Deciphering the design of the tropomyosin molecule. Determined by X-ray diffraction at 2.0 Å resolution. Released 25 Jul 2001.
Explore 1IC2 in 3D Show helices and sheets RCSB PDB PDBe
1IC2 contains 5 α-helices and 0 β-strands across 4 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-74 | 72 | |
| α-helix | 75-77 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-75 | 73 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-73 | 71 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Tropomyosin alpha chain, skeletal muscle | A, B, C, D | protein | 81 | Gallus gallus | P04268 (AlphaFold model) |
>1IC2_1 TROPOMYOSIN ALPHA CHAIN, SKELETAL MUSCLE (chains A, B, C, D) MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEERSKQLEDELVALQKKLKGTEDELDKY SESLKDAQEKLELADKKATDC
Deciphering the design of the tropomyosin molecule. Brown, J.H., Kim, K.-H., Jun, G. et al. Proc Natl Acad Sci U S A (2001) 98:8496-8501. DOI 10.1073/pnas.131219198 · PubMed
Other PDB entries of the same protein (UniProt P04268 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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