3lx9
From Proteopedia
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[[Image:3lx9.png|left|200px]] | [[Image:3lx9.png|left|200px]] | ||
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{{STRUCTURE_3lx9| PDB=3lx9 | SCENE= }} | {{STRUCTURE_3lx9| PDB=3lx9 | SCENE= }} | ||
===Interconversion of Human Lysosomal Enzyme Specificities=== | ===Interconversion of Human Lysosomal Enzyme Specificities=== | ||
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{{ABSTRACT_PUBMED_20444686}} | {{ABSTRACT_PUBMED_20444686}} | ||
==About this Structure== | ==About this Structure== | ||
| - | [[3lx9]] is a 2 chain structure with 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=3LX9 OCA]. | + | [[3lx9]] is a 2 chain structure of [[Galactosidase]] with 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=3LX9 OCA]. |
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| + | ==See Also== | ||
| + | *[[Galactosidase|Galactosidase]] | ||
==Reference== | ==Reference== | ||
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[[Category: Metcalf, M C.]] | [[Category: Metcalf, M C.]] | ||
[[Category: Tomasic, I B.]] | [[Category: Tomasic, I B.]] | ||
| + | [[Category: Carbohydrate-binding protein]] | ||
| + | [[Category: Disease mutation]] | ||
| + | [[Category: Disulfide bond]] | ||
| + | [[Category: Enzyme interconversion]] | ||
| + | [[Category: Glycoprotein]] | ||
| + | [[Category: Glycosidase]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Lysosomal enzyme]] | ||
| + | [[Category: Lysosome]] | ||
Revision as of 04:27, 26 July 2012
Contents |
Interconversion of Human Lysosomal Enzyme Specificities
Template:ABSTRACT PUBMED 20444686
About this Structure
3lx9 is a 2 chain structure of Galactosidase with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See Also
Reference
- Tomasic IB, Metcalf MC, Guce AI, Clark NE, Garman SC. Interconversion of the specificities of human lysosomal enzymes associated with Fabry and Schindler diseases. J Biol Chem. 2010 Jul 9;285(28):21560-6. Epub 2010 May 5. PMID:20444686 doi:10.1074/jbc.M110.118588
