1apy: Difference between revisions
New page: left|200px<br /> <applet load="1apy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1apy, resolution 2.0Å" /> '''HUMAN ASPARTYLGLUCOS... |
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==About this Structure== | ==About this Structure== | ||
1APY 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 NAG as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.26 3.5.1.26]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1APY OCA]]. | 1APY 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 NAG as [[http://en.wikipedia.org/wiki/ligand ligand]]. 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]]. Structure known Active Sites: B1 and D1. Full crystallographic information is available from [[http://ispc.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://ispc.weizmann.ac.il//pmbin/getpm?pmid=8846222 8846222] | 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] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase]] | |||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Oinonen, C.]] | [[Category: Oinonen, C.]] | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
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Revision as of 14:58, 30 October 2007
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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 ... [(full description)]
About this StructureAbout this Structure
1APY is a [Single protein] structure of sequence from [Homo sapiens] with NAG as [ligand]. Active as [N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase], with EC number [3.5.1.26]. Structure known Active Sites: B1 and D1. 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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