1PHK

TWO STRUCTURES OF THE CATALYTIC DOMAIN OF PHOSPHORYLASE, KINASE: AN ACTIVE PROTEIN KINASE COMPLEXED WITH NUCLEOTIDE, SUBSTRATE-ANALOGUE AND PRODUCT

Summary for 1PHK

• Entry DOI: 10.2210/pdb1phk/pdb
• Descriptor: PHOSPHORYLASE KINASE, MANGANESE (II) ION, ADENOSINE-5'-TRIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: glycogen metabolism, transferase, serine/threonine-protein, kinase, atp-binding, calmodulin-binding
• Biological source: Oryctolagus cuniculus (rabbit)
• Total number of polymer chains: 1
• Total formula weight: 34933.35

Authors

Owen, D.J.,Noble, M.E.M.,Garman, E.F.,Papageorgiou, A.C.,Johnson, L.N. (deposition date: 1996-03-15, release date: 1996-08-17, Last modification date: 2024-02-14)

Primary citation

Owen, D.J.,Noble, M.E.,Garman, E.F.,Papageorgiou, A.C.,Johnson, L.N.
Two structures of the catalytic domain of phosphorylase kinase: an active protein kinase complexed with substrate analogue and product.
Structure, 3:467-482, 1995

PubMed Abstract: Control of intracellular events by protein phosphorylation is promoted by specific protein kinases. All the known protein kinase possess a common structure that defines a catalytically competent entity termed the 'kinase catalytic core'. Within this common structural framework each kinase displays its own unique substrate specificity, and a regulatory mechanism that may be modulated by association with other proteins. Structural studies of phosphorylase kinase (Phk), the major substrate of which is glycogen phosphorylase, may be expected to shed light on its regulation.

PubMed: 7663944
DOI: 10.1016/S0969-2126(01)00180-0

Experimental method

X-RAY DIFFRACTION (2.2 Å)