Solution NMR structure of a peptide encompassing residues 2-19 of the human formin INF2. Determined by solution NMR. Released 11 Sept 2024.
Explore 9FJN in 3D Show helices and sheets RCSB PDB PDBe
9FJN contains 1 α-helix and 0 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 |
|---|---|---|---|
| α-helix | 2-16 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Inverted formin-2 | A | protein | 18 | Homo sapiens | Q27J81 (AlphaFold model) |
>9FJN_1 Inverted formin-2 (chains A) SVKEGAQRKWAALKEKLG
Structure and function of the N-terminal extension of the formin INF2. Labat-de-Hoz, L., Comas, L., Rubio-Ramos, A. et al. Cell Mol Life Sci (2022) 79:571. DOI 10.1016/j.jmb.2015.09.014 · PubMed
Other PDB entries of the same protein (UniProt Q27J81 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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