1p6w
From Proteopedia
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|PDB= 1p6w |SIZE=350|CAPTION= <scene name='initialview01'>1p6w</scene>, resolution 2.00Å | |PDB= 1p6w |SIZE=350|CAPTION= <scene name='initialview01'>1p6w</scene>, resolution 2.00Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GLC:GLUCOSE'>GLC</scene>, <scene name='pdbligand=GTM:O1-METHYL-4-DEOXY-4-THIO-BETA-D-GLUCOSE'>GTM</scene>, <scene name='pdbligand=SGC:4-DEOXY-4-THIO-BETA-D-GLUCOPYRANOSE'>SGC</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= AMY1.1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4513 Hordeum vulgare]) | |GENE= AMY1.1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4513 Hordeum vulgare]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1ht6|1HT6]], [[1amy|1AMY]], [[1bg9|1BG9]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1p6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p6w OCA], [http://www.ebi.ac.uk/pdbsum/1p6w PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1p6w RCSB]</span> | ||
}} | }} | ||
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[[Category: Haser, R.]] | [[Category: Haser, R.]] | ||
[[Category: Robert, X.]] | [[Category: Robert, X.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: GLC]] | ||
| - | [[Category: GTM]] | ||
| - | [[Category: SGC]] | ||
[[Category: alpha-amylase]] | [[Category: alpha-amylase]] | ||
[[Category: barley]] | [[Category: barley]] | ||
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[[Category: x-ray diffraction]] | [[Category: x-ray diffraction]] | ||
| - | ''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 22:55:42 2008'' |
Revision as of 19:55, 30 March 2008
| |||||||
| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Gene: | AMY1.1 (Hordeum vulgare) | ||||||
| Activity: | Alpha-amylase, with EC number 3.2.1.1 | ||||||
| Related: | 1HT6, 1AMY, 1BG9
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of barley alpha-amylase isozyme 1 (AMY1) in complex with the substrate analogue, methyl 4I,4II,4III-tri-thiomaltotetraoside (thio-DP4)
Overview
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 Structure
1P6W is a Single protein structure of sequence from Hordeum vulgare. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Sun Mar 30 22:55:42 2008
