Low resolution crystal structures of Taka-amylase A and its complexes with inhibitors.
The molecular structure of Taka-amylase A, an alpha-amylase from Aspergillus oryzae, has been studied at 6 A resolution by X-ray diffraction analysis. The electron density map showed a non-crystallographic three-fold screw arrangement of the molecules in the crystal. The molecule is an ellipsoid with approximate dimensions of 80 x 45 x 35 A and contains a hollow which may correspond to the active center. The inhibitor molecules bind to Taka-amylase A at four different sites, one of which is located in the hollow of the enzyme. The probable position of a thiol group is discussed in connection with heavy atom binding.
D000681:Amylases / Q000037:antagonists & inhibitors; D001230:Aspergillus / Q000201:enzymology*; D001236:Aspergillus oryzae / Q000201:enzymology*; D006046:Gold; D008628:Mercury; D008958:Models, Molecular; D010165:Palladium; D010984:Platinum; D011485:Protein Binding; D011487:Protein Conformation; D012834:Silver; D014501:Uranium; D014961:X-Ray Diffraction; D000516:alpha-Amylases / Q000037:antagonists & inhibitors
D012834:Silver; D010984:Platinum; D014501:Uranium; D010165:Palladium; D006046:Gold; D000681:Amylases; D000516:alpha-Amylases; D008628:Mercury