Acarbose Rearrangement Mechanism Implied by the Kinetic and Structural Analysis of Human Pancreatic alpha-Amylase in Complex with Analogues and Their Elongated Counterparts
The structure was published by Li, C., Begum, A., Numao, S., Park, K.H., Withers, S.G., and Brayer, G.D., in 2005 in a paper entitled "Acarbose Rearrangement Mechanism Implied by the Kinetic and Structural Analysis of Human Pancreatic alpha-Amylase in Complex with Analogues and Their Elongated Counterparts" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.0 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. 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 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: