1ht6: Difference between revisions
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|PDB= 1ht6 |SIZE=350|CAPTION= <scene name='initialview01'>1ht6</scene>, resolution 1.50Å | |PDB= 1ht6 |SIZE=350|CAPTION= <scene name='initialview01'>1ht6</scene>, resolution 1.50Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene> | ||
|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] | |ACTIVITY= <span class='plainlinks'>[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] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1amy|1AMY]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ht6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ht6 OCA], [http://www.ebi.ac.uk/pdbsum/1ht6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ht6 RCSB]</span> | |||
}} | }} | ||
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[[Category: Haser, R.]] | [[Category: Haser, R.]] | ||
[[Category: Robert, X.]] | [[Category: Robert, X.]] | ||
[[Category: alpha-amylase]] | [[Category: alpha-amylase]] | ||
[[Category: barley]] | [[Category: barley]] | ||
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[[Category: isozyme 1]] | [[Category: isozyme 1]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:10:04 2008'' | ||
Revision as of 21:10, 30 March 2008
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| , resolution 1.50Å | |||||||
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| Ligands: | , | ||||||
| Activity: | Alpha-amylase, with EC number 3.2.1.1 | ||||||
| Related: | 1AMY
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE AT 1.5A RESOLUTION OF THE BARLEY ALPHA-AMYLASE ISOZYME 1
OverviewOverview
Though the three-dimensional structures of barley alpha-amylase isozymes AMY1 and AMY2 are very similar, they differ remarkably from each other in their affinity for Ca(2+) and when interacting with substrate analogs. A surface site recognizing maltooligosaccharides, not earlier reported for other alpha-amylases and probably associated with the different activity of AMY1 and AMY2 toward starch granules, has been identified. It is located in the C-terminal part of the enzyme and, thus, highlights a potential role of domain C. In order to scrutinize the possible biological significance of this domain in alpha-amylases, a thorough comparison of their three-dimensional structures was conducted. An additional role for an earlier-identified starch granule binding surface site is proposed, and a new calcium ion is reported.
About this StructureAbout this Structure
1HT6 is a Single protein structure of sequence from Hordeum vulgare. Full crystallographic information is available from OCA.
ReferenceReference
The structure of barley alpha-amylase isozyme 1 reveals a novel role of domain C in substrate recognition and binding: a pair of sugar tongs., Robert X, Haser R, Gottschalk TE, Ratajczak F, Driguez H, Svensson B, Aghajari N, Structure. 2003 Aug;11(8):973-84. PMID:12906828
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