9V43: DICER/26S-UG complex in dicing state

Cryo-EM structure of DICER/26S-UG complex in dicing state. Determined by electron microscopy at 3.34 Å resolution. Released 11 Mar 2026.

Method
Electron microscopy
Resolution
3.34 Å
Organisms
synthetic construct, Homo sapiens
Chains
2
Atoms
6,889
Mol. weight
238.61 kDa
Ligands
CA
Released
11 Mar 2026

Explore 9V43 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9V43 contains 28 α-helices and 15 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.

Chain B: 28 helices, 15 β-strands

ElementResiduesLengthSheet
α-helix750-7523
β-strand769-77021
β-strand773-77642
α-helix792-7943
α-helix795-7973
β-strand801-80661
β-strand816-82162
β-strand823-82972
β-strand83311
α-helix840-85415
β-strand877-88151
β-strand882-88323
β-strand890-89123
α-helix896-9038
β-strand94614
α-helix970-9756
α-helix986-9872
β-strand99114
α-helix1018-102811
α-helix1035-10373
α-helix1045-107329
α-helix1294-13018
α-helix1315-133420
α-helix1340-136324
α-helix1365-13684
α-helix1376-13794
α-helix1556-158530
α-helix1663-167311
α-helix1681-16877
β-strand168815
α-helix1702-172221
α-helix1729-174012
α-helix1742-175110
α-helix1755-17573
β-strand175915
α-helix1763-177513
α-helix1806-182217
α-helix1828-18347
α-helix1839-18479
α-helix1853-18608
β-strand188416
β-strand188816
α-helix1898-191114

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
RNA (64-mer)ARNA64synthetic construct
Endoribonuclease DicerBprotein1909Homo sapiensQ9UPY3 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>9V43_1 RNA (64-MER) (chains A)
UGGAUAUUUCUCGCAGAUCUCAUGUGAAAAAAAAAACACAUGACAUCUGUGAGAAAUAUU
CGUA
Sequence of entity 2 (B), FASTA
>9V43_2 Endoribonuclease Dicer (chains B)
MGHHHHHHHHHHPFFGLPWQQEAIHDNIYTPRKYQVELLEAALDHNTIVCLNTGSGKTFI
AVLLTKELSYQIRGDFSRNGKRTVFLVNSANQVAQQVSAVRTHSDLKVGEYSNLEVNASW
TKERWNQEFTKHQVLIMTCYVALNVLKNGYLSLSDINLLVFDECHLAILDHPYREIMKLC
ENCPSCPRILGLTASILNGKCDPEELEEKIQKLEKILKSNAETATDLVVLDRYTSQPCEI
VVDCGPFTDRSGLYERLLMELEEALNFINDCNISVHSKERDSTLISKQILSDCRAVLVVL
GPWCADKVAGMMVRELQKYIKHEQEELHRKFLLFTDTFLRKIHALCEEHFSPASLDLKFV
TPKVIKLLEILRKYKPYERQQFESVEWYNNRNQDNYVSWSDSEDDDEDEEIEEKEKPETN
FPSPFTNILCGIIFVERRYTAVVLNRLIKEAGKQDPELAYISSNFITGHGIGKNQPRNKQ
MEAEFRKQEEVLRKFRAHETNLLIATSIVEEGVDIPKCNLVVRFDLPTEYRSYVQSKGRA
RAPISNYIMLADTDKIKSFEEDLKTYKAIEKILRNKCSKSVDTGETDIDPVMDDDDVFPP
YVLRPDDGGPRVTINTAIGHINRYCARLPSDPFTHLAPKCRTRELPDGTFYSTLYLPINS
PLRASIVGPPMSCVRLAERVVALICCEKLHKIGELDDHLMPVGKETVKYEEELDLHDEEE
TSVPGRPGSTKRRQCYPKAIPECLRDSYPRPDQPCYLYVIGMVLTTPLPDELNFRRRKLY
PPEDTTRCFGILTAKPIPQIPHFPVYTRSGEVTISIELKKSGFMLSLQMLELITRLHQYI
FSHILRLEKPALEFKPTDADSAYCVLPLNVVNDSSTLDIDFKFMEDIEKSEARIGIPSTK
YTKETPFVFKLEDYQDAVIIPRYRNFDQPHRFYVADVYTDLTPLSKFPSPEYETFAEYYK
TKYNLDLTNLNQPLLDVDHTSSRLNLLTPRHLNQKGKALPLSSAEKRKAKWESLQNKQIL
VPELCAIHPIPASLWRKAVCLPSILYRLHCLLTAEELRAQTASDAGVGVRSLPADFRYPN
LDFGWKKSIDSKSFISISNSSSAENDNYCKHSTIVPENAAHQGANRTSSLENHDQMSVNC
RTLLSESPGKLHVEVSADLTAINGLSYNQNLANGSYDLANRDFCQGNQLNYYKQEIPVQP
TTSYSIQNLYSYENQPQPSDECTLLSNKYLDGNANKSTSDGSPVMAVMPGTTDTIQVLKG
RMDSEQSPSIGYSSRTLGPNPGLILQALTLSNASDGFNLERLEMLGDSFLKHAITTYLFC
TYPDAHEGRLSYMRSKKVSNCNLYRLGKKKGLPSRMVVSIFDPPVNWLPPGYVVNQDKSN
TDKWEKDEMTKDCMLANGKLDEDYEEEDEEEESLMWRAPKEEADYEDDFLEYDQEHIRFI
DNMLMGSGAFVKKISLSPFSTTDSAYEWKMPKKSSLGSMPFSSDFEDFDYSSWDAMCYLD
PSKAVEEDDFVVGFWNPSEENCGVDTGKQSISYDLHTEQCIADKSIADCVEALLGCYLTS
CGERAAQLFLCSLGLKVLPVIKRTDREKALCPTRENFNSQQKNLSVSCAAASVASSRSSV
LKDSEYGCLKIPPRCMFDHPDADKTLNHLISGFENFEKKINYRFKNKAYLLQAFTHASYH
YNTITDCYQRLEFLGDAILDYLITKHLYEDPRQHSPGVLTDLRSALVNNTIFASLAVKYD
YHKYFKAVSPELFHVIDDFVQFQLEKNEMQGMDSELRRSEEDEEKEEDIEVPKAMGDIFE
SLAGAIYMDSGMSLETVWQVYYPMMRPLIEKFSANVPRSPVRELLEMEPETAKFSPAERT
YDGKVRVTVEVVGKGKFKGVGRSYRIAKSAAARRALRSLKANQPQVPNS

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa2

Primary citation

DICER cleavage fidelity is governed by 5'-end binding pockets. Ngo, M.K., Le, C.T., Nguyen, T.A. Nature (2026) 653:611-620. DOI 10.1038/s41586-026-10211-5 · PubMed

Other PDB entries of the same protein (UniProt Q9UPY3 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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