STRUCTURE AND MOLECULAR MODEL REFINEMENT OF ASPERGILLUS ORYZAE (TAKA) ALPHA-AMYLASE: AN APPLICATION OF THE SIMULATED-ANNEALING METHOD
The structure was published by Swift, H.J., Brady, L., Derewenda, Z.S., et al., Dodson, G.G., Turkenburg, J.P., and Wilkinson, A.J., in 1991 in a paper entitled "Structure and molecular model refinement of Aspergillus oryzae (TAKA) alpha-amylase: an application of the simulated-annealing method." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.1 Å and deposited in 1992.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of ALPHA-AMYLASE. This molecule has the UniProt identifier P0C1B3 (AMYA1_ASPOR). The sample contained 478 residues which is 100% of the natural sequence. Out of 478 residues 476 were observed and are deposited in the PDB.
It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.
The molecule is most likely monomeric.
The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):
This entry contains 1 unique UniProt protein: