FANCM-FAAP24-dsDNA complex. Determined by X-ray diffraction at 2.4 Å resolution. Released 11 Jun 2025.
Explore 9HJO in 3D Show helices and sheets RCSB PDB PDBe
9HJO contains 56 α-helices and 24 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 |
|---|---|---|---|
| β-strand | 1819-1823 | 5 | 1 |
| α-helix | 1824-1828 | 5 | |
| α-helix | 1831-1839 | 9 | |
| β-strand | 1844-1848 | 5 | 1 |
| β-strand | 1855-1856 | 2 | 1 |
| β-strand | 1861-1867 | 7 | 1 |
| α-helix | 1868-1872 | 5 | |
| α-helix | 1874-1876 | 3 | |
| α-helix | 1877-1888 | 12 | |
| β-strand | 1893-1899 | 7 | 1 |
| α-helix | 1900-1902 | 3 | |
| α-helix | 1916-1927 | 12 | |
| β-strand | 1931-1935 | 5 | 1 |
| α-helix | 1938-1954 | 17 | |
| α-helix | 1970-1977 | 8 | |
| α-helix | 1984-1993 | 10 | |
| α-helix | 1997-2001 | 5 | |
| α-helix | 2005-2011 | 7 | |
| α-helix | 2016-2026 | 11 | |
| α-helix | 2032-2034 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 18-22 | 5 | 2 |
| α-helix | 23-25 | 3 | |
| α-helix | 29-34 | 6 | |
| β-strand | 39-43 | 5 | 2 |
| β-strand | 50-51 | 2 | 2 |
| β-strand | 56-61 | 6 | 2 |
| α-helix | 63-68 | 6 | |
| α-helix | 71-81 | 11 | |
| β-strand | 86-92 | 7 | 2 |
| α-helix | 97-99 | 3 | |
| α-helix | 101-105 | 5 | |
| α-helix | 106-111 | 6 | |
| β-strand | 115-119 | 5 | 2 |
| α-helix | 122-137 | 16 | |
| α-helix | 140-142 | 3 | |
| α-helix | 156-163 | 8 | |
| α-helix | 173-180 | 8 | |
| α-helix | 184-189 | 6 | |
| α-helix | 192-199 | 8 | |
| α-helix | 201-212 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 18-22 | 5 | 4 |
| α-helix | 23-25 | 3 | |
| α-helix | 29-34 | 6 | |
| β-strand | 39-43 | 5 | 4 |
| β-strand | 50-51 | 2 | 4 |
| β-strand | 56-61 | 6 | 4 |
| α-helix | 63-68 | 6 | |
| α-helix | 71-81 | 11 | |
| β-strand | 86-92 | 7 | 4 |
| α-helix | 97-99 | 3 | |
| α-helix | 101-105 | 5 | |
| α-helix | 106-111 | 6 | |
| β-strand | 115-119 | 5 | 4 |
| α-helix | 122-137 | 16 | |
| α-helix | 140-142 | 3 | |
| α-helix | 156-163 | 8 | |
| α-helix | 173-180 | 8 | |
| α-helix | 184-189 | 6 | |
| α-helix | 192-198 | 7 | |
| α-helix | 201-212 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Fanconi anemia group M protein | A, C | protein | 234 | Homo sapiens | Q8IYD8 (AlphaFold model) |
| Fanconi anemia core complex-associated protein 24 | B, D | protein | 215 | Homo sapiens | Q9BTP7 (AlphaFold model) |
| DNA (25-mer) | F, H | DNA | 25 | synthetic construct | |
| DNA (25-mer) | G, I | DNA | 25 | synthetic construct |
>9HJO_1 Fanconi anemia group M protein (chains A, C) GKGTCILVGGHEITSGLEVISSLRAIHGLQVEVCPLNGCDYIVSNRMVVERRSQSEMLNS VNKNKFIEQIQHLQSMFERICVIVEKDREKTGDTSRMFRRTKSYDSLLTTLIGAGIRILF SSCQEETADLLKELSLVEQRKNVGIHVPTVVNSNKSEALQFYLSIPNISYITALNMCHQF SSVKRMANSSLQEISMYAQVTHQKAEEIYRYIHYVFDIQMLPNDLNQDRLKSDI
>9HJO_2 Fanconi anemia core complex-associated protein 24 (chains B, D) MEKNPPDDTGPVHVPLGHIVANEKWRGSQLAQEMQGKIKLIFEDGLTPDFYLSNRCCILY VTEADLVAGNGYRKRLVRVRNSNNLKGIVVVEKTRMSEQYFPALQKFTVLDLGMVLLPVA SQMEASCLVIQLVQEQTKEPSKNPLLGKKRALLLSEPSLLRTVQQIPGVGKVKAPLLLQK FPSIQQLSNASIGELEQVVGQAVAQQIHAFFTQPR
>9HJO_3 DNA (25-MER) (chains F, H) TACGCATCATCCAGCGCTCGGTTTT
>9HJO_4 DNA (25-MER) (chains G, I) TTTTCCGAGCGCTGGATGATGCGTA
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 4 |
Structural basis of Fanconi anemia pathway activation by FANCM. Bythell-Douglas, R., van Twest, S., Abbouche, L. et al. EMBO J (2025) 44:4013-4036. DOI 10.1038/s44318-025-00468-3 · PubMed
Other PDB entries of the same protein (UniProt Q8IYD8 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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