Crystal Structure Analysis of Triple (T47M/Y164E/T328N)/maltose of Bacillus cereus Beta-Amylase at pH 6.5
The structure was published by Hirata, A., Adachi, M., Utsumi, S., and Mikami, B., in 2004 in a paper entitled "Engineering of the pH optimum of Bacillus cereus beta-amylase: conversion of the pH optimum from a bacterial type to a higher-plant type" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.06 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 P36924 (AMYB_BACCE). The sample contained 516 residues which is 100% of the natural sequence. Out of 516 residues 516 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: