2bki Summary



The structure was published by Menetrey, J., Bahloul, A., Wells, A., et al., Morris, C., Sweeney, H.L., and Houdusse, A., in 2005 in a paper entitled "The Structure of the Myosin Vi Motor Reveals the Mechanism of Directionality Reversal" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.9 Å and deposited in 2005.

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

This PDB entry contains a complex of 2 biomacromolecules, namely UNCONVENTIONAL MYOSIN and 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 most likely forms heterotrimers.

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 UNCONVENTIONAL MYOSIN Q29122 (1-859) (MYO6_PIG)search Sus scrofasearch < 90% 858 96%
B CALMODULIN P62149 (2-149) (CALM_CHICK)search Gallus gallussearch 98% 149 97%
D CALMODULIN P62149 (2-149) (CALM_CHICK)search Gallus gallussearch 98% 149 97%

This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
Q29122 (1 - 859) UNCONVENTIONAL MYOSIN Sus scrofa
P62149 (2 - 149) CALMODULIN Gallus gallus

Chain Structural classification (SCOP) Sequence family (Pfam)
A Myosin head (motor domain)search
B, D (P62149) Calmodulin-likesearch PF00036: EF handsearch, PF13499: EF-hand domain pairsearch, PF13833: EF-hand domain pairsearch

Chain ID Cellular component (GO) Molecular function (GO) Biological process (GO)
A (Q29122) myosin complexsearch motor activitysearch ATP bindingsearch
B, D (P62149) extracellular vesicular exosomesearch sarcomeresearch centrosomesearch nucleussearch spindle microtubulesearch spindle polesearch calcium channel complexsearch calcium ion bindingsearch myosin bindingsearch metal ion bindingsearch titin bindingsearch phospholipase bindingsearch ion channel bindingsearch N-terminal myristoylation domain bindingsearch protein domain specific bindingsearch thioesterase bindingsearch protein phosphatase activator activitysearch detection of calcium ionsearch positive regulation of cyclic-nucleotide phosphodiesterase activitysearch regulation of cardiac muscle contractionsearch regulation of cytokinesissearch positive regulation of phosphoprotein phosphatase activitysearch regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulumsearch positive regulation of ryanodine-sensitive calcium-release channel activitysearch positive regulation of protein dephosphorylationsearch response to calcium ionsearch substantia nigra developmentsearch regulation of heart ratesearch positive regulation of cyclic nucleotide metabolic processsearch

Chain InterPro annotation
A IQ motif, EF-hand binding sitesearch Myosin head, motor domainsearch P-loop containing nucleoside triphosphate hydrolasesearch
B, D EF-hand domainsearch EF-hand domain pairsearch EF-Hand 1, calcium-binding sitesearch