4QX5
Neutron diffraction reveals hydrogen bonds critical for cGMP-selective activation: Insights for PKG agonist design
Summary for 4QX5
Entry DOI | 10.2210/pdb4qx5/pdb |
Descriptor | cGMP-dependent protein kinase 1, ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE, IODIDE ION, ... (4 entities in total) |
Functional Keywords | phosphate binding cassette/cyclic gmp binding domain/pkg, serine/threonine kinase, cyclic gmp, transferase |
Biological source | Homo sapiens (human) |
Cellular location | Cytoplasm : Q13976 |
Total number of polymer chains | 1 |
Total formula weight | 19559.29 |
Authors | Huang, G.Y.,Gerlits, O.O.,Blakeley, M.P.,Sankaran, B.,Kovalevsky, A.Y.,Kim, C. (deposition date: 2014-07-18, release date: 2014-11-12, Last modification date: 2024-02-28) |
Primary citation | Huang, G.Y.,Gerlits, O.O.,Blakeley, M.P.,Sankaran, B.,Kovalevsky, A.Y.,Kim, C. Neutron Diffraction Reveals Hydrogen Bonds Critical for cGMP-Selective Activation: Insights for cGMP-Dependent Protein Kinase Agonist Design. Biochemistry, 53:6725-6727, 2014 Cited by PubMed: 25271401DOI: 10.1021/bi501012v PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.318 Å) |
Structure validation
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