CRYSTAL AND MOLECULAR STRUCTURE OF BARLEY ALPHA-AMYLASE
The structure was published by Kadziola, A., Abe, J., Svensson, B., and Haser, R., in 1994 in a paper entitled "Crystal and molecular structure of barley alpha-amylase." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.8 Å and deposited in 1994.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of 1,4-ALPHA-D-GLUCAN GLUCANOHYDROLASE. This molecule has the UniProt identifier P04063 (AMY2_HORVU). The sample contained 403 residues which is 100% of the natural sequence. Out of 403 residues 403 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: