1SMH
Protein kinase A variant complex with completely ordered N-terminal helix
Summary for 1SMH
Entry DOI | 10.2210/pdb1smh/pdb |
Descriptor | cAMP-Dependent Protein Kinase, alpha-catalytic subunit, cAMP-dependent protein kinase inhibitor, alpha form, (R,R)-2,3-BUTANEDIOL, ... (5 entities in total) |
Functional Keywords | pka; protein kinase a; camp-dependent protein kinase; phosphorylation; ser10; myristoylation; posttranslational modification; signaling; membrane, alpha helix, signaling protein, transferase-inhibitor complex, transferase/inhibitor |
Biological source | Bos taurus (cattle) More |
Cellular location | Cytoplasm: P00517 |
Total number of polymer chains | 2 |
Total formula weight | 43751.92 |
Authors | Breitenlechner, C.,Engh, R.A.,Huber, R.,Kinzel, V.,Bossemeyer, D.,Gassel, M. (deposition date: 2004-03-09, release date: 2004-07-06, Last modification date: 2021-10-27) |
Primary citation | Breitenlechner, C.,Engh, R.A.,Huber, R.,Kinzel, V.,Bossemeyer, D.,Gassel, M. The Typically Disordered N-Terminus of PKA Can Fold as a Helix and Project the Myristoylation Site into Solution Biochemistry, 43:7743-7749, 2004 Cited by PubMed: 15196017DOI: 10.1021/bi0362525 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.044 Å) |
Structure validation
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