2taa | pdb_00002taa

STRUCTURE AND POSSIBLE CATALYTIC RESIDUES OF TAKA-AMYLASE A

spinqualitylabelsall models 2taa, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2taa is a 3 chain structure with sequence from Aspergillus oryzae. This structure supersedes the now removed PDB entry 1taa. The February 2006 RCSB PDB Molecule of the Month feature on Alpha-amylase by David S. Goodsell is 10.2210/rcsb_pdb/mom_2006_2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3Å Ligands: CA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function AMYA1_ASPOR Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Amylase 3D structures

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