1apz
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1apz.gif|left|200px]] | + | [[Image:1apz.gif|left|200px]] |
| - | + | ||
| - | '''HUMAN ASPARTYLGLUCOSAMINIDASE COMPLEX WITH REACTION PRODUCT''' | + | {{Structure |
| + | |PDB= 1apz |SIZE=350|CAPTION= <scene name='initialview01'>1apz</scene>, resolution 2.3Å | ||
| + | |SITE= <scene name='pdbsite=B:A+Catalytic+Residue'>B</scene> and <scene name='pdbsite=D:A+Catalytic+Residue'>D</scene> | ||
| + | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> and <scene name='pdbligand=ASP:ASPARTIC ACID'>ASP</scene> | ||
| + | |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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''HUMAN ASPARTYLGLUCOSAMINIDASE COMPLEX WITH REACTION PRODUCT''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 10: | Line 19: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1APZ is a [ | + | 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== | ||
| - | 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:// | + | 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]] | ||
| Line 25: | Line 34: | ||
[[Category: glycosylasparaginase]] | [[Category: glycosylasparaginase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''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
| |||||||
| , 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
