1o7d - Revision history

OCA at 07:22, 9 October 2024

2024-10-09T07:22:42Z

← Older revision		Revision as of 07:22, 9 October 2024
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	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o7/1o7d_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o7/1o7d_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>

OCA at 12:29, 13 December 2023

2023-12-13T12:29:21Z

← Older revision		Revision as of 12:29, 13 December 2023
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1o7d]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O7D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O7D FirstGlance]. <br>		<table><tr><td colspan='2'>[[1o7d]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O7D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O7D 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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene~~>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>~~		</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.7Å</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Alpha-mannosidase Alpha-mannosidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.24 3.2.1.24] </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=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1o7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o7d OCA], [https://pdbe.org/1o7d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o7d RCSB], [https://www.ebi.ac.uk/pdbsum/1o7d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o7d 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=1o7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o7d OCA], [https://pdbe.org/1o7d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o7d RCSB], [https://www.ebi.ac.uk/pdbsum/1o7d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o7d ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
	[[https://www.uniprot.org/uniprot/MA2B1_BOVIN MA2B1_BOVIN]] Note=Defects in MAN2B1 are the cause of lysosomal alpha-mannosidosis (AM). AM is a lysosomal storage disease characterized by accumulation of unbranched oligosaccharide chains. The disease manifests itself by head tremor, aggressive tendency, ataxia, failure to thrive, and early death.		[https://www.uniprot.org/uniprot/MA2B1_BOVIN MA2B1_BOVIN] Note=Defects in MAN2B1 are the cause of lysosomal alpha-mannosidosis (AM). AM is a lysosomal storage disease characterized by accumulation of unbranched oligosaccharide chains. The disease manifests itself by head tremor, aggressive tendency, ataxia, failure to thrive, and early death.
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/MA2B1_BOVIN MA2B1_BOVIN]] Necessary for the catabolism of N-linked carbohydrates released during glycoprotein turnover.		[https://www.uniprot.org/uniprot/MA2B1_BOVIN MA2B1_BOVIN] Necessary for the catabolism of N-linked carbohydrates released during glycoprotein turnover.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 38:		Line 38:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	~~[[Category: Alpha-mannosidase]]~~
	[[Category: Bos taurus]]		[[Category: Bos taurus]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Evjen, G]]		[[Category: Evjen G]]
	[[Category: Heikinheimo, P]]		[[Category: Heikinheimo P]]
	[[Category: Helland, R]]		[[Category: Helland R]]
	[[Category: Hough, E]]		[[Category: Hough E]]
	[[Category: Karlsen, S]]		[[Category: Karlsen S]]
	[[Category: Leiros~~, H S~~]]		[[Category: Leiros HS]]
	[[Category: Leiros, I]]		[[Category: Leiros I]]
	[[Category: Mcsweeney, S]]		[[Category: Mcsweeney S]]
	[[Category: Ravelli, R]]		[[Category: Ravelli R]]
	[[Category: Ruigrok, R]]		[[Category: Ruigrok R]]
	[[Category: Schoehn, G]]		[[Category: Schoehn G]]
	[[Category: Tollersrud, O K]]		[[Category: Tollersrud O-K]]
	~~[[Category: A-mannosidase]]~~
	~~[[Category: Glycosyl hydrolase family 38]]~~
	~~[[Category: Hydrolase]]~~
	~~[[Category: Lysosomal~~]]

OCA at 07:52, 19 January 2022

2022-01-19T07:52:03Z

OCA at 07:31, 15 April 2020

2020-04-15T07:31:20Z

← Older revision		Revision as of 07:31, 15 April 2020
Line 1:		Line 1:

	==The structure of the bovine lysosomal a-mannosidase suggests a novel mechanism for low pH activation==		==The structure of the bovine lysosomal a-mannosidase suggests a novel mechanism for low pH activation==
	<StructureSection load='1o7d' size='340' side='right' caption='[[1o7d]], [[Resolution\|resolution]] 2.70Å' scene=''>		<StructureSection load='1o7d' size='340' side='right'caption='[[1o7d]], [[Resolution\|resolution]] 2.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1o7d]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O7D OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1O7D FirstGlance]. <br>		<table><tr><td colspan='2'>[[1o7d]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O7D OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1O7D 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=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-mannosidase Alpha-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.24 3.2.1.24] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-mannosidase Alpha-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.24 3.2.1.24] </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=1o7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o7d OCA], [http://pdbe.org/1o7d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1o7d RCSB], [http://www.ebi.ac.uk/pdbsum/1o7d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1o7d 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=1o7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o7d OCA], [http://pdbe.org/1o7d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1o7d RCSB], [http://www.ebi.ac.uk/pdbsum/1o7d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1o7d ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 33:		Line 33:

	==See Also==		==See Also==
	*[[Mannosidase\|Mannosidase]]		*[[Mannosidase 3D structures\|Mannosidase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 40:		Line 40:
	[[Category: Alpha-mannosidase]]		[[Category: Alpha-mannosidase]]
	[[Category: Bos taurus]]		[[Category: Bos taurus]]
			[[Category: Large Structures]]
	[[Category: Evjen, G]]		[[Category: Evjen, G]]
	[[Category: Heikinheimo, P]]		[[Category: Heikinheimo, P]]

OCA at 05:59, 11 July 2018

2018-07-11T05:59:15Z

← Older revision		Revision as of 05:59, 11 July 2018
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1o7d]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O7D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1O7D FirstGlance]. <br>		<table><tr><td colspan='2'>[[1o7d]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O7D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1O7D 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=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG~~</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG~~</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-mannosidase Alpha-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.24 3.2.1.24] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-mannosidase Alpha-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.24 3.2.1.24] </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=1o7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o7d OCA], [http://pdbe.org/1o7d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1o7d RCSB], [http://www.ebi.ac.uk/pdbsum/1o7d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1o7d 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=1o7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o7d OCA], [http://pdbe.org/1o7d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1o7d RCSB], [http://www.ebi.ac.uk/pdbsum/1o7d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1o7d ProSAT]</span></td></tr>
Line 16:		Line 16:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o7/1o7d_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o7/1o7d_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 1o7d" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1o7d" style="background-color:#fffaf0;"></div>

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

OCA at 10:03, 1 November 2017

2017-11-01T10:03:03Z

← Older revision		Revision as of 10:03, 1 November 2017
Line 1:		Line 1:
	==~~THE STRUCTURE OF THE BOVINE LYSOSOMAL A~~-~~MANNOSIDASE SUGGESTS A NOVEL MECHANISM FOR LOW PH ACTIVATION~~==
			==The structure of the bovine lysosomal a-mannosidase suggests a novel mechanism for low pH activation==
	<StructureSection load='1o7d' size='340' side='right' caption='[[1o7d]], [[Resolution\|resolution]] 2.70Å' scene=''>		<StructureSection load='1o7d' size='340' side='right' caption='[[1o7d]], [[Resolution\|resolution]] 2.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1o7d]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O7D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1O7D FirstGlance]. <br>		<table><tr><td colspan='2'>[[1o7d]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O7D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1O7D 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>, <scene name='pdbligand=~~SO4~~:~~SULFATE+ION~~'>~~SO4~~</scene>, <scene name='pdbligand=~~TRS~~:2-~~AMINO~~-2-~~HYDROXYMETHYL~~-~~PROPANE~~-~~1,3~~-~~DIOL~~'>~~TRS~~</scene>, <scene name='pdbligand=ZN:~~ZINC~~+ION'>ZN</scene>, <scene name='pdbligand=~~MAN~~:~~ALPHA~~-D-~~MANNOSE~~'>~~MAN~~</scene>, <scene name='pdbligand=~~NDG~~:~~2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE~~'>~~NDG~~</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=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-mannosidase Alpha-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.24 3.2.1.24] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-mannosidase Alpha-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.24 3.2.1.24] </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=1o7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o7d OCA], [http://pdbe.org/1o7d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1o7d RCSB], [http://www.ebi.ac.uk/pdbsum/1o7d 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=1o7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o7d OCA], [http://pdbe.org/1o7d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1o7d RCSB], [http://www.ebi.ac.uk/pdbsum/1o7d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1o7d ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 19:		Line 20:
	<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=1o7d ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 30:		Line 31:
	</div>		</div>
	<div class="pdbe-citations 1o7d" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1o7d" style="background-color:#fffaf0;"></div>

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

OCA at 01:54, 12 September 2015

2015-09-12T01:54:19Z

← Older revision		Revision as of 01:54, 12 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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-mannosidase Alpha-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.24 3.2.1.24] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-mannosidase Alpha-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.24 3.2.1.24] </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=1o7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o7d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1o7d RCSB], [http://www.ebi.ac.uk/pdbsum/1o7d 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=1o7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o7d OCA], [http://pdbe.org/1o7d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1o7d RCSB], [http://www.ebi.ac.uk/pdbsum/1o7d 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 1o7d" style="background-color:#fffaf0;"></div>

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

OCA at 16:11, 5 January 2015

2015-01-05T16:11:05Z

← Older revision		Revision as of 16:11, 5 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1o7d]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O7D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1O7D FirstGlance]. <br>		<table><tr><td colspan='2'>[[1o7d]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O7D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1O7D 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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene></td></tr>
	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-mannosidase Alpha-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.24 3.2.1.24] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-mannosidase Alpha-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.24 3.2.1.24] </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=1o7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o7d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1o7d RCSB], [http://www.ebi.ac.uk/pdbsum/1o7d 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=1o7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o7d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1o7d RCSB], [http://www.ebi.ac.uk/pdbsum/1o7d PDBsum]</span></td></tr>
	<table>		</table>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/MA2B1_BOVIN MA2B1_BOVIN]] Note=Defects in MAN2B1 are the cause of lysosomal alpha-mannosidosis (AM). AM is a lysosomal storage disease characterized by accumulation of unbranched oligosaccharide chains. The disease manifests itself by head tremor, aggressive tendency, ataxia, failure to thrive, and early death.		[[http://www.uniprot.org/uniprot/MA2B1_BOVIN MA2B1_BOVIN]] Note=Defects in MAN2B1 are the cause of lysosomal alpha-mannosidosis (AM). AM is a lysosomal storage disease characterized by accumulation of unbranched oligosaccharide chains. The disease manifests itself by head tremor, aggressive tendency, ataxia, failure to thrive, and early death.
Line 38:		Line 38:
	[[Category: Alpha-mannosidase]]		[[Category: Alpha-mannosidase]]
	[[Category: Bos taurus]]		[[Category: Bos taurus]]
	[[Category: Evjen, G.]]		[[Category: Evjen, G]]
	[[Category: Heikinheimo, P.]]		[[Category: Heikinheimo, P]]
	[[Category: Helland, R.]]		[[Category: Helland, R]]
	[[Category: Hough, E.]]		[[Category: Hough, E]]
	[[Category: Karlsen, S.]]		[[Category: Karlsen, S]]
	[[Category: Leiros, H S.]]		[[Category: Leiros, H S]]
	[[Category: Leiros, I.]]		[[Category: Leiros, I]]
	[[Category: Mcsweeney, S.]]		[[Category: Mcsweeney, S]]
	[[Category: Ravelli, R.]]		[[Category: Ravelli, R]]
	[[Category: Ruigrok, R.]]		[[Category: Ruigrok, R]]
	[[Category: Schoehn, G.]]		[[Category: Schoehn, G]]
	[[Category: Tollersrud, O K.]]		[[Category: Tollersrud, O K]]
	[[Category: A-mannosidase]]		[[Category: A-mannosidase]]
	[[Category: Glycosyl hydrolase family 38]]		[[Category: Glycosyl hydrolase family 38]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Lysosomal]]		[[Category: Lysosomal]]

OCA at 17:11, 29 September 2014

2014-09-29T17:11:09Z

← Older revision		Revision as of 17:11, 29 September 2014
Line 1:		Line 1:
	~~{{STRUCTURE_1o7d\| PDB=1o7d \| SCENE= }}~~		==THE STRUCTURE OF THE BOVINE LYSOSOMAL A-MANNOSIDASE SUGGESTS A NOVEL MECHANISM FOR LOW PH ACTIVATION==
	===THE STRUCTURE OF THE BOVINE LYSOSOMAL A-MANNOSIDASE SUGGESTS A NOVEL MECHANISM FOR LOW PH ACTIVATION===		<StructureSection load='1o7d' size='340' side='right' caption='[[1o7d]], [[Resolution\|resolution]] 2.70Å' scene=''>
	~~{{ABSTRACT_PUBMED_12634058}}~~		== Structural highlights ==
			<table><tr><td colspan='2'>[[1o7d]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O7D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1O7D FirstGlance]. <br>
	==Disease==		</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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene><br>
			<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-mannosidase Alpha-mannosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.24 3.2.1.24] </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=1o7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o7d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1o7d RCSB], [http://www.ebi.ac.uk/pdbsum/1o7d PDBsum]</span></td></tr>
			<table>
			== Disease ==
	[[http://www.uniprot.org/uniprot/MA2B1_BOVIN MA2B1_BOVIN]] Note=Defects in MAN2B1 are the cause of lysosomal alpha-mannosidosis (AM). AM is a lysosomal storage disease characterized by accumulation of unbranched oligosaccharide chains. The disease manifests itself by head tremor, aggressive tendency, ataxia, failure to thrive, and early death.		[[http://www.uniprot.org/uniprot/MA2B1_BOVIN MA2B1_BOVIN]] Note=Defects in MAN2B1 are the cause of lysosomal alpha-mannosidosis (AM). AM is a lysosomal storage disease characterized by accumulation of unbranched oligosaccharide chains. The disease manifests itself by head tremor, aggressive tendency, ataxia, failure to thrive, and early death.
			== Function ==
			[[http://www.uniprot.org/uniprot/MA2B1_BOVIN MA2B1_BOVIN]] Necessary for the catabolism of N-linked carbohydrates released during glycoprotein turnover.
			== 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/o7/1o7d_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 ==
			Lysosomal alpha-mannosidase (LAM: EC 3.2.1.24) belongs to the sequence-based glycoside hydrolase family 38 (GH38). Two other mammalian GH38 members, Golgi alpha-mannosidase II (GIIAM) and cytosolic alpha-mannosidase, are expressed in all tissues. In humans, cattle, cat and guinea pig, lack of lysosomal alpha-mannosidase activity causes the autosomal recessive disease alpha-mannosidosis. Here, we describe the three-dimensional structure of bovine lysosomal alpha-mannosidase (bLAM) at 2.7A resolution and confirm the solution state dimer by electron microscopy. We present the first structure of a mammalian GH38 enzyme that offers indications for the signal areas for mannose phosphorylation, suggests a previously undetected mechanism of low-pH activation and provides a template for further biochemical studies of the family 38 glycoside hydrolases as well as lysosomal transport. Furthermore, it provides a basis for understanding the human form of alpha-mannosidosis at the atomic level. The atomic coordinates and structure factors have been deposited in the Protein Data Bank (accession codes 1o7d and r1o7dsf).

	~~==Function==~~		The structure of bovine lysosomal alpha-mannosidase suggests a novel mechanism for low-pH activation.,Heikinheimo P, Helland R, Leiros HK, Leiros I, Karlsen S, Evjen G, Ravelli R, Schoehn G, Ruigrok R, Tollersrud OK, McSweeney S, Hough E J Mol Biol. 2003 Mar 28;327(3):631-44. PMID:12634058<ref>PMID:12634058</ref>
	~~[[http://www~~.~~uniprot~~.~~org/uniprot/MA2B1_BOVIN MA2B1_BOVIN]] Necessary for the catabolism of N~~-~~linked carbohydrates released during glycoprotein turnover~~.

	~~==About this Structure==~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	~~[[1o7d]] is~~ a ~~5 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Bos_taurus Bos taurus]~~. ~~Full crystallographic information is available from [http:/~~/~~oca.weizmann.ac.il/oca-bin/ocashort?id=1O7D OCA].~~		</div>

	==See Also==		==See Also==
	*[[Mannosidase\|Mannosidase]]		*[[Mannosidase\|Mannosidase]]
			== References ==
	==~~Reference~~==		<references/>
	~~<ref group="xtra">PMID:012634058</ref>~~<references ~~group="xtra"~~/><~~references~~/>		__TOC__
			</StructureSection>
	[[Category: Alpha-mannosidase]]		[[Category: Alpha-mannosidase]]
	[[Category: Bos taurus]]		[[Category: Bos taurus]]

OCA at 06:15, 25 March 2013

2013-03-25T06:15:31Z

← Older revision		Revision as of 06:15, 25 March 2013
Line 1:		Line 1:
	~~[[Image:1o7d.png\|left\|200px]]~~

	{{STRUCTURE_1o7d\| PDB=1o7d \| SCENE= }}		{{STRUCTURE_1o7d\| PDB=1o7d \| SCENE= }}
			===THE STRUCTURE OF THE BOVINE LYSOSOMAL A-MANNOSIDASE SUGGESTS A NOVEL MECHANISM FOR LOW PH ACTIVATION===
			{{ABSTRACT_PUBMED_12634058}}

	==~~=THE STRUCTURE OF THE BOVINE LYSOSOMAL A-MANNOSIDASE SUGGESTS A NOVEL MECHANISM FOR LOW PH ACTIVATION~~===		==Disease==
			[[http://www.uniprot.org/uniprot/MA2B1_BOVIN MA2B1_BOVIN]] Note=Defects in MAN2B1 are the cause of lysosomal alpha-mannosidosis (AM). AM is a lysosomal storage disease characterized by accumulation of unbranched oligosaccharide chains. The disease manifests itself by head tremor, aggressive tendency, ataxia, failure to thrive, and early death.

	~~{{ABSTRACT_PUBMED_12634058}}~~		==Function==
			[[http://www.uniprot.org/uniprot/MA2B1_BOVIN MA2B1_BOVIN]] Necessary for the catabolism of N-linked carbohydrates released during glycoprotein turnover.

	==About this Structure==		==About this Structure==
Line 14:		Line 16:

	==Reference==		==Reference==
	<ref group="xtra">PMID:012634058</ref><references group="xtra"/>		<ref group="xtra">PMID:012634058</ref><references group="xtra"/><references/>
	[[Category: Alpha-mannosidase]]		[[Category: Alpha-mannosidase]]
	[[Category: Bos taurus]]		[[Category: Bos taurus]]

← Older revision		Revision as of 07:52, 19 January 2022
Line 3:		Line 3:
	<StructureSection load='1o7d' size='340' side='right'caption='[[1o7d]], [[Resolution\|resolution]] 2.70Å' scene=''>		<StructureSection load='1o7d' size='340' side='right'caption='[[1o7d]], [[Resolution\|resolution]] 2.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1o7d]] is a 5 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O7D OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=1O7D FirstGlance]. <br>		<table><tr><td colspan='2'>[[1o7d]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O7D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O7D 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=MAN:ALPHA-D-MANNOSE'>MAN~~</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Alpha-mannosidase Alpha-mannosidase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.24 3.2.1.24] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Alpha-mannosidase Alpha-mannosidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.24 3.2.1.24] </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=1o7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o7d OCA], [~~http~~://pdbe.org/1o7d PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1o7d RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1o7d PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1o7d 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=1o7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o7d OCA], [https://pdbe.org/1o7d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o7d RCSB], [https://www.ebi.ac.uk/pdbsum/1o7d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o7d ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
	[[~~http~~://www.uniprot.org/uniprot/MA2B1_BOVIN MA2B1_BOVIN]] Note=Defects in MAN2B1 are the cause of lysosomal alpha-mannosidosis (AM). AM is a lysosomal storage disease characterized by accumulation of unbranched oligosaccharide chains. The disease manifests itself by head tremor, aggressive tendency, ataxia, failure to thrive, and early death.		[[https://www.uniprot.org/uniprot/MA2B1_BOVIN MA2B1_BOVIN]] Note=Defects in MAN2B1 are the cause of lysosomal alpha-mannosidosis (AM). AM is a lysosomal storage disease characterized by accumulation of unbranched oligosaccharide chains. The disease manifests itself by head tremor, aggressive tendency, ataxia, failure to thrive, and early death.
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/MA2B1_BOVIN MA2B1_BOVIN]] Necessary for the catabolism of N-linked carbohydrates released during glycoprotein turnover.		[[https://www.uniprot.org/uniprot/MA2B1_BOVIN MA2B1_BOVIN]] Necessary for the catabolism of N-linked carbohydrates released during glycoprotein turnover.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]