Cryo-EM structure of human AGO1 in complex with guide RNA. Determined by electron microscopy at 3.3 Å resolution. Released 29 Oct 2025.
Explore 9Q3G in 3D Show helices and sheets RCSB PDB PDBe
9Q3G contains 33 α-helices and 40 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 |
|---|---|---|---|
| α-helix | 23-26 | 4 | |
| β-strand | 34-40 | 7 | 1 |
| β-strand | 42-46 | 5 | 2 |
| β-strand | 51-56 | 6 | 3 |
| β-strand | 57-59 | 3 | 4 |
| α-helix | 66-79 | 14 | |
| α-helix | 81-85 | 5 | |
| β-strand | 91-92 | 2 | 3 |
| β-strand | 97-100 | 4 | 3 |
| β-strand | 128-130 | 3 | 4 |
| β-strand | 134-137 | 4 | 3 |
| α-helix | 138-147 | 10 | |
| α-helix | 155-163 | 9 | |
| α-helix | 166-171 | 6 | |
| β-strand | 173-175 | 3 | 2 |
| β-strand | 178-181 | 4 | 2 |
| β-strand | 194-206 | 13 | 2 |
| β-strand | 211-223 | 13 | 2 |
| α-helix | 228-236 | 9 | |
| α-helix | 250-259 | 10 | |
| α-helix | 307-313 | 7 | |
| α-helix | 323-325 | 3 | |
| α-helix | 356-366 | 11 | |
| α-helix | 370-384 | 15 | |
| α-helix | 386-388 | 3 | |
| α-helix | 390-395 | 6 | |
| β-strand | 398-399 | 2 | 2 |
| α-helix | 403 | 1 | |
| β-strand | 404-410 | 7 | 1 |
| α-helix | 411-413 | 3 | |
| β-strand | 416-417 | 2 | 5 |
| β-strand | 419 | 1 | 6 |
| β-strand | 425-426 | 2 | 5 |
| β-strand | 432 | 1 | 7 |
| β-strand | 439 | 1 | 6 |
| β-strand | 442 | 1 | 8 |
| β-strand | 446 | 1 | 9 |
| β-strand | 450-453 | 4 | 10 |
| α-helix | 457-459 | 3 | |
| α-helix | 462-479 | 18 | |
| β-strand | 483 | 1 | 9 |
| β-strand | 490-492 | 3 | 10 |
| α-helix | 496-498 | 3 | |
| α-helix | 499-509 | 11 | |
| β-strand | 516-520 | 5 | 10 |
| α-helix | 526-533 | 8 | |
| α-helix | 534-538 | 5 | |
| β-strand | 542-546 | 5 | 10 |
| α-helix | 548-551 | 4 | |
| α-helix | 555-569 | 15 | |
| β-strand | 572 | 1 | 8 |
| β-strand | 575-576 | 2 | 5 |
| α-helix | 578-580 | 3 | |
| α-helix | 584-586 | 3 | |
| β-strand | 590-597 | 8 | 1 |
| α-helix | 599-600 | 2 | |
| β-strand | 608-615 | 8 | 1 |
| β-strand | 623-630 | 8 | 1 |
| α-helix | 640-655 | 16 | |
| β-strand | 661-666 | 6 | 1 |
| α-helix | 674-692 | 19 | |
| β-strand | 699-706 | 8 | 1 |
| β-strand | 713-715 | 3 | 1 |
| β-strand | 722 | 1 | 11 |
| β-strand | 727 | 1 | 11 |
| α-helix | 728-729 | 2 | |
| β-strand | 732-734 | 3 | 1 |
| β-strand | 745-749 | 5 | 1 |
| β-strand | 761-767 | 7 | 1 |
| α-helix | 774-784 | 11 | |
| β-strand | 793 | 1 | 7 |
| α-helix | 799-814 | 16 | |
| α-helix | 836-844 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein argonaute-1 | A | protein | 871 | Homo sapiens | Q9UL18 (AlphaFold model) |
| Non-homogenous guide RNA | B | RNA | 8 | Trichoplusia ni |
>9Q3G_1 Protein argonaute-1 (chains A) GAMGSMDYKDDDDKMEAGPSGAAAGAYLPPLQQVFQAPRRPGIGTVGKPIKLLANYFEVD IPKIDVYHYEVDIKPDKCPRRVNREVVEYMVQHFKPQIFGDRKPVYDGKKNIYTVTALPI GNERVDFEVTIPGEGKDRIFKVSIKWLAIVSWRMLHEALVSGQIPVPLESVQALDVAMRH LASMRYTPVGRSFFSPPEGYYHPLGGGREVWFGFHQSVRPAMWKMMLNIDVSATAFYKAQ PVIEFMCEVLDIRNIDEQPKPLTDSQRVRFTKEIKGLKVEVTHCGQMKRKYRVCNVTRRP ASHQTFPLQLESGQTVECTVAQYFKQKYNLQLKYPHLPCLQVGQEQKHTYLPLEVCNIVA GQRCIKKLTDNQTSTMIKATARSAPDRQEEISRLMKNASYNLDPYIQEFGIKVKDDMTEV TGRVLPAPILQYGGRNRAIATPNQGVWDMRGKQFYNGIEIKVWAIACFAPQKQCREEVLK NFTDQLRKISKDAGMPIQGQPCFCKYAQGADSVEPMFRHLKNTYSGLQLIIVILPGKTPV YAEVKRVGDTLLGMATQCVQVKNVVKTSPQTLSNLCLKINVKLGGINNILVPHQRSAVFQ QPVIFLGADVTHPPAGDGKKPSITAVVGSMDAHPSRYCATVRVQRPRQEIIEDLSYMVRE LLIQFYKSTRFKPTRIIFYRDGVPEGQLPQILHYELLAIRDACIKLEKDYQPGITYIVVQ KRHHTRLFCADKNERIGKSGNIPAGTTVDTNITHPFEFDFYLCSHAGIQGTSRPSHYYVL WDDNRFTADELQILTYQLCHTYVRCTRSVSIPAPAYYARLVAFRARYHLVDKEHDSGEGS HISGQSNGRDPQALAKAVQVHQDTLRTMYFA
>9Q3G_2 Non-homogenous guide RNA (chains B) NNNNNNNN
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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