2phk Summary

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THE CRYSTAL STRUCTURE OF A PHOSPHORYLASE KINASE PEPTIDE SUBSTRATE COMPLEX: KINASE SUBSTRATE RECOGNITION

The structure was published by Lowe, E.D., Noble, M.E., Skamnaki, V.T., Oikonomakos, N.G., Owen, D.J., and Johnson, L.N., in 1997 in a paper entitled "The crystal structure of a phosphorylase kinase peptide substrate complex: kinase substrate recognition." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.6 Å and deposited in 1998.

The experimental data on which the structure is based was not deposited.

This PDB entry contains a complex of 2 biomacromolecules, namely PHOSPHORYLASE KINASE and MC-PEPTIDE.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule most likely forms heterotetramers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A PHOSPHORYLASE KINASE P00518 (15-291) (PHKG1_RABIT)search Oryctolagus cuniculussearch < 90% 277 100%
B MC-PEPTIDE Not available
Not available Not available 7 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P00518 (15 - 291) PHOSPHORYLASE KINASE Oryctolagus cuniculus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A Protein kinases, catalytic subunitsearch Phosphorylase Kinase; domain 1search, Transferase(Phosphotransferase) domain 1search Protein kinase domainsearch
B

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A (P00518) ATP bindingsearch transferase activity, transferring phosphorus-containing groupssearch protein kinase activitysearch phosphorylase kinase activitysearch protein serine/threonine kinase activitysearch calmodulin bindingsearch protein phosphorylationsearch glycogen biosynthetic processsearch phosphorylase kinase complexsearch

Chain InterPro annotation
A Protein kinase domainsearch Serine/threonine- / dual specificity protein kinase, catalytic domainsearch Phosphorylase kinase, gamma catalytic subunitsearch Serine/threonine-protein kinase, active sitesearch Protein kinase-like domainsearch Protein kinase, ATP binding sitesearch Calcium/calmodulin-dependent/calcium-dependent protein kinasesearch
B