SEVENFOLD MUTANT OF BARLEY BETA-AMYLASE
The structure was published by Mikami, B., Yoon, H.J., and Yoshigi, N., in 1999 in a paper entitled "The crystal structure of the sevenfold mutant of barley beta-amylase with increased thermostability at 2.5 A resolution." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.5 Å and deposited in 1998.
The experimental data on which the structure is based was not deposited.
The PDB entry contains the structure of PROTEIN (BETA-AMYLASE). This molecule has the UniProt identifier P16098 (AMYB_HORVU). The sample contained 500 residues which is 93% of the natural sequence. Out of 500 residues 500 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: