Filia-N crystal structure. Determined by X-ray diffraction at 2.2 Å resolution. Released 15 Feb 2012.
Explore 3V69 in 3D Show helices and sheets RCSB PDB PDBe
3V69 contains 16 α-helices and 10 β-strands across 2 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 |
|---|---|---|---|
| β-strand | 13-17 | 5 | 1 |
| β-strand | 20-23 | 4 | 1 |
| α-helix | 27-30 | 4 | |
| α-helix | 35-38 | 4 | |
| β-strand | 42-46 | 5 | 2 |
| α-helix | 48-50 | 3 | |
| α-helix | 51-55 | 5 | |
| α-helix | 57-59 | 3 | |
| α-helix | 62-69 | 8 | |
| β-strand | 72-76 | 5 | 2 |
| β-strand | 84-89 | 6 | 2 |
| α-helix | 92-116 | 25 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7-8 | 2 | |
| β-strand | 13-17 | 5 | 3 |
| β-strand | 20-23 | 4 | 3 |
| α-helix | 27-30 | 4 | |
| α-helix | 35-39 | 5 | |
| β-strand | 41-46 | 6 | 4 |
| α-helix | 48-50 | 3 | |
| α-helix | 51-55 | 5 | |
| α-helix | 57-59 | 3 | |
| α-helix | 62-69 | 8 | |
| β-strand | 72-76 | 5 | 4 |
| α-helix | 83 | 1 | |
| β-strand | 84-89 | 6 | 4 |
| α-helix | 98-112 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein Filia | A, B | protein | 140 | Mus musculus | Q9CWU5 (AlphaFold model) |
>3V69_1 Protein Filia (chains A, B) MHHHHHHENLYFQSNAMASLKRFQTLVPLDHKQGTLFEIIGEPKLPKWFHVECLEDPKRL YVEPRLLEIMFGKDGEHIPHLESMLHTLIHVNVWGPERRAEIWIFGPPPFRRDVDRMLTD LAHYCRMKLMEIEALEAGVE
The N-terminus of FILIA Forms an Atypical KH Domain with a Unique Extension Involved in Interaction with RNA. Wang, J., Xu, M., Zhu, K. et al. PLoS One (2012) 7:e30209-e30209. DOI 10.1371/journal.pone.0030209 · PubMed
Other PDB entries of the same protein (UniProt Q9CWU5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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