Role of aromatic residues in starch binding
The structure was published by Ragunath, C., Manuel, S.G.A., Kasinathan, C., and Ramasubbu, N., in 2008 in a paper entitled "Structure-function relationships in human salivary alpha-amylase: role of aromatic residues in a secondary binding site" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 2007.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of Alpha-amylase 1. This molecule has the UniProt identifier P04745 (AMY1_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: