6qsb - Revision history

OCA at 12:07, 24 January 2024

OCA — Wed, 24 Jan 2024 12:07:31 GMT

←Older revision		Revision as of 12:07, 24 January 2024
Line 3:		Line 3:
	<StructureSection load='6qsb' size='340' side='right'caption='[[6qsb]], [[Resolution\|resolution]] 1.99Å' scene=''>		<StructureSection load='6qsb' size='340' side='right'caption='[[6qsb]], [[Resolution\|resolution]] 1.99Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6qsb]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QSB OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6QSB FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6qsb]] is a 2 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=6QSB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QSB 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=MN:MANGANESE+(II)+ION'>MN</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]] 1.99Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~>[[5m4g\|5m4g]], [[5m4j\|5m4j]], [[5mbz\|5mbz]]</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=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
-	~~<tr~~ id~~='activity'><td class~~="~~sblockLbl~~"><~~b>Activity~~:~~</b~~></td><~~td class~~=~~"sblockDat"><span class~~=~~'plainlinks~~'>~~[http://en.wikipedia.org/wiki/Xaa-Pro_dipeptidase Xaa-Pro dipeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.13.9 3.4.13.9]~~ </~~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=6qsb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qsb OCA], [https://pdbe.org/6qsb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qsb RCSB], [https://www.ebi.ac.uk/pdbsum/6qsb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qsb ProSAT]</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=6qsb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qsb OCA], [~~http~~://pdbe.org/6qsb PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6qsb RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6qsb PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6qsb ProSAT]</span></td></tr>	+
	</table>		</table>
	== Disease ==		== Disease ==
-	[~~[http~~://www.uniprot.org/uniprot/PEPD_HUMAN PEPD_HUMAN]] Defects in PEPD are a cause of prolidase deficiency (PD) [MIM:[~~http~~://omim.org/entry/170100 170100]]. Prolidase deficiency is an autosomal recessive disorder associated with iminodipeptiduria. The clinical phenotype includes skin ulcers, mental retardation, recurrent infections, and a characteristic facies. These features, however are incompletely penetrant and highly variable in both age of onset and severity. There is a tight linkage between the polymorphisms of prolidase and the myotonic dystrophy trait.<ref>PMID:2365824</ref> <ref>PMID:8198124</ref> <ref>PMID:8900231</ref> <ref>PMID:12384772</ref>	+	[https://www.uniprot.org/uniprot/PEPD_HUMAN PEPD_HUMAN] Defects in PEPD are a cause of prolidase deficiency (PD) [MIM:[https://omim.org/entry/170100 170100]. Prolidase deficiency is an autosomal recessive disorder associated with iminodipeptiduria. The clinical phenotype includes skin ulcers, mental retardation, recurrent infections, and a characteristic facies. These features, however are incompletely penetrant and highly variable in both age of onset and severity. There is a tight linkage between the polymorphisms of prolidase and the myotonic dystrophy trait.<ref>PMID:2365824</ref> <ref>PMID:8198124</ref> <ref>PMID:8900231</ref> <ref>PMID:12384772</ref>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/PEPD_HUMAN PEPD_HUMAN]] Splits dipeptides with a prolyl or hydroxyprolyl residue in the C-terminal position. Plays an important role in collagen metabolism because the high level of iminoacids in collagen.	+	[https://www.uniprot.org/uniprot/PEPD_HUMAN PEPD_HUMAN] Splits dipeptides with a prolyl or hydroxyprolyl residue in the C-terminal position. Plays an important role in collagen metabolism because the high level of iminoacids in collagen.
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Xaa-Pro dipeptidase]]~~	+	[[Category: Wator E]]
-	[[Category: Wator, E]]	+	[[Category: Weiss MS]]
-	[[Category: Weiss~~, M S~~]]	+	[[Category: Wilk P]]
-	[[Category: Wilk, P]]	+
-	~~[[Category: Dipeptidase]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Metal binding]]~~	+
-	~~[[Category: Mutation~~]]	+

OCA at 09:47, 18 March 2020

OCA — Wed, 18 Mar 2020 09:47:10 GMT

←Older revision		Revision as of 09:47, 18 March 2020
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 6qsb is ~~ON HOLD until Feb 20 2021~~	+	==Crystal Structure of Arg470His mutant of Human Prolidase with Mn ions==
-		+	<StructureSection load='6qsb' size='340' side='right'caption='[[6qsb]], [[Resolution\|resolution]] 1.99Å' scene=''>
-	~~Authors~~: ~~Wilk~~, P., ~~Wator~~, E., ~~Weiss~~, M.S.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[6qsb]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QSB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6QSB FirstGlance]. <br>
-	~~Description~~: ~~Crystal Structure~~ of ~~Arg470His mutant of Human~~ Prolidase with ~~Mn ions~~	+	</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=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
-	[[Category: ~~Unreleased~~ Structures]]	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5m4g\|5m4g]], [[5m4j\|5m4j]], [[5mbz\|5mbz]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Xaa-Pro_dipeptidase Xaa-Pro dipeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.13.9 3.4.13.9] </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=6qsb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qsb OCA], [http://pdbe.org/6qsb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qsb RCSB], [http://www.ebi.ac.uk/pdbsum/6qsb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qsb ProSAT]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/PEPD_HUMAN PEPD_HUMAN]] Defects in PEPD are a cause of prolidase deficiency (PD) [MIM:[http://omim.org/entry/170100 170100]]. Prolidase deficiency is an autosomal recessive disorder associated with iminodipeptiduria. The clinical phenotype includes skin ulcers, mental retardation, recurrent infections, and a characteristic facies. These features, however are incompletely penetrant and highly variable in both age of onset and severity. There is a tight linkage between the polymorphisms of prolidase and the myotonic dystrophy trait.<ref>PMID:2365824</ref> <ref>PMID:8198124</ref> <ref>PMID:8900231</ref> <ref>PMID:12384772</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PEPD_HUMAN PEPD_HUMAN]] Splits dipeptides with a prolyl or hydroxyprolyl residue in the C-terminal position. Plays an important role in collagen metabolism because the high level of iminoacids in collagen.
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Xaa-Pro dipeptidase]]
		+	[[Category: Wator, E]]
		+	[[Category: Weiss, M S]]
	[[Category: Wilk, P]]		[[Category: Wilk, P]]
-	[[Category: ~~Wator, E~~]]	+	[[Category: Dipeptidase]]
-	[[Category: ~~Weiss, M.S~~]]	+	[[Category: Hydrolase]]
		+	[[Category: Metal binding]]
		+	[[Category: Mutation]]

OCA at 06:05, 20 March 2019

OCA — Wed, 20 Mar 2019 06:05:26 GMT

←Older revision		Revision as of 06:05, 20 March 2019
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6qsb is ON HOLD	+	The entry 6qsb is ON HOLD until Feb 20 2021

	Authors: Wilk, P., Wator, E., Weiss, M.S.		Authors: Wilk, P., Wator, E., Weiss, M.S.

OCA: Protected "6qsb" [edit=sysop:move=sysop]

OCA — Wed, 27 Feb 2019 14:01:13 GMT

Protected "6qsb" [edit=sysop:move=sysop]

←Older revision

Revision as of 14:01, 27 February 2019

OCA: New page: '''Unreleased structure''' The entry 6qsb is ON HOLD Authors: Wilk, P., Wator, E., Weiss, M.S. Description: Crystal Structure of Arg470His mutant of Human Prolidase with Mn ions [[Cate...

OCA — Wed, 27 Feb 2019 14:01:12 GMT

New page: '''Unreleased structure''' The entry 6qsb is ON HOLD Authors: Wilk, P., Wator, E., Weiss, M.S. Description: Crystal Structure of Arg470His mutant of Human Prolidase with Mn ions [[Cate...

New page

'''Unreleased structure'''

The entry 6qsb is ON HOLD

Authors: Wilk, P., Wator, E., Weiss, M.S.

Description: Crystal Structure of Arg470His mutant of Human Prolidase with Mn ions
[[Category: Unreleased Structures]]
[[Category: Wilk, P]]
[[Category: Wator, E]]
[[Category: Weiss, M.S]]