Summary for 5UMO
| Entry DOI | 10.2210/pdb5umo/pdb |
| Descriptor | Mitogen-activated protein kinase 1, SULFATE ION (3 entities in total) |
| Functional Keywords | kinase, erk2, transferase |
| Biological source | Rattus norvegicus (Rat) |
| Cellular location | Cytoplasm, cytoskeleton, spindle : P63086 |
| Total number of polymer chains | 1 |
| Total formula weight | 42255.50 |
| Authors | CHLEBOWICZ, J.,ZHANG, F.,GOLDSMITH, E.J. (deposition date: 2017-01-27, release date: 2017-03-01, Last modification date: 2024-05-22) |
| Primary citation | Zhang, F.,Strand, A.,Robbins, D.,Cobb, M.H.,Goldsmith, E.J. Atomic structure of the MAP kinase ERK2 at 2.3 A resolution. Nature, 367:704-711, 1994 Cited by PubMed Abstract: The structure of the MAP kinase ERK2, a ubiquitous protein kinase target for regulation by Ras and Raf, has been solved in its unphosphorylated low-activity conformation to a resolution of 2.3 A. The two domains of unphosphorylated ERK2 are farther apart than in the active conformation of cAMP-dependent protein kinase and the peptide-binding site is blocked by tyrosine 185, one of the two residues that are phosphorylated in the active enzyme. Activation of ERK2 is thus likely to involve both global and local conformational changes. PubMed: 8107865DOI: 10.2210/pdb1erk/pdb PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.26 Å) |
Structure validation
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