SUBSITE MAPPING OF THE ACTIVE SITE OF HUMAN PANCREATIC ALPHA-AMYLASE USING SUBSTRATES, THE PHARMACOLOGICAL INHIBITOR ACARBOSE, AND AN ACTIVE SITE VARIANT
The structure was published by Brayer, G.D., Sidhu, G., Maurus, R., et al., Nguyen, N.T., Overall, C.M., and Withers, S.G., in 2000 in a paper entitled "Subsite mapping of the human pancreatic alpha-amylase active site through structural, kinetic, and mutagenesis techniques." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 1999.
The experimental data on which the structure is based was not deposited.
The PDB entry contains the structure of PROTEIN (ALPHA-AMYLASE). This molecule has the UniProt identifier P04746 (AMYP_HUMAN). The sample contained 496 residues which is 100% of the natural sequence. Out of 496 residues 495 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: