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1apz

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[[Image:1apz.gif|left|200px]]<br /><applet load="1apz" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1apz.gif|left|200px]]
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caption="1apz, resolution 2.3&Aring;" />
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'''HUMAN ASPARTYLGLUCOSAMINIDASE COMPLEX WITH REACTION PRODUCT'''<br />
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{{Structure
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|PDB= 1apz |SIZE=350|CAPTION= <scene name='initialview01'>1apz</scene>, resolution 2.3&Aring;
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|SITE= <scene name='pdbsite=B:A+Catalytic+Residue'>B</scene> and <scene name='pdbsite=D:A+Catalytic+Residue'>D</scene>
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> and <scene name='pdbligand=ASP:ASPARTIC ACID'>ASP</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''HUMAN ASPARTYLGLUCOSAMINIDASE COMPLEX WITH REACTION PRODUCT'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1APZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=ASP:'>ASP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Known structural/functional Sites: <scene name='pdbsite=B:A+Catalytic+Residue'>B</scene> and <scene name='pdbsite=D:A+Catalytic+Residue'>D</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1APZ OCA].
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1APZ is a [[Single protein]] structure of 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=1APZ OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8846222 8846222]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/8846222 8846222]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase]]
[[Category: N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase]]
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[[Category: glycosylasparaginase]]
[[Category: glycosylasparaginase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:47:06 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:00:49 2008''

Revision as of 08:00, 20 March 2008

Image:1apz.gif


PDB ID 1apz

Drag the structure with the mouse to rotate
, resolution 2.3Å
Sites: and
Ligands: and
Activity: N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase, with EC number 3.5.1.26
Coordinates: save as pdb, mmCIF, xml



HUMAN ASPARTYLGLUCOSAMINIDASE COMPLEX WITH REACTION PRODUCT


Contents

Overview

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.

Disease

Known disease associated with this structure: Aspartylglucosaminuria OMIM:[208400]

About this Structure

1APZ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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

Page seeded by OCA on Thu Mar 20 10:00:49 2008

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