Cryo-EM structure of the XPF-ERCC1-SLX4(330-555)-SLX4IP complex. Determined by electron microscopy at 3.2 Å resolution. Released 17 Dec 2025.
Explore 9QED in 3D Show helices and sheets RCSB PDB PDBe
9QED contains 62 α-helices and 36 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 | 17-27 | 11 | |
| β-strand | 32-35 | 4 | 5 |
| α-helix | 41-51 | 11 | |
| β-strand | 58-61 | 4 | 5 |
| α-helix | 66-79 | 14 | |
| β-strand | 86-88 | 3 | 5 |
| α-helix | 94-103 | 10 | |
| β-strand | 105-109 | 5 | 5 |
| α-helix | 111-120 | 10 | |
| β-strand | 128-133 | 6 | 5 |
| α-helix | 136-139 | 4 | |
| α-helix | 143-155 | 13 | |
| β-strand | 160-165 | 6 | 5 |
| α-helix | 168-171 | 4 | |
| α-helix | 178-184 | 7 | |
| β-strand | 190-193 | 4 | 5 |
| α-helix | 198-204 | 7 | |
| β-strand | 212-217 | 6 | 4 |
| α-helix | 218-219 | 2 | |
| α-helix | 220-243 | 24 | |
| α-helix | 245-247 | 3 | |
| α-helix | 250-252 | 3 | |
| α-helix | 254-257 | 4 | |
| α-helix | 262-270 | 9 | |
| α-helix | 280-300 | 21 | |
| α-helix | 303-319 | 17 | |
| α-helix | 330-343 | 14 | |
| α-helix | 376-378 | 3 | |
| α-helix | 379-397 | 19 | |
| β-strand | 407-411 | 5 | 4 |
| α-helix | 414-426 | 13 | |
| α-helix | 428-439 | 12 | |
| α-helix | 445-455 | 11 | |
| β-strand | 544-546 | 3 | 1 |
| β-strand | 552-556 | 5 | 4 |
| α-helix | 563-565 | 3 | |
| α-helix | 566-572 | 7 | |
| β-strand | 577-580 | 4 | 4 |
| α-helix | 585-597 | 13 | |
| β-strand | 604-611 | 8 | 4 |
| α-helix | 614-640 | 27 | |
| β-strand | 683-687 | 5 | 6 |
| α-helix | 688-691 | 4 | |
| α-helix | 695-701 | 7 | |
| β-strand | 705-709 | 5 | 6 |
| β-strand | 716-717 | 2 | 6 |
| β-strand | 723-728 | 6 | 6 |
| α-helix | 729-738 | 10 | |
| α-helix | 740-751 | 12 | |
| β-strand | 755-760 | 6 | 6 |
| α-helix | 784-794 | 11 | |
| β-strand | 799-803 | 5 | 6 |
| α-helix | 806-816 | 11 | |
| α-helix | 821-822 | 2 | |
| α-helix | 829-831 | 3 | |
| α-helix | 846-854 | 9 | |
| α-helix | 861-869 | 9 | |
| α-helix | 876-878 | 3 | |
| α-helix | 881-888 | 8 | |
| α-helix | 892-901 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 101-103 | 3 | 7 |
| α-helix | 105-107 | 3 | |
| α-helix | 111-114 | 4 | |
| β-strand | 121-122 | 2 | 7 |
| β-strand | 130-131 | 2 | 7 |
| β-strand | 136-142 | 7 | 7 |
| α-helix | 143-148 | 6 | |
| α-helix | 152-160 | 9 | |
| β-strand | 166-172 | 7 | 7 |
| α-helix | 179-192 | 14 | |
| β-strand | 195-199 | 5 | 7 |
| α-helix | 202-214 | 13 | |
| α-helix | 220-222 | 3 | |
| α-helix | 231-240 | 10 | |
| α-helix | 247-257 | 11 | |
| α-helix | 260-265 | 6 | |
| α-helix | 268-273 | 6 | |
| α-helix | 278-289 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 7-10 | 4 | 1 |
| β-strand | 13-16 | 4 | 1 |
| β-strand | 17-21 | 5 | 2 |
| α-helix | 22-23 | 2 | |
| α-helix | 30-32 | 3 | |
| α-helix | 35-44 | 10 | |
| α-helix | 46-61 | 16 | |
| β-strand | 76-78 | 3 | 2 |
| β-strand | 83 | 1 | 3 |
| β-strand | 85-91 | 7 | 2 |
| β-strand | 97-100 | 4 | 4 |
| β-strand | 105-107 | 3 | 4 |
| β-strand | 108-109 | 2 | 1 |
| α-helix | 110 | 1 | |
| β-strand | 112-118 | 7 | 2 |
| β-strand | 120 | 1 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 529-532 | 4 | |
| α-helix | 533-535 | 3 | |
| α-helix | 542-545 | 4 | |
| α-helix | 548-550 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein SLX4IP | C | protein | 408 | Homo sapiens | Q5VYV7 (AlphaFold model) |
| DNA repair endonuclease XPF | A | protein | 935 | Homo sapiens | Q92889 (AlphaFold model) |
| DNA excision repair protein ERCC-1 | B | protein | 297 | Homo sapiens | P07992 (AlphaFold model) |
| Structure-specific endonuclease subunit SLX4 | D | protein | 271 | Homo sapiens | Q8IY92 (AlphaFold model) |
>9QED_1 Protein SLX4IP (chains C) MASKKFAVKCGNFAVLVDLHILPQGSNKDTSWFSEQKKEEVCLLLKETIDSRVQEYLEVR KQHRPSNAEFTRSNPLSLKGYGFQITAYFLKRGIRLRCIRSTQNAELCVFPDRFVVCVSQ LAFSRDLLASQNEDLTERVLHGVSDYFAECAESSLPPSAKLRRNALKEIVKRTETKSSVT SKSQTRRDTVETSSDSVIAEIARRRNDGQASSSPPSESMGQAKDSIKAAESHWGLPVQKL EKVNQTQPEDTSGQQKPHPGERLKTGLLSRSPVCSCESASPCPKQSPRVAKTQQKRRNCS SAEDFDHHGRVSLGSDRLVPREIIVEKSKAVRVLPASELSDPGLLLKQDLAKTTSKEELH VLESLSSRHLMKNNPGQAQQTGLATNTERLSTIQNSPTKKRKKYERGH
>9QED_2 DNA repair endonuclease XPF (chains A) MGSSHHHHHHENLYFQSNAMESGQPARRIAMAPLLEYERQLVLELLDTDGLVVCARGLGA DRLLYHFLQLHCHPACLVLVLNTQPAEEEYFINQLKIEGVEHLPRRVTNEITSNSRYEVY TQGGVIFATSRILVVDFLTDRIPSDLITGILVYRAHRIIESCQEAFILRLFRQKNKRGFI KAFTDNAVAFDTGFCHVERVMRNLFVRKLYLWPRFHVAVNSFLEQHKPEVVEIHVSMTPT MLAIQTAILDILNACLKELKCHNPSLEVEDLSLENAIGKPFDKTIRHYLDPLWHQLGAKT KSLVQDLKILRTLLQYLSQYDCVTFLNLLESLRATEKAFGQNSGWLFLDSSTSMFINARA RVYHLPDAKMSKKEKISEKMEIKEGEETKKELVLESNPKWEALTEVLKEIEAENKESEAL GGPGQVLICASDDRTCSQLRDYITLGAEAFLLRLYRKTFEKDSKAEEVWMKFRKEDSSKR IRKSHKRPKDPQNKERASTKERTLKKKKRKLTLTQMVGKPEELEEEGDVEEGYRREISSS PESCPEEIKHEEFDVNLSSDAAFGILKEPLTIIHPLLGCSDPYALTRVLHEVEPRYVVLY DAELTFVRQLEIYRASRPGKPLRVYFLIYGGSTEEQRYLTALRKEKEAFEKLIREKASMV VPEEREGRDETNLDLVRGTASADVSTDTRKAGGQEQNGTQQSIVVDMREFRSELPSLIHR RGIDIEPVTLEVGDYILTPEMCVERKSISDLIGSLNNGRLYSQCISMSRYYKRPVLLIEF DPSKPFSLTSRGALFQEISSNDISSKLTLLTLHFPRLRILWCPSPHATAELFEELKQSKP QPDAATALAITADSETLPESEKYNPGPQDFLLKMPGVNAKNCRSLMHHVKNIAELAALSQ DELTSILGNAANAKQLYDFIHTSFAEVVSKGKGKK
>9QED_3 DNA excision repair protein ERCC-1 (chains B) MDPGKDKEGVPQPSGPPARKKFVIPLDEDEVPPGVAKPLFRSTQSLPTVDTSAQAAPQTY AEYAISQPLEGAGATCPTGSEPLAGETPNQALKPGAKSNSIIVSPRQRGNPVLKFVRNVP WEFGDVIPDYVLGQSTCALFLSLRYHNLHPDYIHGRLQSLGKNFALRVLLVQVDVKDPQQ ALKELAKMCILADCTLILAWSPEEAGRYLETYKAYEQKPADLLMEKLEQDFVSRVTECLT TVKSVNKTDSQTLLTTFGSLEQLIAASREDLALCPGLGPQKARRLFDVLHEPFLKVP
>9QED_4 Structure-specific endonuclease subunit SLX4 (chains D) MASWSHPQFEKGGGSGGGSGGGSWSHPQFEKSGGGSENLYFQSNAVPQIPECPICGKPFL TLKSRTSHLKQCAVKMEVGPQLLLQAVRLQTAQPEGSSSPPMFSFSDHSRGLKRRGPTSK KEPRKRRKVDEAPSEDLLVAMALSRSEMEPGAAVPALRLESAFSERIRPEAENKSRKKKP PVSPPLLLVQDSETTGRQIEDRVALLLSEEVELSSTPPLPASRILKEGWERAGQCPPPPE RKQSFLWEGSALTGAWAMEDFYTARLVPPLV
Molecular basis of XPF-ERCC1 targeting to SLX4-dependent DNA repair pathways. Feng, J., Martin, P.R., Kowalski, S. et al. Nat Commun (2025) 17:522-522. DOI 10.1038/s41467-025-67216-3 · PubMed
Other PDB entries of the same protein (UniProt Q5VYV7 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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