CRYSTAL STRUCTURE ANALYSIS OF THE MUTANT K300Q OF PSEUDOALTEROMONAS HALOPLANCTIS ALPHA-AMYLASE
The structure was published by Aghajari, N., Feller, G., Gerday, C., and Haser, R., in 2002 in a paper entitled "Structural basis of alpha-amylase activation by chloride" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.5 Å and deposited in 2001.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of ALPHA-AMYLASE. This molecule has the UniProt identifier P29957 (AMY_PSEHA). The sample contained 453 residues which is < 90% of the natural sequence. Out of 453 residues 447 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: