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1w9x

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[[Image:1w9x.gif|left|200px]]<br /><applet load="1w9x" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1w9x.gif|left|200px]]
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caption="1w9x, resolution 2.10&Aring;" />
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'''BACILLUS HALMAPALUS ALPHA AMYLASE'''<br />
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{{Structure
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|PDB= 1w9x |SIZE=350|CAPTION= <scene name='initialview01'>1w9x</scene>, resolution 2.10&Aring;
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|SITE= <scene name='pdbsite=AC1:Ac1+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=NA:SODIUM ION'>NA</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Alpha-amylase Alpha-amylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.1 3.2.1.1]
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|GENE=
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}}
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'''BACILLUS HALMAPALUS ALPHA AMYLASE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1W9X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_halmapalus Bacillus halmapalus] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=NA:'>NA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alpha-amylase Alpha-amylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.1 3.2.1.1] Known structural/functional Site: <scene name='pdbsite=AC1:Ac1+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W9X OCA].
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1W9X is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_halmapalus Bacillus halmapalus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W9X OCA].
==Reference==
==Reference==
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Structure of a Bacillus halmapalus family 13 alpha-amylase, BHA, in complex with an acarbose-derived nonasaccharide at 2.1 A resolution., Davies GJ, Brzozowski AM, Dauter Z, Rasmussen MD, Borchert TV, Wilson KS, Acta Crystallogr D Biol Crystallogr. 2005 Feb;61(Pt 2):190-3. Epub 2005, Jan 19. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15681870 15681870]
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Structure of a Bacillus halmapalus family 13 alpha-amylase, BHA, in complex with an acarbose-derived nonasaccharide at 2.1 A resolution., Davies GJ, Brzozowski AM, Dauter Z, Rasmussen MD, Borchert TV, Wilson KS, Acta Crystallogr D Biol Crystallogr. 2005 Feb;61(Pt 2):190-3. Epub 2005, Jan 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15681870 15681870]
[[Category: Alpha-amylase]]
[[Category: Alpha-amylase]]
[[Category: Bacillus halmapalus]]
[[Category: Bacillus halmapalus]]
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[[Category: glycoside hydrolase]]
[[Category: glycoside hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:42:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:54:11 2008''

Revision as of 12:54, 20 March 2008


PDB ID 1w9x

Drag the structure with the mouse to rotate
, resolution 2.10Å
Sites:
Ligands: and
Activity: Alpha-amylase, with EC number 3.2.1.1
Coordinates: save as pdb, mmCIF, xml



BACILLUS HALMAPALUS ALPHA AMYLASE


Overview

The enzymatic digestion of starch by alpha-amylases is one of the key biotechnological reactions of recent times. In the search for industrial biocatalysts, the family GH13 alpha-amylase BHA from Bacillus halmapalus has been cloned and expressed. The three-dimensional structure at 2.1 A resolution has been determined in complex with the (pseudo)tetrasaccharide inhibitor acarbose. Acarbose is found bound as a nonasaccharide transglycosylation product spanning the -6 to +3 subsites. Careful inspection of electron density suggests that the bound ligand could not have been formed through successive transglycosylations of acarbose and must also have featured maltose or maltooligosaccharides as an acceptor.

About this Structure

1W9X is a Single protein structure of sequence from Bacillus halmapalus. Full crystallographic information is available from OCA.

Reference

Structure of a Bacillus halmapalus family 13 alpha-amylase, BHA, in complex with an acarbose-derived nonasaccharide at 2.1 A resolution., Davies GJ, Brzozowski AM, Dauter Z, Rasmussen MD, Borchert TV, Wilson KS, Acta Crystallogr D Biol Crystallogr. 2005 Feb;61(Pt 2):190-3. Epub 2005, Jan 19. PMID:15681870

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