Bridging of double-strand DNA break activates PARP2/HPF1 to modify chromatin. Determined by electron microscopy at 6.3 Å resolution. Released 16 Sept 2020.
Explore 6X0M in 3D Show helices and sheets RCSB PDB PDBe
6X0M contains 64 α-helices and 58 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 | 38-45 | 8 | |
| β-strand | 79-80 | 2 | 7 |
| α-helix | 83-87 | 5 | |
| β-strand | 115-120 | 6 | 7 |
| β-strand | 127-132 | 6 | 7 |
| β-strand | 142-147 | 6 | 7 |
| α-helix | 153-154 | 2 | |
| β-strand | 155-156 | 2 | 7 |
| α-helix | 161-168 | 8 | |
| α-helix | 208-215 | 8 | |
| α-helix | 245-256 | 12 | |
| α-helix | 261-267 | 7 | |
| α-helix | 269-283 | 15 | |
| α-helix | 288-300 | 13 | |
| α-helix | 303-305 | 3 | |
| α-helix | 306-319 | 14 | |
| α-helix | 323-334 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 39-45 | 7 | |
| β-strand | 79-80 | 2 | 1 |
| α-helix | 83-87 | 5 | |
| α-helix | 102-104 | 3 | |
| β-strand | 115-120 | 6 | 1 |
| β-strand | 127-132 | 6 | 1 |
| β-strand | 142-147 | 6 | 1 |
| β-strand | 155-156 | 2 | 1 |
| α-helix | 161-171 | 11 | |
| α-helix | 208-215 | 8 | |
| α-helix | 245-256 | 12 | |
| α-helix | 261-267 | 7 | |
| α-helix | 269-283 | 15 | |
| α-helix | 287-300 | 14 | |
| α-helix | 303-305 | 3 | |
| α-helix | 306-319 | 14 | |
| α-helix | 323-334 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 80-82 | 3 | |
| β-strand | 92-94 | 3 | 8 |
| β-strand | 96-97 | 2 | 9 |
| β-strand | 100-101 | 2 | 9 |
| β-strand | 103-110 | 8 | 8 |
| β-strand | 115-126 | 12 | 8 |
| β-strand | 132-139 | 8 | 8 |
| β-strand | 146-151 | 6 | 8 |
| α-helix | 156-171 | 16 | |
| β-strand | 189-191 | 3 | 8 |
| α-helix | 223-232 | 10 | |
| α-helix | 235-243 | 9 | |
| α-helix | 244-248 | 5 | |
| α-helix | 259-277 | 19 | |
| α-helix | 283-295 | 13 | |
| α-helix | 304-307 | 4 | |
| α-helix | 311-333 | 23 | |
| α-helix | 344-352 | 9 | |
| β-strand | 354-358 | 5 | 10 |
| α-helix | 364-375 | 12 | |
| α-helix | 379-381 | 3 | |
| β-strand | 384-396 | 13 | 10 |
| α-helix | 399-402 | 4 | |
| β-strand | 410-415 | 6 | 10 |
| α-helix | 422-428 | 7 | |
| α-helix | 432-434 | 3 | |
| α-helix | 439-441 | 3 | |
| β-strand | 443 | 1 | 11 |
| β-strand | 445 | 1 | 11 |
| β-strand | 448-451 | 4 | 10 |
| α-helix | 454-458 | 5 | |
| α-helix | 459-461 | 3 | |
| β-strand | 469-478 | 10 | 10 |
| β-strand | 482-485 | 4 | 10 |
| α-helix | 490-493 | 4 | |
| β-strand | 501-504 | 4 | 10 |
| β-strand | 506-510 | 5 | 12 |
| α-helix | 512-514 | 3 | |
| β-strand | 516-518 | 3 | 10 |
| β-strand | 521-523 | 3 | 10 |
| β-strand | 528-530 | 3 | 12 |
| β-strand | 541-543 | 3 | 12 |
| β-strand | 545-548 | 4 | 10 |
| α-helix | 551-553 | 3 | |
| β-strand | 554-566 | 13 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 80-82 | 3 | |
| β-strand | 92-94 | 3 | 2 |
| β-strand | 96-97 | 2 | 3 |
| β-strand | 100-101 | 2 | 3 |
| β-strand | 103-110 | 8 | 2 |
| β-strand | 115-126 | 12 | 2 |
| β-strand | 132-139 | 8 | 2 |
| β-strand | 146-151 | 6 | 2 |
| α-helix | 156-171 | 16 | |
| β-strand | 189-191 | 3 | 2 |
| α-helix | 223-233 | 11 | |
| α-helix | 235-243 | 9 | |
| α-helix | 244-248 | 5 | |
| α-helix | 259-277 | 19 | |
| α-helix | 283-295 | 13 | |
| α-helix | 304-307 | 4 | |
| α-helix | 311-333 | 23 | |
| α-helix | 344-352 | 9 | |
| β-strand | 355-358 | 4 | 4 |
| α-helix | 364-375 | 12 | |
| β-strand | 384-395 | 12 | 4 |
| α-helix | 399-402 | 4 | |
| β-strand | 410-416 | 7 | 4 |
| α-helix | 422-428 | 7 | |
| α-helix | 432-434 | 3 | |
| α-helix | 439-441 | 3 | |
| β-strand | 443 | 1 | 5 |
| β-strand | 445 | 1 | 5 |
| β-strand | 448-451 | 4 | 4 |
| α-helix | 454-458 | 5 | |
| α-helix | 459-461 | 3 | |
| β-strand | 469-478 | 10 | 4 |
| β-strand | 482-485 | 4 | 4 |
| β-strand | 501-504 | 4 | 4 |
| β-strand | 506-510 | 5 | 6 |
| α-helix | 512-514 | 3 | |
| β-strand | 516-518 | 3 | 4 |
| β-strand | 521-523 | 3 | 4 |
| β-strand | 528-530 | 3 | 6 |
| β-strand | 541-543 | 3 | 6 |
| β-strand | 545-548 | 4 | 4 |
| α-helix | 551-553 | 3 | |
| β-strand | 554-566 | 13 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Histone PARylation factor 1 | O, o | protein | 356 | Homo sapiens | Q9NWY4 (AlphaFold model) |
| Poly [ADP-ribose] polymerase 2 | P, p | protein | 590 | Homo sapiens | Q9UGN5 (AlphaFold model) |
| DNA (167-mer) | I, i | DNA | 167 | synthetic construct | |
| DNA (167-mer) | J, j | DNA | 167 | synthetic construct |
>6X0M_1 Histone PARylation factor 1 (chains O, o) MGHHHHHHGGMVGGGGKRRPGGEGPQCEKTTDVKKSKFCEADVSSDLRKEVENHYKLSLP EDFYHFWKFCEELDPEKPSDSLSASLGLQLVGPYDILAGKHKTKKKSTGLNFNLHWRFYY DPPEFQTIIIGDNKTQYHMGYFRDSPDEFPVYVGINEAKKNCIIVPNGDNVFAAVKLFLT KKLKEITDKKKINLLKNIDEKLTEAARELGYSLEQRTVKMKQRDKKVVTKTFHGAGLVVP VDKNDVGYRELPETDADLKRICKTIVEAASDEERLKAFAPIQEMMTFVQFANDECDYGMG LELGMDLFCYGSHYFHKVAGQLLPLAYNLLKRNLFAEIIEEHLANRSQENIDQLAA
>6X0M_2 Poly [ADP-ribose] polymerase 2 (chains P, p) MGSSHHHHHHSSGLVPRGSHMAARRRRSTGGGRARALNESKRVNNGNTAPEDSSPAKKTR RCQRQESKKMPVAGGKANKDRTEDKQDESVKALLLKGKAPVDPECTAKVGKAHVYCEGND VYDVMLNQTNLQFNNNKYYLIQLLEDDAQRNFSVWMRWGRVGKMGQHSLVACSGNLNKAK EIFQKKFLDKTKNNWEDREKFEKVPGKYDMLQMDYATNTQDEEETKKEESLKSPLKPESQ LDLRVQELIKLICNVQAMEEMMMEMKYNTKKAPLGKLTVAQIKAGYQSLKKIEDCIRAGQ HGRALMEACNEFYTRIPHDFGLRTPPLIRTQKELSEKIQLLEALGDIEIAIKLVKTELQS PEHPLDQHYRNLHCALRPLDHESYEFKVISQYLQSTHAPTHSDYTMTLLDLFEVEKDGEK EAFREDLHNRMLLWHGSRMSNWVGILSHGLRIAPPEAPITGYMFGKGIYFADMSSKSANY CFASRLKNTGLLLLSEVALGQCNELLEANPKAEGLLQGKHSTKGLGKMAPSSAHFVTLNG STVPLGPASDTGILNPDGYTLNYNEYIVYNPNQVRMRYLLKVQFNFLQLW
>6X0M_3 DNA (167-MER) (chains I, i) CAATACATGCACAGGATGTATATATCTGACACGTGCCTGGAGACTAGGGAGTAATCCCCT TGGCGGTTAAAACGCGGGGGACAGCGCGTACGTGCGTTTAAGCGGTGCTAGAGCTGTCTA CGACCAATTGAGCGGCCTCGGCACCGGGATTCTCCAGGGCATCATAG
>6X0M_4 DNA (167-MER) (chains J, j) CTATGATGCCCTGGAGAATCCCGGTGCCGAGGCCGCTCAATTGGTCGTAGACAGCTCTAG CACCGCTTAAACGCACGTACGCGCTGTCCCCCGCGTTTTAACCGCCAAGGGGATTACTCC CTAGTCTCCAGGCACGTGTCAGATATATACATCCTGTGCATGTATTG
Bridging of DNA breaks activates PARP2-HPF1 to modify chromatin. Bilokapic, S., Suskiewicz, M.J., Ahel, I. et al. Nature (2020) 585:609-613. DOI 10.1038/s41586-020-2725-7 · PubMed
Other PDB entries of the same protein (UniProt Q9NWY4 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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