Crystal structure of the N-terminal regulatory domains of the formin FHOD1. Determined by X-ray diffraction at 2.3 Å resolution. Released 16 Sept 2008.
Explore 3DAD in 3D Show helices and sheets RCSB PDB PDBe
3DAD contains 43 α-helices and 11 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 | 15-22 | 8 | 1 |
| α-helix | 31-32 | 2 | |
| β-strand | 42-46 | 5 | 1 |
| α-helix | 51-53 | 3 | |
| α-helix | 55-62 | 8 | |
| β-strand | 71-75 | 5 | 1 |
| α-helix | 80 | 1 | |
| β-strand | 81 | 1 | 1 |
| α-helix | 82 | 1 | |
| α-helix | 98-100 | 3 | |
| α-helix | 102-104 | 3 | |
| β-strand | 109-114 | 6 | 1 |
| α-helix | 116-129 | 14 | |
| α-helix | 132-147 | 16 | |
| α-helix | 152-158 | 7 | |
| α-helix | 161-169 | 9 | |
| α-helix | 174-187 | 14 | |
| α-helix | 191-199 | 9 | |
| α-helix | 201-209 | 9 | |
| α-helix | 210-212 | 3 | |
| α-helix | 216-232 | 17 | |
| α-helix | 234-236 | 3 | |
| α-helix | 237-251 | 15 | |
| α-helix | 253-254 | 2 | |
| α-helix | 257-263 | 7 | |
| α-helix | 271-287 | 17 | |
| α-helix | 291-303 | 13 | |
| α-helix | 306-314 | 9 | |
| α-helix | 321-338 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 18 | 1 | 2 |
| β-strand | 20-22 | 3 | 3 |
| β-strand | 43 | 1 | 2 |
| α-helix | 51-53 | 3 | |
| α-helix | 55-61 | 7 | |
| β-strand | 71-75 | 5 | 3 |
| β-strand | 81 | 1 | 3 |
| α-helix | 89-91 | 3 | |
| β-strand | 110-114 | 5 | 3 |
| α-helix | 116-129 | 14 | |
| α-helix | 132-147 | 16 | |
| α-helix | 152-158 | 7 | |
| α-helix | 161-169 | 9 | |
| α-helix | 174-188 | 15 | |
| α-helix | 191-198 | 8 | |
| α-helix | 201-210 | 10 | |
| α-helix | 216-232 | 17 | |
| α-helix | 234-236 | 3 | |
| α-helix | 237-251 | 15 | |
| α-helix | 253-254 | 2 | |
| α-helix | 257-264 | 8 | |
| α-helix | 271-286 | 16 | |
| α-helix | 291-302 | 12 | |
| α-helix | 306-315 | 10 | |
| α-helix | 321-338 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| FH1/FH2 domain-containing protein 1 | A, B | protein | 339 | Homo sapiens | Q9Y613 (AlphaFold model) |
>3DAD_1 FH1/FH2 domain-containing protein 1 (chains A, B) MAGGEDRGDGEPVSVVTVRVQYLEDTDPFASANFPEPRRAPTCSLDGALPLGAQIPAVHR LLGAPLKLEDSALQVSPSGYYLDTELSLEEQREMLEGFYEEISKGRKPTLILRTQLSVRV NAILEKLYSSSGPELRRSLFSLKQIFQEDKDLVPEFVHSEGLSCLIRVGAAADHNYQSYI LRALGQLMLFVDGMLGVVAHSDTIQWLYTLCASLSRLVVKTALKLLLVFVEYSENNAPLF IRAVNSVASTTGAPPWANLVSILEEKNGADPELLVYTVTLINKTLAALPDQDSFYDVTDA LEQQGMEALVQRHLGTAGTDVDLRTQLVLYENALKLEDG
The Human Formin FHOD1 Contains a Bipartite Structure of FH3 and GTPase-Binding Domains Required for Activation. Schulte, A., Stolp, B., Schonichen, A. et al. Structure (2008) 16:1313-1323. DOI 10.1016/j.str.2008.06.008 · PubMed
Other PDB entries of the same protein (UniProt Q9Y613 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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