2taa
From Proteopedia
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|PDB= 2taa |SIZE=350|CAPTION= <scene name='initialview01'>2taa</scene>, resolution 3.0Å | |PDB= 2taa |SIZE=350|CAPTION= <scene name='initialview01'>2taa</scene>, resolution 3.0Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</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= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2taa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2taa OCA], [http://www.ebi.ac.uk/pdbsum/2taa PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2taa RCSB]</span> | ||
}} | }} | ||
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[[Category: Matsuura, Y.]] | [[Category: Matsuura, Y.]] | ||
[[Category: Tanaka, N.]] | [[Category: Tanaka, N.]] | ||
| - | [[Category: CA]] | ||
[[Category: hydrolase (o-glycosyl)]] | [[Category: hydrolase (o-glycosyl)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:03:33 2008'' |
Revision as of 02:03, 31 March 2008
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| , resolution 3.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Alpha-amylase, with EC number 3.2.1.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE AND POSSIBLE CATALYTIC RESIDUES OF TAKA-AMYLASE A
Overview
A complete molecular model of Taka-amylase A consisting of 478 amino acid residues was built with the aid of amino acid sequence data. Some typical structural features of the molecule are described. A model fitting of an amylose chain in the catalytic site of the enzyme showed a possible productive binding mode between substrate and enzyme. On the basis of the difference Fourier analysis and the model fitting study, glutamic acid (Glu230) and aspartic acid (Asp297), which are located at the bottom of the cleft, were concluded to be the catalytic residues, serving as the general acid and base, respectively.
About this Structure
2TAA is a Single protein structure of sequence from Aspergillus oryzae. This structure supersedes the now removed PDB entry 1TAA. The following page contains interesting information on the relation of 2TAA with [Alpha-amylase]. Full crystallographic information is available from OCA.
Reference
Structure and possible catalytic residues of Taka-amylase A., Matsuura Y, Kusunoki M, Harada W, Kakudo M, J Biochem. 1984 Mar;95(3):697-702. PMID:6609921
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