3FJQ
Crystal structure of cAMP-dependent protein kinase catalytic subunit alpha in complex with peptide inhibitor PKI alpha (6-25)
Summary for 3FJQ
| Entry DOI | 10.2210/pdb3fjq/pdb |
| Descriptor | cAMP-dependent protein kinase catalytic subunit alpha, cAMP-dependent protein kinase inhibitor alpha, MANGANESE (II) ION, ... (5 entities in total) |
| Functional Keywords | nucleotide binding, protein kinase activity, protein serine/threonine kinase activity, camp-dependent protein kinase activity, protein binding, atp binding, kinase activity, transferase activity, alternative splicing, atp-binding, camp, cytoplasm, kinase, lipoprotein, myristate, nucleotide-binding, nucleus, phosphoprotein, serine/threonine-protein kinase, transferase, protein kinase inhibitor |
| Biological source | Mus musculus (mouse) More |
| Cellular location | Cytoplasm . Isoform 2: Cell projection, cilium, flagellum : P05132 |
| Total number of polymer chains | 2 |
| Total formula weight | 43500.78 |
| Authors | |
| Primary citation | Thompson, E.E.,Kornev, A.P.,Kannan, N.,Kim, C.,Ten Eyck, L.F.,Taylor, S.S. Comparative surface geometry of the protein kinase family. Protein Sci., 18:2016-2026, 2009 Cited by PubMed Abstract: Identifying conserved pockets on the surfaces of a family of proteins can provide insight into conserved geometric features and sites of protein-protein interaction. Here we describe mapping and comparison of the surfaces of aligned crystallographic structures, using the protein kinase family as a model. Pockets are rapidly computed using two computer programs, FADE and Crevasse. FADE uses gradients of atomic density to locate grooves and pockets on the molecular surface. Crevasse, a new piece of software, splits the FADE output into distinct pockets. The computation was run on 10 kinase catalytic cores aligned on the alphaF-helix, and the resulting pockets spatially clustered. The active site cleft appears as a large, contiguous site that can be subdivided into nucleotide and substrate docking sites. Substrate specificity determinants in the active site cleft between serine/threonine and tyrosine kinases are visible and distinct. The active site clefts cluster tightly, showing a conserved spatial relationship between the active site and alphaF-helix in the C-lobe. When the alphaC-helix is examined, there are multiple mechanisms for anchoring the helix using spatially conserved docking sites. A novel site at the top of the N-lobe is present in all the kinases, and there is a large conserved pocket over the hinge and the alphaC-beta4 loop. Other pockets on the kinase core are strongly conserved but have not yet been mapped to a protein-protein interaction. Sites identified by this algorithm have revealed structural and spatially conserved features of the kinase family and potential conserved intermolecular and intramolecular binding sites. PubMed: 19610074DOI: 10.1002/pro.209 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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