3mft Summary


CASK-4M CaM Kinase Domain, Mn2+

The structure was published by Mukherjee, K., Sharma, M., Jahn, R., Wahl, M.C., and Sudhof, T.C., in 2010 in a paper entitled "Evolution of CASK into a Mg2+-sensitive kinase." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.2 Å and deposited in 2010.

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

The PDB entry contains the structure of Peripheral plasma membrane protein CASK. This molecule has the UniProt identifier O14936 (CSKP_HUMAN)search. The sample contained 351 residues which is < 90% of the natural sequence. Out of 351 residues 302 were observed and are deposited in the PDB.

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 Peripheral plasma membrane protein CASK O14936 (1-337) (CSKP_HUMAN)search Homo sapienssearch < 90% 351 86%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
O14936 (1 - 337) Peripheral plasma membrane protein CASK 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 (O14936) protein kinase activitysearch ATP bindingsearch transferase activity, transferring phosphorus-containing groupssearch protein serine/threonine kinase activitysearch 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