Crystal structure of barley beta-amylase at atomic resolution
The structure was published by Rejzek, M., Stevenson, C.E.M., Southard, A.M., et al., Naldrett, M.J., Lawson, D.M., and Field, R.A., in 2011 in a paper entitled "Chemical Genetics and Cereal Starch Metabolism: Structural Basis of the Non-Covalent and Covalent Inhibition of Barley Beta-Amylase." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 0.97 Å and deposited in 2010.
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 P16098 (AMYB_HORVU). The sample contained 535 residues which is 100% of the natural sequence. Out of 535 residues 486 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: