2d2o
From Proteopedia
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{{STRUCTURE_2d2o| PDB=2d2o | SCENE= }} | {{STRUCTURE_2d2o| PDB=2d2o | SCENE= }} | ||
===Structure of a complex of Thermoactinomyces vulgaris R-47 alpha-amylase 2 with maltohexaose demonstrates the important role of aromatic residues at the reducing end of the substrate binding cleft=== | ===Structure of a complex of Thermoactinomyces vulgaris R-47 alpha-amylase 2 with maltohexaose demonstrates the important role of aromatic residues at the reducing end of the substrate binding cleft=== | ||
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{{ABSTRACT_PUBMED_16564038}} | {{ABSTRACT_PUBMED_16564038}} | ||
==About this Structure== | ==About this Structure== | ||
| - | + | [[2d2o]] is a 2 chain structure of [[Alpha-Amylase]] with sequence from [http://en.wikipedia.org/wiki/Thermoactinomyces_vulgaris Thermoactinomyces vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D2O OCA]. | |
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| + | ==See Also== | ||
| + | *[[Alpha-Amylase|Alpha-Amylase]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:016564038</ref><references group="xtra"/> |
[[Category: Neopullulanase]] | [[Category: Neopullulanase]] | ||
[[Category: Thermoactinomyces vulgaris]] | [[Category: Thermoactinomyces vulgaris]] | ||
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[[Category: Yoshida, H.]] | [[Category: Yoshida, H.]] | ||
[[Category: Beta/alpha barrel]] | [[Category: Beta/alpha barrel]] | ||
| - | + | [[Category: Hydrolase]] | |
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Revision as of 11:34, 27 July 2012
Contents |
Structure of a complex of Thermoactinomyces vulgaris R-47 alpha-amylase 2 with maltohexaose demonstrates the important role of aromatic residues at the reducing end of the substrate binding cleft
Template:ABSTRACT PUBMED 16564038
About this Structure
2d2o is a 2 chain structure of Alpha-Amylase with sequence from Thermoactinomyces vulgaris. Full crystallographic information is available from OCA.
See Also
Reference
- Ohtaki A, Mizuno M, Yoshida H, Tonozuka T, Sakano Y, Kamitori S. Structure of a complex of Thermoactinomyces vulgaris R-47 alpha-amylase 2 with maltohexaose demonstrates the important role of aromatic residues at the reducing end of the substrate binding cleft. Carbohydr Res. 2006 Jun 12;341(8):1041-6. Epub 2006 Mar 27. PMID:16564038 doi:10.1016/j.carres.2006.01.029
