Crystal Structure of F327A/K285P Mutant of cAMP-dependent Protein Kinase
The structure was published by Yang, J., Kennedy, E.J., Wu, J., et al., Pennypacker, J., Ghosh, G., and Taylor, S.S., in 2009 in a paper entitled "Contribution of non-catalytic core residues to activity and regulation in protein kinase A." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.5 Å and deposited in 2007.
The experimental data on which the structure is based was also deposited.
This PDB entry contains a complex of 2 biomacromolecules, namely cAMP-dependent protein kinase, alpha-catalytic subunit and 20-mer fragment from cAMP-dependent protein kinase inhibitor alpha.
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 most likely forms heterodimers.
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 2 unique UniProt proteins: