Summary for 2TAA
| Entry DOI | 10.2210/pdb2taa/pdb |
| Descriptor | TAKA-AMYLASE A, CALCIUM ION (2 entities in total) |
| Functional Keywords | hydrolase (o-glycosyl) |
| Biological source | Aspergillus oryzae |
| Total number of polymer chains | 3 |
| Total formula weight | 157430.73 |
| Authors | Kusunoki, M.,Matsuura, Y.,Tanaka, N.,Kakudo, M. (deposition date: 1982-10-18, release date: 1982-10-21, Last modification date: 2024-11-13) |
| Primary citation | Matsuura, Y.,Kusunoki, M.,Harada, W.,Kakudo, M. Structure and possible catalytic residues of Taka-amylase A J.Biochem.(Tokyo), 95:697-702, 1984 Cited by PubMed Abstract: 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. PubMed: 6609921PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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