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3HVQ

Crystal structure of a complex between Protein Phosphatase 1 alpha (PP1) and the PP1 binding and PDZ domains of Neurabin

Summary for 3HVQ
Entry DOI10.2210/pdb3hvq/pdb
Related1FJM 1S70 2FN5 2GLE 3EGG 3EGH
DescriptorSerine/threonine-protein phosphatase PP1-alpha catalytic subunit, Neurabin-1, MANGANESE (II) ION, ... (6 entities in total)
Functional Keywordspp1, neurabin, serine/threonine phosphatase, post synaptic density, glutametergic receptors, 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, synaptosome, hydrolase-hydrolase regulator complex, hydrolase/hydrolase regulator
Biological sourceHomo sapiens (human)
More
Cellular locationCytoplasm: P62136
Cytoplasm, cytoskeleton: O35867
Total number of polymer chains4
Total formula weight113085.40
Authors
Critton, D.A.,Ragusa, M.J.,Page, R.,Peti, W. (deposition date: 2009-06-16, release date: 2010-03-23, Last modification date: 2023-09-06)
Primary citationRagusa, 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 (2.2 Å)
Structure validation

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