9UA3: Neddylated CUL2-RBX1-FEM1C-ELOB-ELOC
Cryo-EM structure of neddylated CUL2-RBX1-FEM1C-ELOB-ELOC. Determined by electron microscopy at 3.28 Å resolution. Released 4 Mar 2026.
- Method
- Electron microscopy
- Resolution
- 3.28 Å
- Organism
- Homo sapiens
- Chains
- 10
- Atoms
- 17,924
- Mol. weight
- 360.6 kDa
- Released
- 4 Mar 2026
Explore 9UA3 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9UA3 contains 140 α-helices and 42 β-strands across 8 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: 43 helices, 5 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-13 | 11 | |
| α-helix | 16-25 | 10 | |
| α-helix | 28-35 | 8 | |
| α-helix | 44-51 | 8 | |
| α-helix | 54-58 | 5 | |
| α-helix | 59-63 | 5 | |
| β-strand | 72-76 | 5 | 1 |
| β-strand | 79-84 | 6 | 1 |
| α-helix | 86-92 | 7 | |
| α-helix | 96-104 | 9 | |
| α-helix | 119-126 | 8 | |
| α-helix | 129-137 | 9 | |
| α-helix | 152-158 | 7 | |
| α-helix | 162-171 | 10 | |
| α-helix | 186-190 | 5 | |
| α-helix | 195-201 | 7 | |
| α-helix | 202-204 | 3 | |
| α-helix | 217-222 | 6 | |
| α-helix | 227-233 | 7 | |
| α-helix | 241-257 | 17 | |
| α-helix | 262-276 | 15 | |
| α-helix | 285-289 | 5 | |
| β-strand | 292-293 | 2 | 2 |
| α-helix | 294-296 | 3 | |
| α-helix | 299-302 | 4 | |
| α-helix | 305-309 | 5 | |
| α-helix | 310-313 | 4 | |
| α-helix | 317-329 | 13 | |
| α-helix | 339-349 | 11 | |
| α-helix | 354-371 | 18 | |
| α-helix | 373 | 1 | |
| α-helix | 377-399 | 23 | |
| α-helix | 405-407 | 3 | |
| α-helix | 408-427 | 20 | |
| α-helix | 432-434 | 3 | |
| α-helix | 435-452 | 18 | |
| α-helix | 459-474 | 16 | |
| α-helix | 480-482 | 3 | |
| α-helix | 485-489 | 5 | |
| α-helix | 508-515 | 8 | |
| α-helix | 531-537 | 7 | |
| α-helix | 541-549 | 9 | |
| α-helix | 564-567 | 4 | |
| α-helix | 570-575 | 6 | |
| α-helix | 586-597 | 12 | |
| β-strand | 602 | 1 | 3 |
| β-strand | 605 | 1 | 3 |
| α-helix | 607-615 | 9 | |
Chain B: 19 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 10-25 | 16 | |
| α-helix | 32-46 | 15 | |
| α-helix | 55-77 | 23 | |
| α-helix | 80-82 | 3 | |
| α-helix | 83-104 | 22 | |
| α-helix | 106-107 | 2 | |
| α-helix | 108-114 | 7 | |
| α-helix | 139-147 | 9 | |
| α-helix | 148-152 | 5 | |
| α-helix | 156-172 | 17 | |
| α-helix | 178-190 | 13 | |
| α-helix | 201-206 | 6 | |
| α-helix | 208-228 | 21 | |
| α-helix | 232-253 | 22 | |
| α-helix | 258-267 | 10 | |
| α-helix | 268-272 | 5 | |
| α-helix | 275-288 | 14 | |
| α-helix | 291-303 | 13 | |
| α-helix | 307-324 | 18 | |
Chain C: 4 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-4 | 2 | 5 |
| β-strand | 5-9 | 5 | 6 |
| β-strand | 12-14 | 3 | 6 |
| β-strand | 17-18 | 2 | 5 |
| β-strand | 23 | 1 | 7 |
| α-helix | 24-35 | 12 | |
| α-helix | 39-41 | 3 | |
| β-strand | 43-45 | 3 | 6 |
| β-strand | 56 | 1 | 7 |
| α-helix | 57-60 | 4 | |
| β-strand | 73-78 | 6 | 6 |
| β-strand | 80-81 | 2 | 8 |
| β-strand | 84-85 | 2 | 8 |
| α-helix | 90-99 | 10 | |
Chain D: 6 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 18-22 | 5 | 6 |
| α-helix | 23 | 1 | |
| β-strand | 28-32 | 5 | 6 |
| α-helix | 33-36 | 4 | |
| α-helix | 40-45 | 6 | |
| β-strand | 57-61 | 5 | 6 |
| α-helix | 67-83 | 17 | |
| α-helix | 91-94 | 4 | |
| α-helix | 100-110 | 11 | |
Chain E: 41 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-13 | 11 | |
| α-helix | 16-24 | 9 | |
| α-helix | 28-35 | 8 | |
| α-helix | 44-50 | 7 | |
| α-helix | 54-58 | 5 | |
| α-helix | 59-63 | 5 | |
| β-strand | 72-76 | 5 | 4 |
| β-strand | 79-84 | 6 | 4 |
| α-helix | 86-92 | 7 | |
| α-helix | 96-104 | 9 | |
| α-helix | 119-126 | 8 | |
| α-helix | 129-137 | 9 | |
| α-helix | 152-158 | 7 | |
| α-helix | 162-171 | 10 | |
| α-helix | 185-188 | 4 | |
| α-helix | 195-201 | 7 | |
| α-helix | 202-204 | 3 | |
| α-helix | 217-222 | 6 | |
| α-helix | 227-233 | 7 | |
| α-helix | 241-257 | 17 | |
| α-helix | 262-276 | 15 | |
| α-helix | 285-289 | 5 | |
| β-strand | 291-292 | 2 | 2 |
| α-helix | 299-302 | 4 | |
| α-helix | 305-309 | 5 | |
| α-helix | 310-312 | 3 | |
| α-helix | 317-329 | 13 | |
| α-helix | 335-350 | 16 | |
| α-helix | 354-371 | 18 | |
| α-helix | 373 | 1 | |
| α-helix | 377-399 | 23 | |
| α-helix | 408-427 | 20 | |
| α-helix | 432-434 | 3 | |
| α-helix | 435-453 | 19 | |
| α-helix | 459-473 | 15 | |
| α-helix | 480-482 | 3 | |
| α-helix | 485-489 | 5 | |
| α-helix | 508-517 | 10 | |
| α-helix | 531-537 | 7 | |
| α-helix | 541-550 | 10 | |
| α-helix | 565-567 | 3 | |
| α-helix | 570-575 | 6 | |
| α-helix | 586-596 | 11 | |
| α-helix | 607-615 | 9 | |
Chain F: 19 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 10-25 | 16 | |
| α-helix | 32-46 | 15 | |
| α-helix | 54-77 | 24 | |
| α-helix | 83-104 | 22 | |
| α-helix | 106-107 | 2 | |
| α-helix | 108-114 | 7 | |
| α-helix | 139-147 | 9 | |
| α-helix | 148-152 | 5 | |
| α-helix | 156-172 | 17 | |
| α-helix | 178-190 | 13 | |
| α-helix | 201-203 | 3 | |
| α-helix | 204-208 | 5 | |
| α-helix | 209-228 | 20 | |
| α-helix | 232-252 | 21 | |
| α-helix | 258-267 | 10 | |
| α-helix | 268-272 | 5 | |
| α-helix | 275-287 | 13 | |
| α-helix | 292-303 | 12 | |
| α-helix | 307-323 | 17 | |
Chain G: 3 helices, 16 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 5-6 | 2 | 9 |
| β-strand | 9 | 1 | 10 |
| β-strand | 12 | 1 | 10 |
| β-strand | 13-14 | 2 | 11 |
| β-strand | 15-16 | 2 | 9 |
| β-strand | 23 | 1 | 12 |
| α-helix | 24-34 | 11 | |
| β-strand | 43 | 1 | 13 |
| β-strand | 45 | 1 | 14 |
| β-strand | 50 | 1 | 14 |
| β-strand | 56 | 1 | 12 |
| β-strand | 68 | 1 | 15 |
| β-strand | 71 | 1 | 15 |
| α-helix | 72-73 | 2 | |
| β-strand | 74 | 1 | 9 |
| β-strand | 78 | 1 | 13 |
| β-strand | 80-81 | 2 | 16 |
| β-strand | 84-85 | 2 | 16 |
| α-helix | 90-99 | 10 | |
Chain H: 5 helices, 5 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 18 | 1 | 17 |
| β-strand | 20-22 | 3 | 11 |
| β-strand | 28-30 | 3 | 11 |
| β-strand | 32 | 1 | 17 |
| α-helix | 33-36 | 4 | |
| α-helix | 40-45 | 6 | |
| β-strand | 59-61 | 3 | 11 |
| α-helix | 67-82 | 16 | |
| α-helix | 89-93 | 5 | |
| α-helix | 100-110 | 11 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Protein fem-1 homolog C | A, E | protein | 617 | Homo sapiens | Q96JP0 (AlphaFold model) |
| Cullin-2 | B, F | protein | 745 | Homo sapiens | Q13617 (AlphaFold model) |
| Elongin-B | C, G | protein | 118 | Homo sapiens | Q15370 (AlphaFold model) |
| Elongin-C | D, H | protein | 96 | Homo sapiens | Q15369 (AlphaFold model) |
| Ala-arg-ala-arg | I, J | protein | 4 | Homo sapiens | |
Sequence of entity 1 (A, E), FASTA
>9UA3_1 Protein fem-1 homolog C (chains A, E)
MDLKTAVFNAARDGKLRLLTKLLASKSKEEVSSLISEKTNGATPLLMAARYGHLDMVEFL
LEQCSASIEVGGSVNFDGETIEGAPPLWAASAAGHLKVVQSLLNHGASVNNTTLTNSTPL
RAACFDGHLEIVKYLVEHKADLEVSNRHGHTCLMISCYKGHKEIAQYLLEKGADVNRKSV
KGNTALHDCAESGSLDIMKMLLMYCAKMEKDGYGMTPLLSASVTGHTNIVDFLTHHAQTS
KTERINALELLGATFVDKKRDLLGALKYWKKAMNMRYSDRTNIISKPVPQTLIMAYDYAK
EVNSAEELEGLIADPDEMRMQALLIRERILGPSHPDTSYYIRYRGAVYADSGNFKRCINL
WKYALDMQQSNLDPLSPMTASSLLSFAELFSFMLQDRAKGLLGTTVTFDDLMGILCKSVL
EIERAIKQTQCPADPLQLNKALSIILHLICLLEKVPCTLEQDHFKKQTIYRFLKLHPRGK
NNFSPLHLAVDKNTTCVGRYPVCKFPSLQVTAILIECGADVNVRDSDDNSPLHIAALNNH
PDIMNLLIKSGAHFDATNLHKQTASDLLDEKEIAKNLIQPINHTTLQCLAARVIVNHRIY
YKGHIPEKLETFVSLHR
Sequence of entity 2 (B, F), FASTA
>9UA3_2 Cullin-2 (chains B, F)
TSLKPRVVDFDETWNKLLTTIKAVVMLEYVERATWNDRFSDIYALCVAYPEPLGERLYTE
TKIFLENHVRHLHKRVLESEEQVLVMYHRYWEEYSKGADYMDCLYRYLNTQFIKKNKLTE
ADLQYGYGGVDMNEPLMEIGELALDMWRKLMVEPLQAILIRMLLREIKNDRGGEDPNQKV
IHGVINSFVHVEQYKKKFPLKFYQEIFESPFLTETGEYYKQEASNLLQESNCSQYMEKVL
GRLKDEEIRCRKYLHPSSYTKVIHECQQRMVADHLQFLHAECHNIIRQEKKNDMANMYVL
LRAVSTGLPHMIQELQNHIHDEGLRATSNLTQENMPTLFVESVLEVHGKFVQLINTVLNG
DQHFMSALDKALTSVVNYREPKSVCKAPELLAKYCDNLLKKSAKGMTENEVEDRLTSFIT
VFKYIDDKDVFQKFYARMLAKRLIHGLSMSMDSEEAMINKLKQACGYEFTSKLHRMYTDM
SVSADLNNKFNNFIKNQDTVIDLGISFQIYVLQAGAWPLTQAPSSTFAIPQELEKSVQMF
ELFYSQHFSGRKLTWLHYLCTGEVKMNYLGKPYVAMVTTYQMAVLLAFNNSETVSYKELQ
DSTQMNEKELTKTIKSLLDVKMINHDSEKEDIDAESSFSLNMNFSSKRTKFKITTSMQKD
TPQEMEQTRSAVDEDRKMYLQAAIVRIMKARKVLRHNALIQEVISQSRARFNPSISMIKK
CIEVLIDKQYIERSQASADEYSYVA
Sequence of entity 3 (C, G), FASTA
>9UA3_3 Elongin-B (chains C, G)
MDVFLMIRRHKTTIFTDAKESSTVFELKRIVEGILKRPPDEQRLYKDDQLLDDGKTLGEC
GFTSQTARPQAPATVGLAFRADDTFEALCIEPFSSPPELPDVMKPQDSGSSANEQAVQ
Sequence of entity 4 (D, H), FASTA
>9UA3_4 Elongin-C (chains D, H)
MYVKLISSDGHEFIVKREHALTSGTIKAMLSGPGQFAENETNEVNFREIPSHVLSKVCMY
FTYKVRYTNSSTEIPEFPIAPEIALELLMAANFLDC
Sequence of entity 5 (I, J), FASTA
>9UA3_5 ALA-ARG-ALA-ARG (chains I, J)
ARAR
Primary citation
Structural insights into CRL2FEM1C ubiquitin ligase-mediated protein ubiquitination. Zhou, H., Israel-Gueta, M., Chen, X. et al. J Mol Cell Biol (2025) 17. DOI 10.1093/jmcb/mjaf016 · PubMed
Other PDB entries of the same protein (UniProt Q96JP0 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 6XKC 2.03 Å, Crystal structure of E3 ligase
- 6LF0 2.11 Å, Structure of FEM1C
- 6LE6 2.33 Å, Structure of LNLPTQGRAR bound FEM1C
- 6LDP 2.35 Å, Structure of CDK5R1-bound FEM1C
- 6LEN 2.38 Å, Structure of NS11 bound FEM1C
- 6LEY 2.39 Å, Structure of Sil1G bound FEM1C
- 7JYA 2.46 Å, Crystal structure of E3 ligase in complex with peptide
- 6LBG 2.51 Å, Structure of OR51B2 bound FEM1C
- 6LBN 2.9 Å, Structure of SIL1-bound FEM1C
- 8Q7R 3.71 Å, Ubiquitin ligation to substrate by a cullin-RING E3 ligase & Cdc34:…
- 8PQL 3.76 Å, K48-linked ubiquitin chain formation with a cullin-RING E3 ligase and Cdc34:…
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