1qiw Summary

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CALMODULIN COMPLEXED WITH N-(3,3,-DIPHENYLPROPYL)-N'-[1-R-(3,4-BIS-BUTOXYPHENYL)-ETHYL]-PROPYLENEDIAMINE (DPD)

The structure was published by Harmat, V., Bocskei, Z.S., Naray-Szabo, G., et al., Liliom, K., Vertessy, B.G., and Ovadi, J., in 2000 in a paper entitled "A New Potent Calmodulin Antagonist with Arylalkylamine Structure: Crystallographic, Spectroscopic and Functional Studies" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.3 Å and deposited in 1999.

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

This PDB entry contains multiple copies of the structure of CALMODULIN.

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 CALMODULIN P62157 (2-149) (CALM_BOVIN)search Bos taurussearch 95% 148 97%
B CALMODULIN P62157 (2-149) (CALM_BOVIN)search Bos taurussearch 95% 148 97%


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, B (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, B (P62157) calcium ion bindingsearch protein bindingsearch metal ion bindingsearch spindle polesearch cytoplasmsearch spindlesearch cytosolsearch 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, B EF-hand domainsearch EF-hand domain pairsearch EF-Hand 1, calcium-binding sitesearch