Nesprin-1G (aa2070-2200)-FHOD1(aa1-339) complex, H. sapiens. Determined by X-ray diffraction at 7.11 Å resolution. Released 3 Feb 2021.
Explore 6XF2 in 3D Show helices and sheets RCSB PDB PDBe
6XF2 contains 51 α-helices and 14 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 | 2071-2107 | 37 | |
| α-helix | 2118-2150 | 33 | |
| α-helix | 2166-2196 | 31 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 15-22 | 8 | 1 |
| α-helix | 28-30 | 3 | |
| β-strand | 42-46 | 5 | 1 |
| β-strand | 50 | 1 | 2 |
| α-helix | 52-54 | 3 | |
| α-helix | 55-62 | 8 | |
| α-helix | 68-70 | 3 | |
| β-strand | 71-75 | 5 | 1 |
| β-strand | 81 | 1 | 1 |
| β-strand | 87 | 1 | 2 |
| α-helix | 92-94 | 3 | |
| α-helix | 96-103 | 8 | |
| β-strand | 109-114 | 6 | 1 |
| α-helix | 116-129 | 14 | |
| α-helix | 132-148 | 17 | |
| α-helix | 152-158 | 7 | |
| α-helix | 161-169 | 9 | |
| α-helix | 174-188 | 15 | |
| α-helix | 191-199 | 9 | |
| α-helix | 201-210 | 10 | |
| α-helix | 216-232 | 17 | |
| α-helix | 237-251 | 15 | |
| α-helix | 254 | 1 | |
| α-helix | 257-263 | 7 | |
| α-helix | 271-285 | 15 | |
| α-helix | 291-304 | 14 | |
| α-helix | 306-315 | 10 | |
| α-helix | 321-333 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2071-2102 | 32 | |
| α-helix | 2104-2106 | 3 | |
| α-helix | 2120-2155 | 36 | |
| α-helix | 2168-2196 | 29 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 15-22 | 8 | 3 |
| α-helix | 28-30 | 3 | |
| β-strand | 42-46 | 5 | 3 |
| β-strand | 50 | 1 | 4 |
| α-helix | 52-54 | 3 | |
| α-helix | 55-62 | 8 | |
| α-helix | 68-70 | 3 | |
| β-strand | 71-75 | 5 | 3 |
| α-helix | 80 | 1 | |
| β-strand | 81 | 1 | 3 |
| α-helix | 82-83 | 2 | |
| β-strand | 87 | 1 | 4 |
| α-helix | 92-94 | 3 | |
| α-helix | 96-103 | 8 | |
| β-strand | 109-114 | 6 | 3 |
| α-helix | 116-129 | 14 | |
| α-helix | 132-148 | 17 | |
| α-helix | 152-158 | 7 | |
| α-helix | 161-169 | 9 | |
| α-helix | 174-188 | 15 | |
| α-helix | 191-199 | 9 | |
| α-helix | 201-210 | 10 | |
| α-helix | 216-232 | 17 | |
| α-helix | 237-251 | 15 | |
| α-helix | 254 | 1 | |
| α-helix | 257-263 | 7 | |
| α-helix | 271-285 | 15 | |
| α-helix | 292-304 | 13 | |
| α-helix | 306-315 | 10 | |
| α-helix | 321-333 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Nesprin-1 | A, C | protein | 131 | Homo sapiens | Q8NF91 (AlphaFold model) |
| FH1/FH2 domain-containing protein 1 | B, D | protein | 321 | Homo sapiens | Q9Y613 (AlphaFold model) |
>6XF2_1 Nesprin-1 (chains A, C) TKRLIHENQGQCCGLIDLMREYQNLKSAVSKVLENASSVIVTRTTIKDQEDLKWAFSKHE TAKNKMNYKQKDLDNFTSKGKHLLSELKKIHSSDFSLVKTDMESTVDKWLDVSEKLEENM DRLRVSLSIWD
>6XF2_2 FH1/FH2 domain-containing protein 1 (chains B, D) SVVTVRVQYLEDTDPFACANFPEPRRAPTCSLDGALPLGAQIPAVHRLLGAPLKLEDCAL QVSPSGYYLDTELSLEEQREMLEGFYEEISKGRKPTLILRTQLSVRVNAILEKLYSSSGP ELRRSLFSLKQIFQEDKDLVPEFVHSEGLSCLIRVGAAADHNYQSYILRALGQLMLFVDG MLGVVAHSDTIQWLYTLCASLSRLVVKTALKLLLVFVEYSENNAPLFIRAVNSVASTTGA PPWANLVSILEEKNGADPELLVYTVTLINKTLAALPDQDSFYDVTDALEQQGMEALVQRH LGTAGTDVDLRTQLVLYENAL
Structures of FHOD1-Nesprin1/2 complexes reveal alternate binding modes for the FH3 domain of formins. Lim, S.M., Cruz, V.E., Antoku, S. et al. Structure (2021) 29:540-552.e5. DOI 10.1016/j.str.2020.12.013 · PubMed
Other PDB entries of the same protein (UniProt Q8NF91 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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