1z57 Summary


Crystal structure of human CLK1 in complex with 10Z-Hymenialdisine

The structure was published by Bullock, A.N., Das, S., Debreczeni, J.E., et al., Turk, B.E., Ghosh, G., and Knapp, S., in 2009 in a paper entitled "Kinase domain insertions define distinct roles of CLK kinases in SR protein phosphorylation." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.7 Å and deposited in 2005.

The experimental data on which the structure is based was also deposited.

The PDB entry contains the structure of Dual specificity protein kinase CLK1. This molecule has the UniProt identifier P49759 (CLK1_HUMAN)search. The sample contained 339 residues which is < 90% of the natural sequence. Out of 339 residues 326 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 Dual specificity protein kinase CLK1 P49759 (148-484) (CLK1_HUMAN)search Homo sapienssearch < 90% 339 98%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P49759 (148 - 484) Dual specificity protein kinase CLK1 Homo sapiens

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

Chain ID Molecular function (GO) Biological process (GO)
A (P49759) protein kinase activitysearch transferase activity, transferring phosphorus-containing groupssearch ATP bindingsearch protein phosphorylationsearch

Chain InterPro annotation
A Protein kinase domainsearch Serine/threonine/dual specificity protein kinase, catalytic domainsearch Serine/threonine-protein kinase, active sitesearch Protein kinase-like domainsearch Protein kinase, ATP binding sitesearch