Directed 'in situ' Elongation as a Strategy to Characterize the Covalent Glycosyl-Enzyme Catalytic Intermediate of Human Pancreatic a-Amylase
The structure was published by Zhang, R., Li, C., Williams, L.K., Rempel, B.P., Brayer, G.D., and Withers, S.G., in 2009 in a paper entitled "Directed "in situ" inhibitor elongation as a strategy to structurally characterize the covalent glycosyl-enzyme intermediate of human pancreatic alpha-amylase" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.85 Å and deposited in 2009.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of Pancreatic 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: