1c7s: Difference between revisions
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[[Image:1c7s.png|left|200px]] | [[Image:1c7s.png|left|200px]] | ||
{{STRUCTURE_1c7s| PDB=1c7s | SCENE= }} | {{STRUCTURE_1c7s| PDB=1c7s | SCENE= }} | ||
===BETA-N-ACETYLHEXOSAMINIDASE MUTANT D539A COMPLEXED WITH DI-N-ACETYL-BETA-D-GLUCOSAMINE (CHITOBIASE)=== | ===BETA-N-ACETYLHEXOSAMINIDASE MUTANT D539A COMPLEXED WITH DI-N-ACETYL-BETA-D-GLUCOSAMINE (CHITOBIASE)=== | ||
{{ABSTRACT_PUBMED_10884356}} | {{ABSTRACT_PUBMED_10884356}} | ||
==About this Structure== | ==About this Structure== | ||
[[1c7s]] is a 1 chain structure of [[Beta-Hexosaminidase]] with sequence from [http://en.wikipedia.org/wiki/Serratia_marcescens Serratia marcescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C7S OCA]. | |||
==See Also== | |||
*[[Beta-Hexosaminidase|Beta-Hexosaminidase]] | |||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID: | <ref group="xtra">PMID:010884356</ref><references group="xtra"/> | ||
[[Category: Beta-N-acetylhexosaminidase]] | [[Category: Beta-N-acetylhexosaminidase]] | ||
[[Category: Serratia marcescens]] | [[Category: Serratia marcescens]] | ||
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[[Category: Chitinolysis]] | [[Category: Chitinolysis]] | ||
[[Category: Glycosyl hydrolase]] | [[Category: Glycosyl hydrolase]] | ||
[[Category: Hydrolase]] | |||
[[Category: Site directed mutagenesis]] | [[Category: Site directed mutagenesis]] | ||
[[Category: Substrate nucleophile stabilizer mutation]] | [[Category: Substrate nucleophile stabilizer mutation]] | ||
Revision as of 07:55, 27 July 2012
BETA-N-ACETYLHEXOSAMINIDASE MUTANT D539A COMPLEXED WITH DI-N-ACETYL-BETA-D-GLUCOSAMINE (CHITOBIASE)
Template:ABSTRACT PUBMED 10884356
About this Structure
1c7s is a 1 chain structure of Beta-Hexosaminidase with sequence from Serratia marcescens. Full crystallographic information is available from OCA.
See Also
Reference
- Prag G, Papanikolau Y, Tavlas G, Vorgias CE, Petratos K, Oppenheim AB. Structures of chitobiase mutants complexed with the substrate Di-N-acetyl-d-glucosamine: the catalytic role of the conserved acidic pair, aspartate 539 and glutamate 540. J Mol Biol. 2000 Jul 14;300(3):611-7. PMID:10884356 doi:10.1006/jmbi.2000.3906