3nr9 Summary


Structure of human CDC2-like kinase 2 (CLK2)

A publication describing this structure is not available. The depositing authors are Chaikuad, A.search; Savitsky, P.search; Krojer, T.search; Muniz, J.R.C.search; Filippakopoulos, P.search; Rellos, P.search; Keates, T.search; Fedorov, O.search; Pike, A.C.W.search; Eswaran, J.search; Berridge, G.search; Phillips, C.search; Zhang, Y.search; von Delft, F.search; Weigelt, J.search; Arrowsmith, C.H.search; Edwards, A.M.search; Bountra, C.search; Knapp, S.search; Structural Genomics Consortium (SGC)search

This crystal structure was determined using X-ray diffraction at a resolution of 2.89 Å and deposited in 2010.

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

This PDB entry contains multiple copies of the structure of Dual specificity protein kinase CLK2.

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 has more than one probable quaternary state observed. For more details see the quaternary structure page.

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 CLK2 P49760 (135-496) (CLK2_HUMAN)search Homo sapienssearch < 90% 368 94%
B Dual specificity protein kinase CLK2 P49760 (135-496) (CLK2_HUMAN)search Homo sapienssearch < 90% 368 94%
C Dual specificity protein kinase CLK2 P49760 (135-496) (CLK2_HUMAN)search Homo sapienssearch < 90% 368 94%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P49760 (135 - 496) Dual specificity protein kinase CLK2 Homo sapiens

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

Chain ID Molecular function (GO) Biological process (GO)
A, B, C (P49760) protein kinase activitysearch transferase activity, transferring phosphorus-containing groupssearch ATP bindingsearch protein serine/threonine kinase activitysearch protein phosphorylationsearch

Chain InterPro annotation
A, B, C 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