1apy: Difference between revisions
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[[Image:1apy.gif|left|200px]] | [[Image:1apy.gif|left|200px]] | ||
'''HUMAN ASPARTYLGLUCOSAMINIDASE''' | {{Structure | ||
|PDB= 1apy |SIZE=350|CAPTION= <scene name='initialview01'>1apy</scene>, resolution 2.0Å | |||
|SITE= <scene name='pdbsite=B1:A+Catalytic+Residue'>B1</scene> and <scene name='pdbsite=D1:A+Catalytic+Residue'>D1</scene> | |||
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1APY is a [ | 1APY 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=1APY 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]] | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
''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 10:00:46 2008'' | ||
Revision as of 11:00, 20 March 2008
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| , resolution 2.0Å | |||||||
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| Sites: | and | ||||||
| Ligands: | |||||||
| Activity: | N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase, with EC number 3.5.1.26 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HUMAN ASPARTYLGLUCOSAMINIDASE
OverviewOverview
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.
DiseaseDisease
Known disease associated with this structure: Aspartylglucosaminuria OMIM:[208400]
About this StructureAbout this Structure
1APY is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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
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