1lin Summary

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CALMODULIN COMPLEXED WITH TRIFLUOPERAZINE (1:4 COMPLEX)

The structure was published by Vandonselaar, M., Hickie, R.A., Quail, J.W., and Delbaere, L.T., in 1994 in a paper entitled "Trifluoperazine-induced conformational change in Ca(2+)-calmodulin." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 1995.

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

The PDB entry contains the structure of CALMODULIN. This molecule has the UniProt identifier P62157 (CALM_BOVIN)search. The sample contained 148 residues which is 99% of the natural sequence. Out of 148 residues 142 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 CALMODULIN P62157 (2-149) (CALM_BOVIN)search Bos taurussearch 95% 148 98%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P62157 (2 - 149) CALMODULIN Bos taurus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P62157) Calmodulin-likesearch EF-handsearch PF00036: EF handsearch, PF13499: EF-hand domain pairsearch, PF13833: EF-hand domain pairsearch

Chain ID Molecular function (GO) Cellular component (GO) Biological process (GO)
A (P62157) protein bindingsearch calcium ion bindingsearch metal ion bindingsearch cytosolsearch spindle polesearch cytoplasmsearch spindlesearch cytoskeletonsearch positive regulation of ryanodine-sensitive calcium-release channel activitysearch negative regulation of ryanodine-sensitive calcium-release channel activitysearch regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulumsearch

Chain InterPro annotation
A EF-hand domainsearch EF-hand domain pairsearch EF-Hand 1, calcium-binding sitesearch