9Q3E: RotavirusA NSP1-ELOB-ELOC-CUL3
Cryo-EM structure of RotavirusA NSP1-ELOB-ELOC-CUL3. Determined by electron microscopy at 3.3 Å resolution. Released 8 Jul 2026.
- Method
- Electron microscopy
- Resolution
- 3.3 Å
- Organisms
- Rotavirus A, Homo sapiens
- Chains
- 4
- Atoms
- 6,028
- Mol. weight
- 172.91 kDa
- Ligands
- ZN
- Released
- 8 Jul 2026
Explore 9Q3E in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9Q3E contains 50 α-helices and 29 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.
Chain B: 6 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-9 | 8 | 7 |
| β-strand | 12-19 | 8 | 7 |
| β-strand | 23 | 1 | 8 |
| α-helix | 24-35 | 12 | |
| α-helix | 39-41 | 3 | |
| β-strand | 42-46 | 5 | 7 |
| β-strand | 49-50 | 2 | 7 |
| α-helix | 51-52 | 2 | |
| β-strand | 56 | 1 | 8 |
| β-strand | 68 | 1 | 9 |
| β-strand | 71 | 1 | 9 |
| α-helix | 72 | 1 | |
| β-strand | 73-79 | 7 | 7 |
| β-strand | 80 | 1 | 10 |
| β-strand | 85 | 1 | 10 |
| α-helix | 86-88 | 3 | |
| α-helix | 90-95 | 6 | |
Chain C: 7 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 18-22 | 5 | 7 |
| β-strand | 28-32 | 5 | 7 |
| α-helix | 33-36 | 4 | |
| α-helix | 40-45 | 6 | |
| α-helix | 53-57 | 5 | |
| β-strand | 59-61 | 3 | 7 |
| α-helix | 67-83 | 17 | |
| α-helix | 91-94 | 4 | |
| α-helix | 97-99 | 3 | |
| α-helix | 100-110 | 11 | |
Chain L: 10 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 28-45 | 18 | |
| α-helix | 54-66 | 13 | |
| α-helix | 70-84 | 15 | |
| α-helix | 85-90 | 6 | |
| α-helix | 91-94 | 4 | |
| α-helix | 101-122 | 22 | |
| α-helix | 124-134 | 11 | |
| α-helix | 139-147 | 9 | |
| α-helix | 148-152 | 5 | |
| α-helix | 155-167 | 13 | |
Chain N: 27 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-11 | 9 | |
| α-helix | 16-21 | 6 | |
| α-helix | 34-36 | 3 | |
| β-strand | 39-42 | 4 | 1 |
| β-strand | 47-50 | 4 | 1 |
| β-strand | 51-53 | 3 | 2 |
| β-strand | 59 | 1 | 3 |
| β-strand | 60-63 | 4 | 2 |
| α-helix | 80-84 | 5 | |
| β-strand | 85-87 | 3 | 4 |
| α-helix | 92-105 | 14 | |
| α-helix | 110-115 | 6 | |
| α-helix | 136-138 | 3 | |
| β-strand | 144-150 | 7 | 4 |
| β-strand | 153-158 | 6 | 4 |
| α-helix | 172 | 1 | |
| β-strand | 173-176 | 4 | 4 |
| α-helix | 183-194 | 12 | |
| α-helix | 199-213 | 15 | |
| α-helix | 217-223 | 7 | |
| α-helix | 225-227 | 3 | |
| β-strand | 228 | 1 | 3 |
| α-helix | 230-234 | 5 | |
| β-strand | 242-249 | 8 | 5 |
| α-helix | 256-264 | 9 | |
| α-helix | 266-273 | 8 | |
| β-strand | 277-284 | 8 | 5 |
| α-helix | 288-299 | 12 | |
| α-helix | 304-308 | 5 | |
| α-helix | 315-317 | 3 | |
| α-helix | 325-327 | 3 | |
| α-helix | 331-333 | 3 | |
| α-helix | 336-356 | 21 | |
| α-helix | 369-372 | 4 | |
| α-helix | 381-394 | 14 | |
| β-strand | 398 | 1 | 6 |
| β-strand | 405-407 | 3 | 6 |
| α-helix | 414-423 | 10 | |
| β-strand | 430-432 | 3 | 6 |
| α-helix | 433-445 | 13 | |
| α-helix | 458-460 | 3 | |
| α-helix | 463-469 | 7 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Non-structural protein 1 | N | protein | 486 | Rotavirus A | B3SRV2 |
| Elongin-B | B | protein | 118 | Homo sapiens | Q15370 (AlphaFold model) |
| Elongin-C | C | protein | 112 | Homo sapiens | Q15369 (AlphaFold model) |
| Cullin-3 | L | protein | 771 | Homo sapiens | Q13618 (AlphaFold model) |
Sequence of entity 1 (N), FASTA
>9Q3E_1 Non-structural protein 1 (chains N)
MATFKDACYHYKRINKLNHTVLKLGVNDTWRSSPPTKYKGWCLDCCQHTDLTYCRGCTMY
HVCQWCSQYGRCFLDNEPHLLRMRTFKNEVTKDDLKNLIDMYEILFPMNQKIVCRFINNT
RQHKCRNECMTQWYNHLLLPITLQSMSIELDGDVYYVFGYYDNMNSINQTPFSFTNLVDI
YDKLLLDDVNFARMSFLPASLQQEYALRYFSKSRFISEQRKCVNDSHFSINVLENLHNPS
FKVQITRNCSELSFDWNEACKLVKNVSAYFDMLKTSHIEFYSVSTRCRIFTQCKLKMASK
LIKPNYITSNHKTLATEVHNCKWCSVNNSYTVWNDFRIKKIYDNIFNFLRALVKSNVNIG
HCSSQEKIYEYVEDVLNVCDDERWKTSIMEIFNCLEPVELDDVKYVLFNHEINWDVINVL
VHSIGKVPQILTLENVITIMQSIIYEWFDIRYMRNTPMVTFTIDKLRRLHTGLKTVEYDS
GISDIE
Sequence of entity 2 (B), FASTA
>9Q3E_2 Elongin-B (chains B)
MDVFLMIRRHKTTIFTDAKESSTVFELKRIVEGILKRPPDEQRLYKDDQLLDDGKTLGEC
GFTSQTARPQAPATVGLAFRADDTFEALCIEPFSSPPELPDVMKPQDSGSSANEQAVQ
Sequence of entity 3 (C), FASTA
>9Q3E_3 Elongin-C (chains C)
MDGEEKTYGGCEGPDAMYVKLISSDGHEFIVKREHALTSGTIKAMLSGPGQFAENETNEV
NFREIPSHVLSKVCMYFTYKVRYTNSSTEIPEFPIAPEIALELLMAANFLDC
Sequence of entity 4 (L), FASTA
>9Q3E_4 Cullin-3 (chains L)
GGRMSNLSKGTGSRKDTKMRIRAFPMTMDEKYVNSIWDLLKNAIQEIQRKNNSGLSFEEL
YRNAYTMVLHKHGEKLYTGLREVVTEHLINKVREDVLNSLNNNFLQTLNQAWNDHQTAMV
MIRDILMYMDRVYVQQNNVENVYNLGLIIFRDQVVRYGCIRDHLRQTLLDMIARERKGEV
VDRGAIRNACQMLMILGLEGRSVYEEDFEAPFLEMSAEFFQMESQKFLAENSASVYIKKV
EARINEEIERVMHCLDKSTEEPIVKVVERELISKHMKTIVEMENSGLVHMLKNGKTEDLG
CMYKLFSRVPNGLKTMCECMSSYLREQGKALVSEEGEGKNPVDYIQGLLDLKSRFDRFLL
ESFNNDRLFKQTIAGDFEYFLNLNSRSPEYLSLFIDDKLKKGVKGLTEQEVETILDKAMV
LFRFMQEKDVFERYYKQHLARRLLTNKSVSDDSEKNMISKLKTECGCQFTSKLEGMFRDM
SISNTTMDEFRQHLQATGVSLGGVDLTVRVLTTGYWPTQSATPKCNIPPAPRHAFEIFRR
FYLAKHSGRQLTLQHHMGSADLNATFYGPVKKEDGSEVGVGGAQVTGSNTRKHILQVSTF
QMTILMLFNNREKYTFEEIQQETDIPERELVRALQSLACGKPTQRVLTKEPKSKEIENGH
IFTVNDQFTSKLHRVKIQTVAAKQGESDPERKETRQKVDDDRKHEIEAAIVRIMKSRKKM
QHNVLVAEVTQQLKARFLPSPVVIKKRIEGLIEREYLARTPEDRKVYTYVA
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| ZN | Zinc ion | Zn | 3 |
Primary citation
Virome-wide ubiquitin ligase discovery reveals diverse mechanisms of immune evasion. Glassman, C.R., Baek, K., Hou, G. et al. Science (2026) 393:eaec6299-eaec6299. DOI 10.1126/science.aec6299 · PubMed
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