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3bax
From Proteopedia
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[[Image:3bax.png|left|200px]] | [[Image:3bax.png|left|200px]] | ||
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{{STRUCTURE_3bax| PDB=3bax | SCENE= }} | {{STRUCTURE_3bax| PDB=3bax | SCENE= }} | ||
===N298S Variant of Human Pancreatic Alpha-Amylase in Complex with Azide=== | ===N298S Variant of Human Pancreatic Alpha-Amylase in Complex with Azide=== | ||
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{{ABSTRACT_PUBMED_18284212}} | {{ABSTRACT_PUBMED_18284212}} | ||
==About this Structure== | ==About this Structure== | ||
| - | + | [[3bax]] is a 1 chain structure of [[Alpha-Amylase]] 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=3BAX OCA]. | |
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| + | ==See Also== | ||
| + | *[[Alpha-Amylase|Alpha-Amylase]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:018284212</ref><references group="xtra"/> |
[[Category: Alpha-amylase]] | [[Category: Alpha-amylase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
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[[Category: Anion activation]] | [[Category: Anion activation]] | ||
[[Category: Azide]] | [[Category: Azide]] | ||
| - | [[Category: Calcium]] | ||
[[Category: Carbohydrate metabolism]] | [[Category: Carbohydrate metabolism]] | ||
[[Category: Catalysis]] | [[Category: Catalysis]] | ||
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[[Category: Human]] | [[Category: Human]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
| - | [[Category: Mechanism]] | ||
[[Category: Metal-binding]] | [[Category: Metal-binding]] | ||
[[Category: Pancreatic]] | [[Category: Pancreatic]] | ||
[[Category: Pyrrolidone carboxylic acid]] | [[Category: Pyrrolidone carboxylic acid]] | ||
[[Category: Secreted]] | [[Category: Secreted]] | ||
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 05:50:08 2009'' | ||
Revision as of 12:14, 27 July 2012
Contents |
N298S Variant of Human Pancreatic Alpha-Amylase in Complex with Azide
Template:ABSTRACT PUBMED 18284212
About this Structure
3bax is a 1 chain structure of Alpha-Amylase with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See Also
Reference
- Maurus R, Begum A, Williams LK, Fredriksen JR, Zhang R, Withers SG, Brayer GD. Alternative catalytic anions differentially modulate human alpha-amylase activity and specificity(,). Biochemistry. 2008 Mar 18;47(11):3332-44. Epub 2008 Feb 20. PMID:18284212 doi:10.1021/bi701652t
Categories: Alpha-amylase | Homo sapiens | Brayer, G D. | Maurus, R. | Amylase | Anion activation | Azide | Carbohydrate metabolism | Catalysis | Chloride | Diabetes | Enzyme | Glycoprotein | Glycosidase | Human | Hydrolase | Metal-binding | Pancreatic | Pyrrolidone carboxylic acid | Secreted
