1f6w - Revision history

OCA at 06:02, 9 August 2023

OCA — Wed, 09 Aug 2023 06:02:41 GMT

←Older revision		Revision as of 06:02, 9 August 2023
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	<StructureSection load='1f6w' size='340' side='right'caption='[[1f6w]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='1f6w' size='340' side='right'caption='[[1f6w]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1f6w]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F6W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F6W FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1f6w]] 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=1F6W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F6W FirstGlance]. <br>
-	</td></tr><tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat">~~<div style='overflow: auto; max~~-~~height: 3em;'>~~[[~~1akn~~\|~~1akn~~]]~~</div></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]] 2.3Å</td></tr>
-	~~<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en~~.~~wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=~~3~~.1.1.3 3.1.1.3] </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=1f6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f6w OCA], [https://pdbe.org/1f6w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f6w RCSB], [https://www.ebi.ac.uk/pdbsum/1f6w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f6w 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=1f6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f6w OCA], [https://pdbe.org/1f6w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f6w RCSB], [https://www.ebi.ac.uk/pdbsum/1f6w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f6w ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/CEL_HUMAN CEL_HUMAN]] Defects in CEL are a cause of maturity-onset diabetes of the young type 8 with exocrine dysfunction (MODY8) [MIM:[https://omim.org/entry/609812 609812]]; also known as diabetes and pancreatic exocrine dysfunction (DPED). MODY is a form of diabetes that is characterized by an autosomal dominant mode of inheritance, onset in childhood or early adulthood (usually before 25 years of age), a primary defect in insulin secretion and frequent insulin-independence at the beginning of the disease.<ref>PMID:16369531</ref>	+	[https://www.uniprot.org/uniprot/CEL_HUMAN CEL_HUMAN] Defects in CEL are a cause of maturity-onset diabetes of the young type 8 with exocrine dysfunction (MODY8) [MIM:[https://omim.org/entry/609812 609812]; also known as diabetes and pancreatic exocrine dysfunction (DPED). MODY is a form of diabetes that is characterized by an autosomal dominant mode of inheritance, onset in childhood or early adulthood (usually before 25 years of age), a primary defect in insulin secretion and frequent insulin-independence at the beginning of the disease.<ref>PMID:16369531</ref>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/CEL_HUMAN CEL_HUMAN]] Catalyzes fat and vitamin absorption. Acts in concert with pancreatic lipase and colipase for the complete digestion of dietary triglycerides.	+	[https://www.uniprot.org/uniprot/CEL_HUMAN CEL_HUMAN] Catalyzes fat and vitamin absorption. Acts in concert with pancreatic lipase and colipase for the complete digestion of dietary triglycerides.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Triacylglycerol lipase]]~~	+	[[Category: Terzyan S]]
-	[[Category: Terzyan, S]]	+	[[Category: Zhang X]]
-	[[Category: Zhang, X]]	+
-	~~[[Category: Bile salt activated lipase]]~~	+
-	~~[[Category: Catalytic domain]]~~	+
-	~~[[Category: Esterase]]~~	+
-	~~[[Category: Hydrolase~~]]	+

OCA at 09:47, 21 July 2021

OCA — Wed, 21 Jul 2021 09:47:01 GMT

←Older revision		Revision as of 09:47, 21 July 2021
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	<StructureSection load='1f6w' size='340' side='right'caption='[[1f6w]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='1f6w' size='340' side='right'caption='[[1f6w]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1f6w]] is a 1 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=1F6W OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1F6W FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1f6w]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F6W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F6W FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1akn\|1akn]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1akn\|1akn]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] </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=1f6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f6w OCA], [~~http~~://pdbe.org/1f6w PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1f6w RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1f6w PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1f6w 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=1f6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f6w OCA], [https://pdbe.org/1f6w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f6w RCSB], [https://www.ebi.ac.uk/pdbsum/1f6w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f6w ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/CEL_HUMAN CEL_HUMAN]] Defects in CEL are a cause of maturity-onset diabetes of the young type 8 with exocrine dysfunction (MODY8) [MIM:[~~http~~://omim.org/entry/609812 609812]]; also known as diabetes and pancreatic exocrine dysfunction (DPED). MODY is a form of diabetes that is characterized by an autosomal dominant mode of inheritance, onset in childhood or early adulthood (usually before 25 years of age), a primary defect in insulin secretion and frequent insulin-independence at the beginning of the disease.<ref>PMID:16369531</ref>	+	[[https://www.uniprot.org/uniprot/CEL_HUMAN CEL_HUMAN]] Defects in CEL are a cause of maturity-onset diabetes of the young type 8 with exocrine dysfunction (MODY8) [MIM:[https://omim.org/entry/609812 609812]]; also known as diabetes and pancreatic exocrine dysfunction (DPED). MODY is a form of diabetes that is characterized by an autosomal dominant mode of inheritance, onset in childhood or early adulthood (usually before 25 years of age), a primary defect in insulin secretion and frequent insulin-independence at the beginning of the disease.<ref>PMID:16369531</ref>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/CEL_HUMAN CEL_HUMAN]] Catalyzes fat and vitamin absorption. Acts in concert with pancreatic lipase and colipase for the complete digestion of dietary triglycerides.	+	[[https://www.uniprot.org/uniprot/CEL_HUMAN CEL_HUMAN]] Catalyzes fat and vitamin absorption. Acts in concert with pancreatic lipase and colipase for the complete digestion of dietary triglycerides.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	==See Also==		==See Also==
	*[[Cholesterol esterase 3D structures\|Cholesterol esterase 3D structures]]		*[[Cholesterol esterase 3D structures\|Cholesterol esterase 3D structures]]
-	*[[Lipase\|Lipase]]	+	*[[Lipase 3D Structures\|Lipase 3D Structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 13:15, 16 October 2019

OCA — Wed, 16 Oct 2019 13:15:18 GMT

←Older revision		Revision as of 13:15, 16 October 2019
Line 1:		Line 1:

	==STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN BILE SALT ACTIVATED LIPASE==		==STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN BILE SALT ACTIVATED LIPASE==
-	<StructureSection load='1f6w' size='340' side='right' caption='[[1f6w]], [[Resolution\|resolution]] 2.30Å' scene=''>	+	<StructureSection load='1f6w' size='340' side='right'caption='[[1f6w]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1f6w]] is a 1 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=1F6W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F6W FirstGlance]. <br>		<table><tr><td colspan='2'>[[1f6w]] is a 1 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=1F6W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F6W FirstGlance]. <br>
Line 31:		Line 31:
	</div>		</div>
	<div class="pdbe-citations 1f6w" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1f6w" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Cholesterol esterase 3D structures\|Cholesterol esterase 3D structures]]
		+	*[[Lipase\|Lipase]]
	== References ==		== References ==
	<references/>		<references/>
Line 36:		Line 40:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Triacylglycerol lipase]]		[[Category: Triacylglycerol lipase]]
	[[Category: Terzyan, S]]		[[Category: Terzyan, S]]

OCA at 09:23, 27 December 2017

OCA — Wed, 27 Dec 2017 09:23:24 GMT

←Older revision		Revision as of 09:23, 27 December 2017
Line 1:		Line 1:
		+
	==STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN BILE SALT ACTIVATED LIPASE==		==STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN BILE SALT ACTIVATED LIPASE==
	<StructureSection load='1f6w' size='340' side='right' caption='[[1f6w]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='1f6w' size='340' side='right' caption='[[1f6w]], [[Resolution\|resolution]] 2.30Å' scene=''>
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	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1akn\|1akn]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1akn\|1akn]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] </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=1f6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f6w OCA], [http://pdbe.org/1f6w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1f6w RCSB], [http://www.ebi.ac.uk/pdbsum/1f6w PDBsum]</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=1f6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f6w OCA], [http://pdbe.org/1f6w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1f6w RCSB], [http://www.ebi.ac.uk/pdbsum/1f6w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1f6w ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f6/1f6w_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f6/1f6w_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 30:		Line 31:
	</div>		</div>
	<div class="pdbe-citations 1f6w" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1f6w" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Cholesterol esterase\|Cholesterol esterase]]
-	*[[Lipase\|Lipase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 06:29, 9 February 2016

OCA — Tue, 09 Feb 2016 06:29:29 GMT

←Older revision		Revision as of 06:29, 9 February 2016
Line 19:		Line 19:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1f6w ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 19:30, 10 September 2015

OCA — Thu, 10 Sep 2015 19:30:44 GMT

←Older revision		Revision as of 19:30, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1f6w' size='340' side='right' caption='[[1f6w]], [[Resolution\|resolution]] 2.30Å' scene=''>		<StructureSection load='1f6w' size='340' side='right' caption='[[1f6w]], [[Resolution\|resolution]] 2.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1f6w]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F6W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F6W FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1f6w]] is a 1 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=1F6W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F6W FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1akn\|1akn]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1akn\|1akn]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] </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=1f6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f6w OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1f6w RCSB], [http://www.ebi.ac.uk/pdbsum/1f6w PDBsum]</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=1f6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f6w OCA], [http://pdbe.org/1f6w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1f6w RCSB], [http://www.ebi.ac.uk/pdbsum/1f6w PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 29:		Line 29:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 1f6w" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 37:		Line 38:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Triacylglycerol lipase]]		[[Category: Triacylglycerol lipase]]
	[[Category: Terzyan, S]]		[[Category: Terzyan, S]]

OCA at 22:12, 22 December 2014

OCA — Mon, 22 Dec 2014 22:12:58 GMT

←Older revision		Revision as of 22:12, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1f6w]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F6W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F6W FirstGlance]. <br>		<table><tr><td colspan='2'>[[1f6w]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F6W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F6W FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1akn\|1akn]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1akn\|1akn]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] </span></td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1f6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f6w OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1f6w RCSB], [http://www.ebi.ac.uk/pdbsum/1f6w PDBsum]</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=1f6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f6w OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1f6w RCSB], [http://www.ebi.ac.uk/pdbsum/1f6w PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/CEL_HUMAN CEL_HUMAN]] Defects in CEL are a cause of maturity-onset diabetes of the young type 8 with exocrine dysfunction (MODY8) [MIM:[http://omim.org/entry/609812 609812]]; also known as diabetes and pancreatic exocrine dysfunction (DPED). MODY is a form of diabetes that is characterized by an autosomal dominant mode of inheritance, onset in childhood or early adulthood (usually before 25 years of age), a primary defect in insulin secretion and frequent insulin-independence at the beginning of the disease.<ref>PMID:16369531</ref>		[[http://www.uniprot.org/uniprot/CEL_HUMAN CEL_HUMAN]] Defects in CEL are a cause of maturity-onset diabetes of the young type 8 with exocrine dysfunction (MODY8) [MIM:[http://omim.org/entry/609812 609812]]; also known as diabetes and pancreatic exocrine dysfunction (DPED). MODY is a form of diabetes that is characterized by an autosomal dominant mode of inheritance, onset in childhood or early adulthood (usually before 25 years of age), a primary defect in insulin secretion and frequent insulin-independence at the beginning of the disease.<ref>PMID:16369531</ref>
Line 39:		Line 39:
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Triacylglycerol lipase]]		[[Category: Triacylglycerol lipase]]
-	[[Category: Terzyan, S.]]	+	[[Category: Terzyan, S]]
-	[[Category: Zhang, X.]]	+	[[Category: Zhang, X]]
	[[Category: Bile salt activated lipase]]		[[Category: Bile salt activated lipase]]
	[[Category: Catalytic domain]]		[[Category: Catalytic domain]]
	[[Category: Esterase]]		[[Category: Esterase]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

OCA at 16:06, 29 September 2014

OCA — Mon, 29 Sep 2014 16:06:23 GMT

←Older revision		Revision as of 16:06, 29 September 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_1f6w\| PDB=1f6w \| SCENE= }}~~	+	==STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN BILE SALT ACTIVATED LIPASE==
-	===STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN BILE SALT ACTIVATED LIPASE===	+	<StructureSection load='1f6w' size='340' side='right' caption='[[1f6w]], [[Resolution\|resolution]] 2.30Å' scene=''>
-	~~{{ABSTRACT_PUBMED_11045623}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1f6w]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F6W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F6W FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1akn\|1akn]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] </span></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1f6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f6w OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1f6w RCSB], [http://www.ebi.ac.uk/pdbsum/1f6w PDBsum]</span></td></tr>
		+	<table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/CEL_HUMAN CEL_HUMAN]] Defects in CEL are a cause of maturity-onset diabetes of the young type 8 with exocrine dysfunction (MODY8) [MIM:[http://omim.org/entry/609812 609812]]; also known as diabetes and pancreatic exocrine dysfunction (DPED). MODY is a form of diabetes that is characterized by an autosomal dominant mode of inheritance, onset in childhood or early adulthood (usually before 25 years of age), a primary defect in insulin secretion and frequent insulin-independence at the beginning of the disease.<ref>PMID:16369531</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/CEL_HUMAN CEL_HUMAN]] Catalyzes fat and vitamin absorption. Acts in concert with pancreatic lipase and colipase for the complete digestion of dietary triglycerides.
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f6/1f6w_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Bile-salt activated lipase (BAL) is a pancreatic enzyme that digests a variety of lipids in the small intestine. A distinct property of BAL is its dependency on bile salts in hydrolyzing substrates of long acyl chains or bulky alcoholic motifs. A crystal structure of the catalytic domain of human BAL (residues 1-538) with two surface mutations (N186D and A298D), which were introduced in attempting to facilitate crystallization, has been determined at 2.3 A resolution. The crystal form belongs to space group P2(1)2(1)2(1) with one monomer per asymmetric unit, and the protein shows an alpha/beta hydrolase fold. In the absence of bound bile salt molecules, the protein possesses a preformed catalytic triad and a functional oxyanion hole. Several surface loops around the active site are mobile, including two loops potentially involved in substrate binding (residues 115-125 and 270-285).

-	~~==Disease==~~	+	Crystal structure of the catalytic domain of human bile salt activated lipase.,Terzyan S, Wang CS, Downs D, Hunter B, Zhang XC Protein Sci. 2000 Sep;9(9):1783-90. PMID:11045623<ref>PMID:11045623</ref>
-	~~[[http://www.uniprot.org/uniprot/CEL_HUMAN CEL_HUMAN]] Defects in CEL are a cause~~ of ~~maturity-onset diabetes~~ of ~~the young type 8 with exocrine dysfunction (MODY8) [MIM:[http://omim~~.~~org/entry/609812 609812]]~~; ~~also known as diabetes and pancreatic exocrine dysfunction~~ (~~DPED~~). MODY is a form of diabetes that is characterized by an autosomal dominant mode of inheritance, onset in childhood or early adulthood (usually before 25 years of age), a primary defect in insulin secretion and frequent insulin-~~independence at the beginning of the disease~~.<ref>PMID:~~16369531~~</ref>	+

-	~~==Function==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[http:~~/~~/www~~.~~uniprot~~.~~org/uniprot/CEL_HUMAN CEL_HUMAN]] Catalyzes fat and vitamin absorption. Acts in concert with pancreatic lipase and colipase for the complete digestion~~ of ~~dietary triglycerides~~.	+	</div>
-		+
-	~~==About this Structure==~~	+
-	~~[[1f6w]] is a 1 chain structure with sequence from [http:~~/~~/en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F6W OCA].~~	+

	==See Also==		==See Also==
	*[[Cholesterol esterase\|Cholesterol esterase]]		*[[Cholesterol esterase\|Cholesterol esterase]]
	*[[Lipase\|Lipase]]		*[[Lipase\|Lipase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:011045623</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Triacylglycerol lipase]]		[[Category: Triacylglycerol lipase]]

OCA at 03:49, 25 March 2013

OCA — Mon, 25 Mar 2013 03:49:31 GMT

←Older revision		Revision as of 03:49, 25 March 2013
Line 1:		Line 1:
-	[[Image:1f6w.png\|left\|200px]]
-
	{{STRUCTURE_1f6w\| PDB=1f6w \| SCENE= }}		{{STRUCTURE_1f6w\| PDB=1f6w \| SCENE= }}
-
	===STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN BILE SALT ACTIVATED LIPASE===		===STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN BILE SALT ACTIVATED LIPASE===
		+	{{ABSTRACT_PUBMED_11045623}}

-	~~{{ABSTRACT_PUBMED_11045623}}~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/CEL_HUMAN CEL_HUMAN]] Defects in CEL are a cause of maturity-onset diabetes of the young type 8 with exocrine dysfunction (MODY8) [MIM:[http://omim.org/entry/609812 609812]]; also known as diabetes and pancreatic exocrine dysfunction (DPED). MODY is a form of diabetes that is characterized by an autosomal dominant mode of inheritance, onset in childhood or early adulthood (usually before 25 years of age), a primary defect in insulin secretion and frequent insulin-independence at the beginning of the disease.<ref>PMID:16369531</ref>
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/CEL_HUMAN CEL_HUMAN]] Catalyzes fat and vitamin absorption. Acts in concert with pancreatic lipase and colipase for the complete digestion of dietary triglycerides.

	==About this Structure==		==About this Structure==
Line 11:		Line 13:

	==See Also==		==See Also==
		+	*[[Cholesterol esterase\|Cholesterol esterase]]
	*[[Lipase\|Lipase]]		*[[Lipase\|Lipase]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:011045623</ref><references group="xtra"/>	+	<ref group="xtra">PMID:011045623</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Triacylglycerol lipase]]		[[Category: Triacylglycerol lipase]]

OCA at 12:58, 20 October 2012

OCA — Sat, 20 Oct 2012 12:58:15 GMT

←Older revision		Revision as of 12:58, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1f6w]] is a 1 chain structure ~~of [[Lipase]]~~ with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F6W OCA].	+	[[1f6w]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F6W OCA].

	==See Also==		==See Also==