The role of an inner loop in the catalytic mechanism of soybean beta-amylase
The structure was published by Kang, Y.N., Tanabe, A., Adachi, M., Utsumi, S., and Mikami, B., in 2005 in a paper entitled "Structural analysis of threonine 342 mutants of soybean beta-amylase: role of a conformational change of the inner loop in the catalytic mechanism." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.35 Å and deposited in 2004.
The experimental data on which the structure is based was also 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 493 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: