3EGH

Crystal structure of a complex between Protein Phosphatase 1 alpha (PP1), the PP1 binding and PDZ domains of Spinophilin and the small natural molecular toxin Nodularin-R

Summary for 3EGH

Entry DOI	10.2210/pdb3egh/pdb
Related	1FJM 1S70 2G5M 3E7A 3EGG 3HVQ
Related PRD ID	PRD_000214
Descriptor	Serine/threonine-protein phosphatase PP1-alpha catalytic subunit, Spinophilin, nodularin R, ... (6 entities in total)
Functional Keywords	pp1, serine/threonine phosphatase, post synaptic density, inhibitor, carbohydrate metabolism, cell cycle, cell division, glycogen metabolism, hydrolase, iron, manganese, metal-binding, phosphoprotein, protein phosphatase, actin-binding, cell junction, cell projection, cytoskeleton, developmental protein, differentiation, neurogenesis, nucleus, synapse, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
Biological source	Homo sapiens (Human) More
Cellular location	Cytoplasm: P62136 Cytoplasm, cytoskeleton: O35274
Total number of polymer chains	6
Total formula weight	114118.92
Authors	Ragusa, M.J.,Page, R.,Peti, W. (deposition date: 2008-09-10, release date: 2010-03-23, Last modification date: 2023-11-15)
Primary citation	Ragusa, M.J.,Dancheck, B.,Critton, D.A.,Nairn, A.C.,Page, R.,Peti, W. Spinophilin directs protein phosphatase 1 specificity by blocking substrate binding sites. Nat.Struct.Mol.Biol., 17:459-464, 2010 Cited by PubMed: 20305656 DOI: 10.1038/nsmb.1786 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2 Å)

Structure validation