CRYSTAL STRUCTURE AT 1.5A RESOLUTION OF THE BARLEY ALPHA-AMYLASE ISOZYME 1
The structure was published by Robert, X., Haser, R., Gottschalk, T.E., et al., Driguez, H., Svensson, B., and Aghajari, N., in 2003 in a paper entitled "The structure of barley alpha-amylase isozyme 1 reveals a novel role of domain C in substrate recognition and binding: a pair of sugar tongs" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.5 Å and deposited in 2000.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of ALPHA-AMYLASE ISOZYME 1. This molecule has the UniProt identifier P00693 (AMY1_HORVU). The sample contained 405 residues which is 98% of the natural sequence. Out of 405 residues 404 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: