2k3s Summary


HADDOCK-derived structure of the CH-domain of the smoothelin-like 1 complexed with the C-domain of apocalmodulin

The structure was published by Ishida, H., Borman, M.A., Ostrander, J., Vogel, H.J., and MacDonald, J.A., in 2008 in a paper entitled "Solution structure of the calponin homology (CH) domain from the smoothelin-like 1 protein: a unique apocalmodulin-binding mode and the possible role of the C-terminal type-2 CH-domain in smooth muscle relaxation." (abstract).

The structure was determined using NMR spectroscopy and deposited in 2008.

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

This PDB entry contains a complex of 2 biomacromolecules, namely Smoothelin-like protein 1 and Calmodulin.

The molecule most likely forms heterodimers.

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 Smoothelin-like protein 1 Q99LM3 (346-459) (SMTL1_MOUSE)search Mus musculussearch < 90% 119 100%
B Calmodulin P62155 (83-149) (CALM_XENLA)search Xenopus laevissearch 97% 67 100%

This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
Q99LM3 (346 - 459) Smoothelin-like protein 1 Mus musculus
P62155 (83 - 149) Calmodulin Xenopus laevis

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A Actin-binding Protein, T-fimbrin; domain 1search Calponin homology (CH) domainsearch
B (P62155) Calmodulin-likesearch PF00036: EF handsearch, PF13499: EF-hand domain pairsearch

Chain ID Molecular function (GO)
B (P62155) calcium ion bindingsearch

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