1k9a Summary

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Crystal structure analysis of full-length carboxyl-terminal Src kinase at 2.5 A resolution

The structure was published by Ogawa, A., Takayama, Y., Sakai, H., et al., Nada, S., Okada, M., and Tsukihara, T., in 2002 in a paper entitled "Structure of the carboxyl-terminal Src kinase, Csk." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.5 Å and deposited in 2001.

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

This PDB entry contains multiple copies of the structure of Carboxyl-terminal Src kinase.

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 Carboxyl-terminal Src kinase P32577 (1-450) (CSK_RAT)search Rattus norvegicussearch 100% 450 98%
B Carboxyl-terminal Src kinase P32577 (1-450) (CSK_RAT)search Rattus norvegicussearch 100% 450 98%
C Carboxyl-terminal Src kinase P32577 (1-450) (CSK_RAT)search Rattus norvegicussearch 100% 450 98%
D Carboxyl-terminal Src kinase P32577 (1-450) (CSK_RAT)search Rattus norvegicussearch 100% 450 98%
E Carboxyl-terminal Src kinase P32577 (1-450) (CSK_RAT)search Rattus norvegicussearch 100% 450 98%
F Carboxyl-terminal Src kinase P32577 (1-450) (CSK_RAT)search Rattus norvegicussearch 100% 450 98%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P32577 (1 - 450) Carboxyl-terminal Src kinase Rattus norvegicus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B, C, D, E, F (P32577) SH3-domainsearch, SH2 domainsearch, Protein kinases, catalytic subunitsearch SH3 Domainssearch, SHC Adaptor Proteinsearch, Phosphorylase Kinase; domain 1search, Transferase(Phosphotransferase) domain 1search PF00017: SH2 domainsearch, PF00018: SH3 domainsearch, PF07714: Protein tyrosine kinasesearch

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A, B, C, D, E, F (P32577) protein tyrosine kinase activitysearch protein kinase activitysearch transferase activity, transferring phosphorus-containing groupssearch transferase activitysearch protein phosphatase bindingsearch ATP bindingsearch proline-rich region bindingsearch kinase activitysearch nucleotide bindingsearch identical protein bindingsearch non-membrane spanning protein tyrosine kinase activitysearch protein phosphorylationsearch negative regulation of phagocytosissearch cellular response to peptide hormone stimulussearch phosphorylationsearch peptidyl-tyrosine phosphorylationsearch negative regulation of Golgi to plasma membrane protein transportsearch brain developmentsearch oligodendrocyte differentiationsearch negative regulation of interleukin-6 productionsearch negative regulation of low-density lipoprotein particle clearancesearch immune system processsearch negative regulation of kinase activitysearch negative regulation of cell proliferationsearch positive regulation of MAP kinase activitysearch adherens junction organizationsearch regulation of Fc receptor mediated stimulatory signaling pathwaysearch negative regulation of bone resorptionsearch negative regulation of ERK1 and ERK2 cascadesearch protein autophosphorylationsearch plasma membranesearch cytoplasmsearch cell-cell junctionsearch membrane raftsearch membranesearch Golgi apparatussearch intracellular membrane-bounded organellesearch centrosomesearch

Chain InterPro annotation
A, B, C, D, E, F Protein kinase domainsearch SH2 domainsearch Serine-threonine/tyrosine-protein kinase catalytic domainsearch SH3 domainsearch Tyrosine-protein kinase, active sitesearch Protein kinase-like domainsearch Protein kinase, ATP binding sitesearch Tyrosine-protein kinase, catalytic domainsearch