THE CATALYTIC MECHANISM OF PHOSPHORYLASE KINASE PROBED BY MUTATIONAL STUDIES
The structure was published by Skamnaki, V.T., Owen, D.J., Noble, M.E., et al., Lowe, G., Oikonomakos, N.G., and Johnson, L.N., in 1999 in a paper entitled "Catalytic Mechanism of Phosphorylase Kinase Probed by Mutational Studies." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.4 Å and deposited in 1999.
The experimental data on which the structure is based was not deposited.
The PDB entry contains the structure of PHOSPHORYLASE KINASE. This molecule has the UniProt identifier P00518 (PHKG1_RABIT). The sample contained 298 residues which is < 90% of the natural sequence. Out of 298 residues 281 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: