1ahr Summary

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CALMODULIN MUTANT WITH A TWO RESIDUE DELETION IN THE CENTRAL HELIX

The structure was published by Tabernero, L., Taylor, D.A., Chandross, R.J., et al., Means, A.R., Quiocho, F.A., and Sack, J.S., in 1997 in a paper entitled "The structure of a calmodulin mutant with a deletion in the central helix: implications for molecular recognition and protein binding." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.8 Å and deposited in 1997.

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 P62149 (CALM_CHICK)search. The sample contained 146 residues which is 98% of the natural sequence. Out of 146 residues 146 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 P62149 (2-149) (CALM_CHICK)search Gallus gallussearch 98% 146 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P62149 (2 - 149) CALMODULIN Gallus gallus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P62149) Calmodulin-likesearch EF-handsearch PF00036: EF handsearch, PF13499: EF-hand domain pairsearch, PF13833: EF-hand domain pairsearch

Chain ID Biological process (GO) Molecular function (GO) Cellular component (GO)
A (P62149) positive regulation of ryanodine-sensitive calcium-release channel activitysearch positive regulation of phosphoprotein phosphatase activitysearch regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulumsearch positive regulation of protein dephosphorylationsearch regulation of cytokinesissearch regulation of cardiac muscle contractionsearch detection of calcium ionsearch substantia nigra developmentsearch regulation of heart ratesearch positive regulation of cyclic-nucleotide phosphodiesterase activitysearch positive regulation of cyclic nucleotide metabolic processsearch response to calcium ionsearch myosin bindingsearch protein domain specific bindingsearch thioesterase bindingsearch phospholipase bindingsearch protein kinase bindingsearch N-terminal myristoylation domain bindingsearch ion channel bindingsearch metal ion bindingsearch protein phosphatase activator activitysearch titin bindingsearch calcium ion bindingsearch nucleussearch spindle microtubulesearch sarcomeresearch extracellular vesicular exosomesearch calcium channel complexsearch spindle polesearch centrosomesearch vesiclesearch

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