CALCIUM BINDING IN ALPHA-AMYLASES: AN X-RAY DIFFRACTION STUDY AT 2.1 ANGSTROMS RESOLUTION OF TWO ENZYMES FROM ASPERGILLUS
The structure was published by Boel, E., Brady, L., Brzozowski, A.M., et al., Swift, H., Thim, L., and Woldike, H.F., in 1990 in a paper entitled "Calcium binding in alpha-amylases: an X-ray diffraction study at 2.1-A resolution of two enzymes from Aspergillus." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.12 Å and deposited in 1991.
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 P56271 (AMYA_ASPNG). The sample contained 484 residues which is 100% of the natural sequence. Out of 484 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: