29HI: CUL1-RBX1-SKP1-FBXO22 SCF ubiquition ligase
Cryo-EM structure of the CUL1-RBX1-SKP1-FBXO22 SCF ubiquition ligase in complex with NSD2 via UNC10415667. Determined by electron microscopy at 5.9 Å resolution. Released 6 May 2026.
- Method
- Electron microscopy
- Resolution
- 5.9 Å
- Organism
- Homo sapiens
- Chains
- 5
- Atoms
- 12,383
- Mol. weight
- 318.48 kDa
- Ligands
- A1J21
- Released
- 6 May 2026
Explore 29HI in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
29HI contains 70 α-helices and 42 β-strands across 5 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 A: 14 helices, 17 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 17-25 | 9 | |
| α-helix | 27-35 | 9 | |
| α-helix | 39-46 | 8 | |
| α-helix | 50-62 | 13 | |
| β-strand | 67-71 | 5 | 1 |
| α-helix | 83-94 | 12 | |
| α-helix | 98-99 | 2 | |
| β-strand | 101-107 | 7 | 1 |
| α-helix | 108-111 | 4 | |
| α-helix | 130-138 | 9 | |
| β-strand | 144-150 | 7 | 1 |
| β-strand | 152-155 | 4 | 2 |
| β-strand | 166-168 | 3 | 2 |
| β-strand | 174-179 | 6 | 1 |
| β-strand | 186-194 | 9 | 3 |
| α-helix | 203-208 | 6 | |
| β-strand | 219-225 | 7 | 3 |
| α-helix | 232-243 | 12 | |
| β-strand | 249-254 | 6 | 3 |
| β-strand | 257-258 | 2 | 1 |
| α-helix | 267-268 | 2 | |
| β-strand | 273-281 | 9 | 3 |
| β-strand | 286-291 | 6 | 2 |
| α-helix | 299-311 | 13 | |
| β-strand | 319-325 | 7 | 2 |
| α-helix | 340-348 | 9 | |
| β-strand | 354-358 | 5 | 2 |
| β-strand | 363 | 1 | 3 |
| β-strand | 369 | 1 | 2 |
| α-helix | 383-385 | 3 | |
| β-strand | 392-398 | 7 | 2 |
Chain B: 9 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 213-217 | 5 | |
| β-strand | 225-228 | 4 | 4 |
| β-strand | 236-240 | 5 | 4 |
| α-helix | 255-257 | 3 | |
| β-strand | 261-266 | 6 | 4 |
| α-helix | 267 | 1 | |
| β-strand | 273-277 | 5 | 4 |
| α-helix | 278-280 | 3 | |
| β-strand | 281-283 | 3 | 4 |
| α-helix | 287-289 | 3 | |
| α-helix | 290-299 | 10 | |
| α-helix | 318-329 | 12 | |
| α-helix | 337-344 | 8 | |
| β-strand | 347-349 | 3 | 5 |
| β-strand | 352-354 | 3 | 5 |
| α-helix | 357-361 | 5 | |
Chain C: 10 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-8 | 6 | 6 |
| β-strand | 13-17 | 5 | 6 |
| α-helix | 18-23 | 6 | |
| α-helix | 25-34 | 10 | |
| α-helix | 43-44 | 2 | |
| β-strand | 45-47 | 3 | 6 |
| α-helix | 52-64 | 13 | |
| α-helix | 71-74 | 4 | |
| α-helix | 87-92 | 6 | |
| α-helix | 97-110 | 14 | |
| α-helix | 113-127 | 15 | |
| α-helix | 132-139 | 8 | |
| α-helix | 147-157 | 11 | |
Chain D: 34 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 17-34 | 18 | |
| α-helix | 39-54 | 16 | |
| α-helix | 86-108 | 23 | |
| α-helix | 112-150 | 39 | |
| α-helix | 159-166 | 8 | |
| α-helix | 167-172 | 6 | |
| α-helix | 173-192 | 20 | |
| α-helix | 198-210 | 13 | |
| α-helix | 226-254 | 29 | |
| α-helix | 257-278 | 22 | |
| α-helix | 281-313 | 33 | |
| α-helix | 316-327 | 12 | |
| α-helix | 330-332 | 3 | |
| α-helix | 333-361 | 29 | |
| α-helix | 363-381 | 19 | |
| α-helix | 382-386 | 5 | |
| α-helix | 389-403 | 15 | |
| α-helix | 407-412 | 6 | |
| α-helix | 417-430 | 14 | |
| β-strand | 431 | 1 | 7 |
| α-helix | 432-433 | 2 | |
| α-helix | 440-455 | 16 | |
| α-helix | 459-476 | 18 | |
| β-strand | 479 | 1 | 7 |
| α-helix | 482-496 | 15 | |
| α-helix | 498-528 | 31 | |
| β-strand | 537-541 | 5 | 8 |
| α-helix | 542-544 | 3 | |
| α-helix | 557-573 | 17 | |
| β-strand | 577-581 | 5 | 8 |
| α-helix | 583-585 | 3 | |
| β-strand | 587-591 | 5 | 9 |
| β-strand | 600-604 | 5 | 9 |
| α-helix | 605-616 | 12 | |
| β-strand | 619-621 | 3 | 10 |
| α-helix | 622-629 | 8 | |
| α-helix | 633-645 | 13 | |
| β-strand | 650 | 1 | 10 |
| α-helix | 653-655 | 3 | |
| β-strand | 668-670 | 3 | 10 |
| β-strand | 681-683 | 3 | 9 |
| α-helix | 689-721 | 33 | |
| β-strand | 724-726 | 3 | 11 |
| α-helix | 727-738 | 12 | |
| α-helix | 746-758 | 13 | |
| β-strand | 762-765 | 4 | 11 |
| β-strand | 771-774 | 4 | 11 |
Chain E: 3 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 26-28 | 3 | 9 |
| β-strand | 29-35 | 7 | 8 |
| α-helix | 43-45 | 3 | |
| α-helix | 54-60 | 7 | |
| α-helix | 81-88 | 8 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| F-box only protein 22 | A | protein | 403 | Homo sapiens | Q8NEZ5 (AlphaFold model) |
| Histone-lysine N-methyltransferase NSD2 | B | protein | 1365 | Homo sapiens | O96028 (AlphaFold model) |
| S-phase kinase-associated protein 1 | C | protein | 163 | Homo sapiens | P63208 (AlphaFold model) |
| Cullin-1 | D | protein | 776 | Homo sapiens | Q13616 (AlphaFold model) |
| E3 ubiquitin-protein ligase RBX1 | E | protein | 108 | Homo sapiens | P62877 |
Sequence of entity 1 (A), FASTA
>29HI_1 F-box only protein 22 (chains A)
MEPVGCCGECRGSSVDPRSTFVLSNLAEVVERVLTFLPAKALLRVACVCRLWRECVRRVL
RTHRSVTWISAGLAEAGHLEGHCLVRVVAEELENVRILPHTVLYMADSETFISLEECRGH
KRARKRTSMETALALEKLFPKQCQVLGIVTPGIVVTPMGSGSNRPQEIEIGESGFALLFP
QIEGIKIQPFHFIKDPKNLTLERHQLTEVGLLDNPELRVVLVFGYNCCKVGASNYLQQVV
STFSDMNIILAGGQVDNLSSLTSEKNPLDIDASGVVGLSFSGHRIQSATVLLNEDVSDEK
TAEAAMQRLKAANIPEHNTIGFMFACVGRGFQYYRAKGNVEADAFRKFFPSVPLFGFFGN
GEIGCDRIVTGNFILRKCNEVKDDDLFHSYTTIMALIHLGSSK
Sequence of entity 2 (B), FASTA
>29HI_2 Histone-lysine N-methyltransferase NSD2 (chains B)
MEFSIKQSPLSVQSVVKCIKMKQAPEILGSANGKTPSCEVNRECSVFLSKAQLSSSLQEG
VMQKFNGHDALPFIPADKLKDLTSRVFNGEPGAHDAKLRFESQEMKGIGTPPNTTPIKNG
SPEIKLKITKTYMNGKPLFESSICGDSAADVSQSEENGQKPENKARRNRKRSIKYDSLLE
QGLVEAALVSKISSPSDKKIPAKKESCPNTGRDKDHLLKYNVGDLVWSKVSGYPWWPCMV
SADPLLHSYTKLKGQKKSARQYHVQFFGDAPERAWIFEKSLVAFEGEGQFEKLCQESAKQ
APTKAEKIKLLKPISGKLRAQWEMGIVQAEEAASMSVEERKAKFTFLYVGDQLHLNPQVA
KEAGIAAESLGEMAESSGVSEEAAENPKSVREECIPMKRRRRAKLCSSAETLESHPDIGK
STPQKTAEADPRRGVGSPPGRKKTTVSMPRSRKGDAASQFLVFCQKHRDEVVAEHPDASG
EEIEELLRSQWSLLSEKQRARYNTKFALVAPVQAEEDSGNVNGKKRNHTKRIQDPTEDAE
AEDTPRKRLRTDKHSLRKRDTITDKTARTSSYKAMEAASSLKSQAATKNLSDACKPLKKR
NRASTAASSALGFSKSSSPSASLTENEVSDSPGDEPSESPYESADETQTEVSVSSKKSER
GVTAKKEYVCQLCEKPGSLLLCEGPCCGAFHLACLGLSRRPEGRFTCSECASGIHSCFVC
KESKTDVKRCVVTQCGKFYHEACVKKYPLTVFESRGFRCPLHSCVSCHASNPSNPRPSKG
KMMRCVRCPVAYHSGDACLAAGCSVIASNSIICTAHFTARKGKRHHAHVNVSWCFVCSKG
GSLLCCESCPAAFHPDCLNIEMPDGSWFCNDCRAGKKLHFQDIIWVKLGNYRWWPAEVCH
PKNVPPNIQKMKHEIGEFPVFFFGSKDYYWTHQARVFPYMEGDRGSRYQGVRGIGRVFKN
ALQEAEARFREIKLQREARETQESERKPPPYKHIKVNKPYGKVQIYTADISEIPKCNCKP
TDENPCGFDSECLNRMLMFECHPQVCPAGEFCQNQCFTKRQYPETKIIKTDGKGWGLVAK
RDIRKGEFVNEYVGELIDEEECMARIKHAHENDITHFYMLTIDKDRIIDAGPKGNYSRFM
NHSCQPNCETLKWTVNGDTRVGLFAVCDIPAGTELTFNYNLDCLGNEKTVCRCGASNCSG
FLGDRPKTSTTLSSEEKGKKTKKKTRRRRAKGEGKRQSEDECFRCGDGGQLVLCDRKFCT
KAYHLSCLGLGKRPFGKWECPWHHCDVCGKPSTSFCHLCPNSFCKEHQDGTAFSCTPDGR
SYCCEHDLGAASVRSTKTEKPPPEPGKPKGKRRRRRGWRRVTEGK
Sequence of entity 3 (C), FASTA
>29HI_3 S-phase kinase-associated protein 1 (chains C)
MPSIKLQSSDGEIFEVDVEIAKQSVTIKTMLEDLGMDDEGDDDPVPLPNVNAAILKKVIQ
WCTHHKDDPPPPEDDENKEKRTDDIPVWDQEFLKVDQGTLFELILAANYLDIKGLLDVTC
KTVANMIKGKTPEEIRKTFNIKNDFTEEEEAQVRKENQWCEEK
Sequence of entity 4 (D), FASTA
>29HI_4 Cullin-1 (chains D)
MSSTRSQNPHGLKQIGLDQIWDDLRAGIQQVYTRQSMAKSRYMELYTHVYNYCTSVHQSN
QARGAGVPPSKSKKGQTPGGAQFVGLELYKRLKEFLKNYLTNLLKDGEDLMDESVLKFYT
QQWEDYRFSSKVLNGICAYLNRHWVRRECDEGRKGIYEIYSLALVTWRDCLFRPLNKQVT
NAVLKLIEKERNGETINTRLISGVVQSYVELGLNEDDAFAKGPTLTVYKESFESQFLADT
ERFYTRESTEFLQQNPVTEYMKKAEARLLEEQRRVQVYLHESTQDELARKCEQVLIEKHL
EIFHTEFQNLLDADKNEDLGRMYNLVSRIQDGLGELKKLLETHIHNQGLAAIEKCGEAAL
NDPKMYVQTVLDVHKKYNALVMSAFNNDAGFVAALDKACGRFINNNAVTKMAQSSSKSPE
LLARYCDSLLKKSSKNPEEAELEDTLNQVMVVFKYIEDKDVFQKFYAKMLAKRLVHQNSA
SDDAEASMISKLKQACGFEYTSKLQRMFQDIGVSKDLNEQFKKHLTNSEPLDLDFSIQVL
SSGSWPFQQSCTFALPSELERSYQRFTAFYASRHSGRKLTWLYQLSKGELVTNCFKNRYT
LQASTFQMAILLQYNTEDAYTVQQLTDSTQIKMDILAQVLQILLKSKLLVLEDENANVDE
VELKPDTLIKLYLGYKNKKLRVNINVPMKTEQKQEQETTHKNIEEDRKLLIQAAIVRIMK
MRKVLKHQQLLGEVLTQLSSRFKPRVPVIKKCIDILIEKEYLERVDGEKDTYSYLA
Sequence of entity 5 (E), FASTA
>29HI_5 E3 ubiquitin-protein ligase RBX1 (chains E)
MAAAMDVDTPSGTNSGAGKKRFEVKKWNAVALWAWDIVVDNCAICRNHIMDLCIECQANQ
ASATSEECTVAWGVCNHAFHFHCISRWLKTRQVCPLDNREWEFQKYGH
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| A1J21 | 4-[[cyclopropyl-[(~{Z})-2-methyl-4-(5-oxidanylidene-2~{H}-1,4-oxazin-3-yl)but-3… | C37 H40 N4 O6 | 1 |
Primary citation
Structural basis of NSD2 degradation via targeted recruitment of SCF-FBXO22. Robertson, K.C., Amann, S.J., Liu, T. et al. Nat Commun (2026) 17. DOI 10.1038/s41467-026-72235-9 · PubMed
Other PDB entries of the same protein (UniProt Q8NEZ5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 8S7D 3.2 Å, Cryo-EM structure of SKP1-FBXO22 in complex with a BACH1 BTB dimer at 3.2A resolution
- 8S7E 3.4 Å, Cryo-EM structure of SKP1-FBXO22
- 8UA3 3.8 Å, Cryo-EM Structure of FBOX22-BACH1BTB
- 8UA6 3.9 Å, Cryo-EM Structure of SCF-FBOX22-BACH1BTB
- 29HG 4.0 Å, Cryo-EM structure of the CUL1-RBX1-SKP1-FBXO22 SCF ubiquition ligase in complex with…
- 29HH 4.2 Å, Cryo-EM structure of the CUL1-RBX1-SKP1-FBXO22 SCF ubiquition ligase in complex with…
Browse structure collections
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