Structure of neurodevelopmental mutant AGO1 F180del in complex with guide RNA. Determined by electron microscopy at 3.3 Å resolution. Released 5 Nov 2025.
Explore 9Q3F in 3D Show helices and sheets RCSB PDB PDBe
9Q3F contains 29 α-helices and 52 β-strands across 1 chain. 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 | 34-35 | 2 | 1 |
| β-strand | 38-40 | 3 | 2 |
| β-strand | 42-46 | 5 | 3 |
| β-strand | 51-52 | 2 | 4 |
| β-strand | 53-56 | 4 | 5 |
| α-helix | 66-79 | 14 | |
| α-helix | 81-84 | 4 | |
| β-strand | 91-92 | 2 | 5 |
| β-strand | 97-100 | 4 | 5 |
| β-strand | 112-113 | 2 | 6 |
| β-strand | 128-129 | 2 | 6 |
| β-strand | 136-137 | 2 | 4 |
| α-helix | 139-146 | 8 | |
| α-helix | 151-152 | 2 | |
| α-helix | 154-163 | 10 | |
| α-helix | 166-171 | 6 | |
| β-strand | 175 | 1 | 3 |
| β-strand | 178 | 1 | 3 |
| β-strand | 188 | 1 | 3 |
| β-strand | 194-202 | 9 | 3 |
| β-strand | 205 | 1 | 3 |
| β-strand | 210-221 | 12 | 3 |
| α-helix | 227-235 | 9 | |
| α-helix | 252-259 | 8 | |
| β-strand | 264 | 1 | 7 |
| β-strand | 280-281 | 2 | 8 |
| α-helix | 305-313 | 9 | |
| β-strand | 324-327 | 4 | 8 |
| β-strand | 334-337 | 4 | 8 |
| β-strand | 343 | 1 | 7 |
| β-strand | 348 | 1 | 3 |
| α-helix | 355-365 | 11 | |
| α-helix | 369-383 | 15 | |
| α-helix | 385-387 | 3 | |
| α-helix | 389-394 | 6 | |
| β-strand | 397-398 | 2 | 3 |
| α-helix | 402 | 1 | |
| β-strand | 403-405 | 3 | 2 |
| β-strand | 408-409 | 2 | 1 |
| α-helix | 410-412 | 3 | |
| β-strand | 415-416 | 2 | 9 |
| β-strand | 418 | 1 | 10 |
| β-strand | 425 | 1 | 9 |
| β-strand | 428 | 1 | 11 |
| β-strand | 431 | 1 | 11 |
| β-strand | 438 | 1 | 10 |
| β-strand | 441 | 1 | 12 |
| β-strand | 449-451 | 3 | 13 |
| α-helix | 462-477 | 16 | |
| β-strand | 489-490 | 2 | 13 |
| α-helix | 499-508 | 10 | |
| β-strand | 515-519 | 5 | 13 |
| α-helix | 525-531 | 7 | |
| α-helix | 532-536 | 5 | |
| β-strand | 541-545 | 5 | 13 |
| α-helix | 547-550 | 4 | |
| α-helix | 554-568 | 15 | |
| β-strand | 571 | 1 | 12 |
| β-strand | 574-575 | 2 | 9 |
| α-helix | 582-585 | 4 | |
| β-strand | 588-596 | 9 | 14 |
| α-helix | 605-606 | 2 | |
| β-strand | 607-614 | 8 | 14 |
| β-strand | 622-624 | 3 | 14 |
| β-strand | 627-629 | 3 | 14 |
| α-helix | 639-654 | 16 | |
| β-strand | 660-666 | 7 | 14 |
| α-helix | 673-691 | 19 | |
| β-strand | 698-705 | 8 | 14 |
| β-strand | 712-714 | 3 | 2 |
| β-strand | 721 | 1 | 15 |
| β-strand | 726 | 1 | 15 |
| β-strand | 731-732 | 2 | 1 |
| β-strand | 744-747 | 4 | 14 |
| β-strand | 748 | 1 | 1 |
| β-strand | 760-766 | 7 | 14 |
| α-helix | 773-783 | 11 | |
| β-strand | 792 | 1 | 11 |
| α-helix | 798-814 | 17 | |
| α-helix | 836-843 | 8 | |
| α-helix | 847-849 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein argonaute-1 | A | protein | 870 | Homo sapiens | Q9UL18 (AlphaFold model) |
| Non-homogenous guide RNA | B | RNA | 8 | Trichoplusia ni |
>9Q3F_1 Protein argonaute-1 (chains A) GAMGSMDYKDDDDKMEAGPSGAAAGAYLPPLQQVFQAPRRPGIGTVGKPIKLLANYFEVD IPKIDVYHYEVDIKPDKCPRRVNREVVEYMVQHFKPQIFGDRKPVYDGKKNIYTVTALPI GNERVDFEVTIPGEGKDRIFKVSIKWLAIVSWRMLHEALVSGQIPVPLESVQALDVAMRH LASMRYTPVGRSFSPPEGYYHPLGGGREVWFGFHQSVRPAMWKMMLNIDVSATAFYKAQP VIEFMCEVLDIRNIDEQPKPLTDSQRVRFTKEIKGLKVEVTHCGQMKRKYRVCNVTRRPA SHQTFPLQLESGQTVECTVAQYFKQKYNLQLKYPHLPCLQVGQEQKHTYLPLEVCNIVAG QRCIKKLTDNQTSTMIKATARSAPDRQEEISRLMKNASYNLDPYIQEFGIKVKDDMTEVT GRVLPAPILQYGGRNRAIATPNQGVWDMRGKQFYNGIEIKVWAIACFAPQKQCREEVLKN FTDQLRKISKDAGMPIQGQPCFCKYAQGADSVEPMFRHLKNTYSGLQLIIVILPGKTPVY AEVKRVGDTLLGMATQCVQVKNVVKTSPQTLSNLCLKINVKLGGINNILVPHQRSAVFQQ PVIFLGADVTHPPAGDGKKPSITAVVGSMDAHPSRYCATVRVQRPRQEIIEDLSYMVREL LIQFYKSTRFKPTRIIFYRDGVPEGQLPQILHYELLAIRDACIKLEKDYQPGITYIVVQK RHHTRLFCADKNERIGKSGNIPAGTTVDTNITHPFEFDFYLCSHAGIQGTSRPSHYYVLW DDNRFTADELQILTYQLCHTYVRCTRSVSIPAPAYYARLVAFRARYHLVDKEHDSGEGSH ISGQSNGRDPQALAKAVQVHQDTLRTMYFA
>9Q3F_2 Non-homogenous guide RNA (chains B) AAAAAAAA
Neurodevelopmental disorder-linked Argonaute mutations permit delayed RISC formation and unusual shortening of miRNAs by 3'→5' trimming. Savidge, A., Zhang, H., Annasaheb Adhav, V. et al. Proc Natl Acad Sci U S A (2025) 122:e2524644122-e2524644122. DOI 10.1073/pnas.2524644122 · PubMed
Other PDB entries of the same protein (UniProt Q9UL18 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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