1ql6 Summary

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THE CATALYTIC MECHANISM OF PHOSPHORYLASE KINASE PROBED BY MUTATIONAL STUDIES

The structure was published by Skamnaki, V.T., Owen, D.J., Noble, M.E., et al., Lowe, G., Oikonomakos, N.G., and Johnson, L.N., in 1999 in a paper entitled "Catalytic Mechanism of Phosphorylase Kinase Probed by Mutational Studies." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.4 Å and deposited in 1999.

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

The PDB entry contains the structure of PHOSPHORYLASE KINASE. This molecule has the UniProt identifier P00518 (PHKG1_RABIT)search. The sample contained 298 residues which is < 90% of the natural sequence. Out of 298 residues 281 were observed and are deposited in the PDB.

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 is most likely monomeric.

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 (2-299) (PHKG1_RABIT)search Oryctolagus cuniculussearch < 90% 298 94%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P00518 (2 - 299) 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

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

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