2IX7: Apo-calmodulin

Structure of apo-calmodulin bound to unconventional myosin V. Determined by X-ray diffraction at 2.5 Å resolution. Released 13 Dec 2006.

Method
X-ray diffraction
Resolution
2.5 Å
Organism
MUS MUSCULUS
Chains
3
Atoms
2,935
Mol. weight
40.42 kDa
Ligands
CYS
Released
13 Dec 2006

Explore 2IX7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2IX7 contains 19 α-helices and 9 β-strands across 3 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 9 helices, 4 β-strands

ElementResiduesLengthSheet
α-helix6-1914
β-strand26-2831
α-helix29-313
α-helix32-387
α-helix45-539
β-strand62-6431
α-helix65-7713
α-helix82-909
β-strand100-10122
α-helix102-11110
α-helix118-12710
β-strand135-13622
α-helix138-1447
Chain B: 9 helices, 5 β-strands
ElementResiduesLengthSheet
α-helix6-1813
β-strand26-2833
α-helix29-313
α-helix32-387
α-helix45-5410
β-strand62-6433
α-helix65-7511
α-helix82-909
β-strand99-10134
α-helix102-1098
α-helix118-1269
β-strand13014
β-strand135-13734
α-helix139-1457
Chain C: 1 helix, 0 β-strands
ElementResiduesLengthSheet
α-helix765-81854

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
CalmodulinA, Bprotein145MUS MUSCULUSP0DP26 (AlphaFold model)
Myosin-5ACprotein58MUS MUSCULUSQ99104 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>2IX7_1 CALMODULIN (chains A, B)
DQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNG
TIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEV
DEMIREADIDGDGQVNYEEFVQMMT
Sequence of entity 2 (C), FASTA
>2IX7_2 MYOSIN-5A (chains C)
ADKLRAACIRIQKTIRGWLLRKRYLCMQRAAITVQRYVRGYQARCYAKFLRRTKAATT

Ligands and cofactors

IDNameFormulaCopies
CYSCysteineC3 H7 N O2 S1

Water and common crystallization additives (SO4) are not listed.

Primary citation

Crystal Structure of Apo-Calmodulin Bound to the First Two Iq Motifs of Myosin V Reveals Essential Recognition Features. Houdusse, A., Gaucher, J.F., Krementsova, E. et al. Proc Natl Acad Sci U S A (2006) 103:19326. DOI 10.1073/PNAS.0609436103 · PubMed

Other PDB entries of the same protein (UniProt P0DP26 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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