CRYSTAL STRUCTURES OF SOYBEAN BETA-AMYLASE REACTED WITH BETA-MALTOSE AND MALTAL: ACTIVE SITE COMPONENTS AND THEIR APPARENT ROLE IN CATALYSIS
The structure was published by Mikami, B., Degano, M., Hehre, E.J., and Sacchettini, J.C., in 1994 in a paper entitled "Crystal structures of soybean beta-amylase reacted with beta-maltose and maltal: active site components and their apparent roles in catalysis." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.2 Å and deposited in 1994.
The experimental data on which the structure is based was not deposited.
The PDB entry contains the structure of BETA-AMYLASE. This molecule has the UniProt identifier P10538 (AMYB_SOYBN). The sample contained 495 residues which is 100% of the natural sequence. Out of 495 residues 491 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: