1BKX
A BINARY COMPLEX OF THE CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE AND ADENOSINE FURTHER DEFINES CONFORMATIONAL FLEXIBILITY
1BKX の概要
| エントリーDOI | 10.2210/pdb1bkx/pdb |
| 分子名称 | CAMP-DEPENDENT PROTEIN KINASE, ADENOSINE MONOPHOSPHATE (3 entities in total) |
| 機能のキーワード | conformational changes, electrostatic complementarity, phosphorylation, protein kinase, transferase, complex (phosphotransferase-adenosine), phosphotransferase, complex (phosphotransferase-adenosine) complex, complex (phosphotransferase/adenosine) |
| 由来する生物種 | Mus musculus (house mouse) |
| 細胞内の位置 | Cytoplasm (By similarity): P05132 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 41084.52 |
| 構造登録者 | Narayana, N.,Cox, S.,Xuong, N.,Ten Eyck, L.F.,Taylor, S.S. (登録日: 1997-07-01, 公開日: 1998-03-18, 最終更新日: 2024-10-30) |
| 主引用文献 | 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 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.6 Å) |
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