1BKX
A BINARY COMPLEX OF THE CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE AND ADENOSINE FURTHER DEFINES CONFORMATIONAL FLEXIBILITY
Summary for 1BKX
| Entry DOI | 10.2210/pdb1bkx/pdb |
| Descriptor | CAMP-DEPENDENT PROTEIN KINASE, ADENOSINE MONOPHOSPHATE (3 entities in total) |
| Functional Keywords | conformational changes, electrostatic complementarity, phosphorylation, protein kinase, transferase, complex (phosphotransferase-adenosine), phosphotransferase, complex (phosphotransferase-adenosine) complex, complex (phosphotransferase/adenosine) |
| Biological source | Mus musculus (house mouse) |
| Cellular location | Cytoplasm (By similarity): P05132 |
| Total number of polymer chains | 1 |
| Total formula weight | 41084.52 |
| Authors | Narayana, N.,Cox, S.,Xuong, N.,Ten Eyck, L.F.,Taylor, S.S. (deposition date: 1997-07-01, release date: 1998-03-18, Last modification date: 2024-10-30) |
| Primary citation | Narayana, N.,Cox, S.,Nguyen-huu, X.,Ten Eyck, L.F.,Taylor, S.S. A binary complex of the catalytic subunit of cAMP-dependent protein kinase and adenosine further defines conformational flexibility. Structure, 5:921-935, 1997 Cited by PubMed Abstract: cAMP-dependent protein kinase (cAPK), a ubiquitous protein in eukaryotic cells, is one of the simplest members of the protein kinase family. It was the first protein kinase to be crystallized and continues to serve as a biochemical and structural prototype for this family of enzymes. To further understand the conformational changes that occur in different liganded and unliganded states of cAPK, the catalytic subunit of cAPK was crystallized in the absence of peptide inhibitor. PubMed: 9261084DOI: 10.1016/S0969-2126(97)00246-3 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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