1apy - Revision history

OCA at 07:11, 9 October 2024

2024-10-09T07:11:32Z

← Older revision		Revision as of 07:11, 9 October 2024
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	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ap/1apy_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ap/1apy_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/~~initialview01~~.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
	<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/main_output.php?pdb_ID=1apy 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=1apy ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			The high resolution crystal structure of human lysosomal aspartylglucosaminidase (AGA) has been determined. This lysosomal enzyme is synthesized as a single polypeptide precursor, which is immediately post-translationally cleaved into alpha- and beta-subunits. Two alpha- and beta-chains are found to pack together forming the final heterotetrameric structure. The catalytically essential residue, the N-terminal threonine of the beta-chain is situated in the deep pocket of the funnel-shaped active site. On the basis of the structure of the enzyme-product complex we present a catalytic mechanism for this lysosomal enzyme with an exceptionally high pH optimum. The three-dimensional structure also allows the prediction of the structural consequences of human mutations resulting in aspartylglucosaminuria (AGU), a lysosomal storage disease.

			Three-dimensional structure of human lysosomal aspartylglucosaminidase.,Oinonen C, Tikkanen R, Rouvinen J, Peltonen L Nat Struct Biol. 1995 Dec;2(12):1102-8. PMID:8846222<ref>PMID:8846222</ref>

			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
			<div class="pdbe-citations 1apy" style="background-color:#fffaf0;"></div>

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

OCA at 15:27, 13 March 2024

2024-03-13T15:27:16Z

← Older revision		Revision as of 15:27, 13 March 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1apy]] 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=1APY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1APY FirstGlance]. <br>		<table><tr><td colspan='2'>[[1apy]] 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=1APY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1APY FirstGlance]. <br>
	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=BMA:BETA-D~~-~~MANNOSE'>BMA</scene>~~, ~~<scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 2Å</td></tr>
	<tr id='~~activity~~'><td class="sblockLbl"><b>~~Activity~~:</b></td><td class="sblockDat"><~~span class~~='~~plainlinks~~'>~~[https~~:~~//en.wikipedia.org/wiki/~~N~~(4)~~-~~(beta~~-N-~~acetylglucosaminyl)-L-asparaginase N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.26 3.5.1.26]~~ </~~span~~></td></tr>		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=1apy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1apy OCA], [https://pdbe.org/1apy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1apy RCSB], [https://www.ebi.ac.uk/pdbsum/1apy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1apy 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=1apy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1apy OCA], [https://pdbe.org/1apy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1apy RCSB], [https://www.ebi.ac.uk/pdbsum/1apy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1apy ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
	[[https://www.uniprot.org/uniprot/ASPG_HUMAN ASPG_HUMAN]] Defects in AGA are the cause of aspartylglucosaminuria (AGU) [MIM:[https://omim.org/entry/208400 208400]]. AGU is an inborn lysosomal storage disease. Clinical features of AGU include mild to severe mental retardation manifesting from the age of 2, coarse facial features and mild connective tissue abnormalities. This recessively inherited disease is overrepresented in the Finnish population.<ref>PMID:1703489</ref> <ref>PMID:1904874</ref> <ref>PMID:2011603</ref> <ref>PMID:8776587</ref> <ref>PMID:9137882</ref> <ref>PMID:11309371</ref>		[https://www.uniprot.org/uniprot/ASPG_HUMAN ASPG_HUMAN] Defects in AGA are the cause of aspartylglucosaminuria (AGU) [MIM:[https://omim.org/entry/208400 208400]. AGU is an inborn lysosomal storage disease. Clinical features of AGU include mild to severe mental retardation manifesting from the age of 2, coarse facial features and mild connective tissue abnormalities. This recessively inherited disease is overrepresented in the Finnish population.<ref>PMID:1703489</ref> <ref>PMID:1904874</ref> <ref>PMID:2011603</ref> <ref>PMID:8776587</ref> <ref>PMID:9137882</ref> <ref>PMID:11309371</ref>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/ASPG_HUMAN ASPG_HUMAN]] Cleaves the GlcNAc-Asn bond which joins oligosaccharides to the peptide of asparagine-linked glycoproteins.		[https://www.uniprot.org/uniprot/ASPG_HUMAN ASPG_HUMAN] Cleaves the GlcNAc-Asn bond which joins oligosaccharides to the peptide of asparagine-linked glycoproteins.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</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=1apy 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=1apy ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	The high resolution crystal structure of human lysosomal aspartylglucosaminidase (AGA) has been determined. This lysosomal enzyme is synthesized as a single polypeptide precursor, which is immediately post-translationally cleaved into alpha- and beta-subunits. Two alpha- and beta-chains are found to pack together forming the final heterotetrameric structure. The catalytically essential residue, the N-terminal threonine of the beta-chain is situated in the deep pocket of the funnel-shaped active site. On the basis of the structure of the enzyme-product complex we present a catalytic mechanism for this lysosomal enzyme with an exceptionally high pH optimum. The three-dimensional structure also allows the prediction of the structural consequences of human mutations resulting in aspartylglucosaminuria (AGU), a lysosomal storage disease.

	~~Three-dimensional structure of human lysosomal aspartylglucosaminidase.,Oinonen C, Tikkanen R, Rouvinen J, Peltonen L Nat Struct Biol. 1995 Dec;2(12):1102-8. PMID:8846222<ref>PMID:8846222</ref>~~

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 1apy" style="background-color:#fffaf0;"></div>~~

	==See Also==		==See Also==
Line 40:		Line 31:
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Oinonen, C]]		[[Category: Oinonen C]]
	[[Category: Rouvinen, J]]		[[Category: Rouvinen J]]
	~~[[Category: Aspartylglucosaminidase]]~~
	~~[[Category: Glycosylasparaginase]]~~
	~~[[Category: Hydrolase~~]]

OCA at 09:47, 26 May 2021

2021-05-26T09:47:49Z

OCA at 07:49, 21 August 2019

2019-08-21T07:49:16Z

← Older revision		Revision as of 07:49, 21 August 2019
Line 1:		Line 1:

	==HUMAN ASPARTYLGLUCOSAMINIDASE==		==HUMAN ASPARTYLGLUCOSAMINIDASE==
	<StructureSection load='1apy' size='340' side='right' caption='[[1apy]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='1apy' size='340' side='right'caption='[[1apy]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1apy]] is a 4 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=1APY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1APY FirstGlance]. <br>		<table><tr><td colspan='2'>[[1apy]] is a 4 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=1APY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1APY FirstGlance]. <br>
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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/ap/1apy_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ap/1apy_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 31:		Line 31:
	</div>		</div>
	<div class="pdbe-citations 1apy" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1apy" style="background-color:#fffaf0;"></div>

			==See Also==
			*[[Glycosylasparaginase\|Glycosylasparaginase]]
	== References ==		== References ==
	<references/>		<references/>
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	</StructureSection>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
			[[Category: Large Structures]]
	[[Category: Oinonen, C]]		[[Category: Oinonen, C]]
	[[Category: Rouvinen, J]]		[[Category: Rouvinen, J]]

OCA at 10:47, 15 November 2017

2017-11-15T10:47:50Z

← Older revision		Revision as of 10:47, 15 November 2017
Line 1:		Line 1:

	==HUMAN ASPARTYLGLUCOSAMINIDASE==		==HUMAN ASPARTYLGLUCOSAMINIDASE==
	<StructureSection load='1apy' size='340' side='right' caption='[[1apy]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='1apy' size='340' side='right' caption='[[1apy]], [[Resolution\|resolution]] 2.00Å' scene=''>
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	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.26 3.5.1.26] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.26 3.5.1.26] </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=1apy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1apy OCA], [http://pdbe.org/1apy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1apy RCSB], [http://www.ebi.ac.uk/pdbsum/1apy 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=1apy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1apy OCA], [http://pdbe.org/1apy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1apy RCSB], [http://www.ebi.ac.uk/pdbsum/1apy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1apy ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
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	</div>		</div>
	<div class="pdbe-citations 1apy" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1apy" style="background-color:#fffaf0;"></div>

	~~==See Also==~~
	*[[Glycosylasparaginase\|Glycosylasparaginase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 02:18, 10 February 2016

2016-02-10T02:18:16Z

← Older revision		Revision as of 02:18, 10 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=1apy ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 04:23, 11 September 2015

2015-09-11T04:23:52Z

← Older revision		Revision as of 04:23, 11 September 2015
Line 5:		Line 5:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.26 3.5.1.26] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.26 3.5.1.26] </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=1apy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1apy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1apy RCSB], [http://www.ebi.ac.uk/pdbsum/1apy 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=1apy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1apy OCA], [http://pdbe.org/1apy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1apy RCSB], [http://www.ebi.ac.uk/pdbsum/1apy PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
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	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 1apy" style="background-color:#fffaf0;"></div>

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

OCA at 12:08, 22 December 2014

2014-12-22T12:08:53Z

← Older revision		Revision as of 12:08, 22 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1apy]] is a 4 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=1APY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1APY FirstGlance]. <br>		<table><tr><td colspan='2'>[[1apy]] is a 4 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=1APY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1APY FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene><br>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.26 3.5.1.26] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.26 3.5.1.26] </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=1apy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1apy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1apy RCSB], [http://www.ebi.ac.uk/pdbsum/1apy 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=1apy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1apy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1apy RCSB], [http://www.ebi.ac.uk/pdbsum/1apy PDBsum]</span></td></tr>
	<table>		</table>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/ASPG_HUMAN ASPG_HUMAN]] Defects in AGA are the cause of aspartylglucosaminuria (AGU) [MIM:[http://omim.org/entry/208400 208400]]. AGU is an inborn lysosomal storage disease. Clinical features of AGU include mild to severe mental retardation manifesting from the age of 2, coarse facial features and mild connective tissue abnormalities. This recessively inherited disease is overrepresented in the Finnish population.<ref>PMID:1703489</ref> <ref>PMID:1904874</ref> <ref>PMID:2011603</ref> <ref>PMID:8776587</ref> <ref>PMID:9137882</ref> <ref>PMID:11309371</ref>		[[http://www.uniprot.org/uniprot/ASPG_HUMAN ASPG_HUMAN]] Defects in AGA are the cause of aspartylglucosaminuria (AGU) [MIM:[http://omim.org/entry/208400 208400]]. AGU is an inborn lysosomal storage disease. Clinical features of AGU include mild to severe mental retardation manifesting from the age of 2, coarse facial features and mild connective tissue abnormalities. This recessively inherited disease is overrepresented in the Finnish population.<ref>PMID:1703489</ref> <ref>PMID:1904874</ref> <ref>PMID:2011603</ref> <ref>PMID:8776587</ref> <ref>PMID:9137882</ref> <ref>PMID:11309371</ref>
Line 37:		Line 37:
	</StructureSection>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Oinonen, C.]]		[[Category: Oinonen, C]]
	[[Category: Rouvinen, J.]]		[[Category: Rouvinen, J]]
	[[Category: Aspartylglucosaminidase]]		[[Category: Aspartylglucosaminidase]]
	[[Category: Glycosylasparaginase]]		[[Category: Glycosylasparaginase]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

OCA at 17:38, 29 September 2014

2014-09-29T17:38:04Z

@@ Line 1: / Line 1: @@
-{{STRUCTURE_1apy|  PDB=1apy  |  SCENE=  }}
+==HUMAN ASPARTYLGLUCOSAMINIDASE==
-===HUMAN ASPARTYLGLUCOSAMINIDASE===
+<StructureSection load='1apy' size='340' side='right' caption='[[1apy]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-{{ABSTRACT_PUBMED_8846222}}
+== Structural highlights ==
-==Disease==
+Three-dimensional structure of human lysosomal aspartylglucosaminidase.,Oinonen C, Tikkanen R, Rouvinen J, Peltonen L Nat Struct Biol. 1995 Dec;2(12):1102-8. PMID:8846222<ref>PMID:8846222</ref>
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[1apy]] is a 4 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=1APY OCA].
+</div>
-==Reference==
+==See Also==
-<ref group="xtra">PMID:008846222</ref><references group="xtra"/><references/>
+*[[Glycosylasparaginase|Glycosylasparaginase]]
 [[Category: Homo sapiens]]
 [[Category: Oinonen, C.]]

OCA at 22:35, 24 March 2013

2013-03-24T22:35:42Z

← Older revision		Revision as of 22:35, 24 March 2013
Line 1:		Line 1:
	~~[[Image:1apy.png\|left\|200px]]~~

	{{STRUCTURE_1apy\| PDB=1apy \| SCENE= }}		{{STRUCTURE_1apy\| PDB=1apy \| SCENE= }}
			===HUMAN ASPARTYLGLUCOSAMINIDASE===
			{{ABSTRACT_PUBMED_8846222}}

	==~~=HUMAN ASPARTYLGLUCOSAMINIDASE=~~==		==Disease==
			[[http://www.uniprot.org/uniprot/ASPG_HUMAN ASPG_HUMAN]] Defects in AGA are the cause of aspartylglucosaminuria (AGU) [MIM:[http://omim.org/entry/208400 208400]]. AGU is an inborn lysosomal storage disease. Clinical features of AGU include mild to severe mental retardation manifesting from the age of 2, coarse facial features and mild connective tissue abnormalities. This recessively inherited disease is overrepresented in the Finnish population.<ref>PMID:1703489</ref><ref>PMID:1904874</ref><ref>PMID:2011603</ref><ref>PMID:8776587</ref><ref>PMID:9137882</ref><ref>PMID:11309371</ref>

	~~{{ABSTRACT_PUBMED_8846222}}~~		==Function==
			[[http://www.uniprot.org/uniprot/ASPG_HUMAN ASPG_HUMAN]] Cleaves the GlcNAc-Asn bond which joins oligosaccharides to the peptide of asparagine-linked glycoproteins.

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

	==Reference==		==Reference==
	<ref group="xtra">PMID:008846222</ref><references group="xtra"/>		<ref group="xtra">PMID:008846222</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Oinonen, C.]]		[[Category: Oinonen, C.]]

← Older revision		Revision as of 09:47, 26 May 2021
Line 3:		Line 3:
	<StructureSection load='1apy' size='340' side='right'caption='[[1apy]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='1apy' size='340' side='right'caption='[[1apy]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1apy]] is a 4 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=1APY OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1APY FirstGlance]. <br>		<table><tr><td colspan='2'>[[1apy]] 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=1APY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1APY FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.26 3.5.1.26] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.26 3.5.1.26] </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=1apy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1apy OCA], [~~http~~://pdbe.org/1apy PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1apy RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1apy PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1apy 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=1apy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1apy OCA], [https://pdbe.org/1apy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1apy RCSB], [https://www.ebi.ac.uk/pdbsum/1apy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1apy ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
	[[~~http~~://www.uniprot.org/uniprot/ASPG_HUMAN ASPG_HUMAN]] Defects in AGA are the cause of aspartylglucosaminuria (AGU) [MIM:[~~http~~://omim.org/entry/208400 208400]]. AGU is an inborn lysosomal storage disease. Clinical features of AGU include mild to severe mental retardation manifesting from the age of 2, coarse facial features and mild connective tissue abnormalities. This recessively inherited disease is overrepresented in the Finnish population.<ref>PMID:1703489</ref> <ref>PMID:1904874</ref> <ref>PMID:2011603</ref> <ref>PMID:8776587</ref> <ref>PMID:9137882</ref> <ref>PMID:11309371</ref>		[[https://www.uniprot.org/uniprot/ASPG_HUMAN ASPG_HUMAN]] Defects in AGA are the cause of aspartylglucosaminuria (AGU) [MIM:[https://omim.org/entry/208400 208400]]. AGU is an inborn lysosomal storage disease. Clinical features of AGU include mild to severe mental retardation manifesting from the age of 2, coarse facial features and mild connective tissue abnormalities. This recessively inherited disease is overrepresented in the Finnish population.<ref>PMID:1703489</ref> <ref>PMID:1904874</ref> <ref>PMID:2011603</ref> <ref>PMID:8776587</ref> <ref>PMID:9137882</ref> <ref>PMID:11309371</ref>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/ASPG_HUMAN ASPG_HUMAN]] Cleaves the GlcNAc-Asn bond which joins oligosaccharides to the peptide of asparagine-linked glycoproteins.		[[https://www.uniprot.org/uniprot/ASPG_HUMAN ASPG_HUMAN]] Cleaves the GlcNAc-Asn bond which joins oligosaccharides to the peptide of asparagine-linked glycoproteins.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]