Magic Angle Spinning NMR Structure of Human Cofilin-2 Assembled on Actin Filaments. Determined by solid-state NMR. Released 20 Apr 2022.
Explore 7M0G in 3D Show helices and sheets RCSB PDB PDBe
7M0G contains 8 α-helices and 9 β-strands across 1 chain. 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 |
|---|---|---|---|
| β-strand | 6-7 | 2 | 1 |
| α-helix | 9-11 | 3 | |
| α-helix | 12-19 | 8 | |
| α-helix | 28-31 | 4 | |
| β-strand | 37 | 1 | 2 |
| β-strand | 38-40 | 3 | 1 |
| β-strand | 46-49 | 4 | 1 |
| α-helix | 57-60 | 4 | |
| α-helix | 68-74 | 7 | |
| β-strand | 81-90 | 10 | 2 |
| β-strand | 95-104 | 10 | 2 |
| α-helix | 111-127 | 17 | |
| β-strand | 131-137 | 7 | 2 |
| α-helix | 140-144 | 5 | |
| α-helix | 146-153 | 8 | |
| β-strand | 160-161 | 2 | 2 |
| β-strand | 164-165 | 2 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cofilin-2 | A | protein | 166 | Homo sapiens | Q9Y281 (AlphaFold model) |
>7M0G_1 Cofilin-2 (chains A) MASGVTVNDEVIKVFNDMKVRKSSTQEEIKKRKKAVLFCLSDDKRQIIVEEAKQILVGDI GDTVEDPYTSFVKLLPLNDCRYALYDATYETKESKKEDLVFIFWAPESAPLKSKMIYASS KDAIKKKFTGIKHEWQVNGLDDIKDRSTLGEKLGGNVVVSLEGKPL
Magic angle spinning NMR structure of human cofilin-2 assembled on actin filaments reveals isoform-specific conformation and binding mode. Kraus, J., Russell, R.W., Kudryashova, E. et al. Nat Commun (2022) 13:2114-2114. DOI 10.1038/s41467-022-29595-9 · PubMed
Other PDB entries of the same protein (UniProt Q9Y281 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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