Crystal structure of the pig pancreatic alpha-amylase complexed with malto-oligosaacharides under the effect of the chloride ion
The structure was published by Qian, M., Ajandouz, E.H., Payan, F., and Nahoum, V., in 2005 in a paper entitled "Molecular Basis of the Effects of Chloride Ion on the Acid-Base Catalyst in the Mechanism of Pancreatic alpha-Amylase" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.01 Å and deposited in 2004.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of Alpha-amylase, pancreatic. This molecule has the UniProt identifier P00690 (AMYP_PIG). The sample contained 496 residues which is 100% of the natural sequence. Out of 496 residues 496 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: