMID:14532282</ref> <ref>PMID:12670868</ref> <ref>PMID:15190068</ref> <ref>PMID:16624878</ref> <ref>PMID:17578910</ref> <ref>PMID:20018852</ref> <ref>PMID:20200153</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 21:		Line 21:
	</div>		</div>
	<div class="pdbe-citations 5lwv" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5lwv" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[O-GlcNAc transferase 3D structures\|O-GlcNAc transferase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Protein O-GlcNAc transferase]]~~	+	[[Category: Herr W]]
-	~~[[Category: Aalten, D van]]~~	+	[[Category: Kapuria V]]
-	[[Category: Herr, W]]	+	[[Category: Rafie K]]
-	[[Category: Kapuria, V]]	+	[[Category: Raimi O]]
-	[[Category: Rafie, K]]	+	[[Category: Van Aalten D]]
-	[[Category: Raimi, O]]	+
-	[[Category: ~~Glycosylation]]~~	+
-	~~[[Category: O-glcnac]]~~	+
-	~~[[Category: O-glcnac transferase]]~~	+
-	~~[[Category: Signalling]]~~	+
-	~~[[Category: Substrate recognition]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 10:52, 12 August 2020

OCA — Wed, 12 Aug 2020 10:52:51 GMT

←Older revision		Revision as of 10:52, 12 August 2020
Line 1:		Line 1:

	==Human OGT in complex with UDP and fused substrate peptide (HCF1)==		==Human OGT in complex with UDP and fused substrate peptide (HCF1)==
-	<StructureSection load='5lwv' size='340' side='right' caption='[[5lwv]], [[Resolution\|resolution]] 1.90Å' scene=''>	+	<StructureSection load='5lwv' size='340' side='right'caption='[[5lwv]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5lwv]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LWV OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5LWV FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5lwv]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LWV OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5LWV FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein_O-GlcNAc_transferase Protein O-GlcNAc transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.255 2.4.1.255] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein_O-GlcNAc_transferase Protein O-GlcNAc transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.255 2.4.1.255] </span></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=5lwv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lwv OCA], [http://pdbe.org/5lwv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lwv RCSB], [http://www.ebi.ac.uk/pdbsum/5lwv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lwv ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5lwv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lwv OCA], [http://pdbe.org/5lwv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lwv RCSB], [http://www.ebi.ac.uk/pdbsum/5lwv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lwv ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 25:		Line 25:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Protein O-GlcNAc transferase]]		[[Category: Protein O-GlcNAc transferase]]
	[[Category: Aalten, D van]]		[[Category: Aalten, D van]]

OCA at 10:07, 10 September 2017

OCA — Sun, 10 Sep 2017 10:07:55 GMT

←Older revision		Revision as of 10:07, 10 September 2017
Line 1:		Line 1:
-	'''Unreleased structure'''

-	The entry ~~5lwv~~ is ~~ON HOLD~~ ~~until Paper~~ Publication	+	==Human OGT in complex with UDP and fused substrate peptide (HCF1)==
		+	<StructureSection load='5lwv' size='340' side='right' caption='[[5lwv]], [[Resolution\|resolution]] 1.90Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5lwv]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LWV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LWV FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein_O-GlcNAc_transferase Protein O-GlcNAc transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.255 2.4.1.255] </span></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=5lwv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lwv OCA], [http://pdbe.org/5lwv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lwv RCSB], [http://www.ebi.ac.uk/pdbsum/5lwv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lwv ProSAT]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/HCFC1_HUMAN HCFC1_HUMAN]] X-linked nonsyndromic intellectual deficit. Mental retardation, X-linked 3 (MRX3) [MIM:[http://omim.org/entry/309541 309541]]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptative behavior and manifested during the developmental period. Intellectual deficiency is the only primary symptom of non-syndromic X-linked mental retardation, while syndromic mental retardation presents with associated physical, neurological and/or psychiatric manifestations. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:23000143</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/HCFC1_HUMAN HCFC1_HUMAN]] Involved in control of the cell cycle. Also antagonizes transactivation by ZBTB17 and GABP2; represses ZBTB17 activation of the p15(INK4b) promoter and inhibits its ability to recruit p300. Coactivator for EGR2 and GABP2. Tethers the chromatin modifying Set1/Ash2 histone H3 'Lys-4' methyltransferase (H3K4me) and Sin3 histone deacetylase (HDAC) complexes (involved in the activation and repression of transcription, respectively) together. Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the regulation of the transcriptional activity of RRM1. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. In case of human herpes simplex virus (HSV) infection, HCFC1 forms a multiprotein-DNA complex with the viral transactivator protein VP16 and POU2F1 thereby enabling the transcription of the viral immediate early genes.<ref>PMID:10920196</ref> <ref>PMID:9990006</ref> <ref>PMID:10675337</ref> <ref>PMID:10629049</ref> <ref>PMID:10779346</ref> <ref>PMID:12244100</ref> <ref>PMID:14532282</ref> <ref>PMID:12670868</ref> <ref>PMID:15190068</ref> <ref>PMID:16624878</ref> <ref>PMID:17578910</ref> <ref>PMID:20018852</ref> <ref>PMID:20200153</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	O-linked N-acetylglucosamine (O-GlcNAc) is an essential and dynamic post-translational modification found on hundreds of nucleocytoplasmic proteins in metazoa. Although a single enzyme, O-GlcNAc transferase (OGT), generates the entire cytosolic O-GlcNAc proteome, it is not understood how it recognizes its protein substrates, targeting only a fraction of serines/threonines in the metazoan proteome for glycosylation. We describe a trapped complex of human OGT with the C-terminal domain of TAB1, a key innate immunity-signalling O-GlcNAc protein, revealing extensive interactions with the tetratricopeptide repeats of OGT. Confirmed by mutagenesis, this interaction suggests that glycosylation substrate specificity is achieved by recognition of a degenerate sequon in the active site combined with an extended conformation C-terminal of the O-GlcNAc target site.

-	~~Authors~~:	+	Recognition of a glycosylation substrate by the O-GlcNAc transferase TPR repeats.,Rafie K, Raimi O, Ferenbach AT, Borodkin VS, Kapuria V, van Aalten DMF Open Biol. 2017 Jun;7(6). pii: 170078. doi: 10.1098/rsob.170078. PMID:28659383<ref>PMID:28659383</ref>

-	~~Description~~:	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased Structures~~]]	+	</div>
		+	<div class="pdbe-citations 5lwv" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Protein O-GlcNAc transferase]]
		+	[[Category: Aalten, D van]]
		+	[[Category: Herr, W]]
		+	[[Category: Kapuria, V]]
		+	[[Category: Rafie, K]]
		+	[[Category: Raimi, O]]
		+	[[Category: Glycosylation]]
		+	[[Category: O-glcnac]]
		+	[[Category: O-glcnac transferase]]
		+	[[Category: Signalling]]
		+	[[Category: Substrate recognition]]
		+	[[Category: Transferase]]

OCA at 14:53, 19 October 2016

OCA — Wed, 19 Oct 2016 14:53:06 GMT

←Older revision		Revision as of 14:53, 19 October 2016
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5lwv is ON HOLD	+	The entry 5lwv is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "5lwv" [edit=sysop:move=sysop]

OCA — Mon, 03 Oct 2016 14:49:24 GMT

Protected "5lwv" [edit=sysop:move=sysop]

←Older revision

Revision as of 14:49, 3 October 2016

OCA: New page: '''Unreleased structure''' The entry 5lwv is ON HOLD Authors: Description: Category: Unreleased Structures

OCA — Mon, 03 Oct 2016 14:49:23 GMT

New page: '''Unreleased structure''' The entry 5lwv is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 5lwv is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]