9J77: CRL2-FEM1B
Cryo-EM structure of CRL2-FEM1B (dimer 1). Determined by electron microscopy at 3.56 Å resolution. Released 9 Apr 2025.
- Method
- Electron microscopy
- Resolution
- 3.56 Å
- Organism
- Homo sapiens
- Chains
- 12
- Atoms
- 26,209
- Mol. weight
- 387.71 kDa
- Ligands
- ZN
- Released
- 9 Apr 2025
Explore 9J77 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9J77 contains 169 α-helices and 58 β-strands across 12 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: 40 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 10-25 | 16 | |
| α-helix | 32-47 | 16 | |
| α-helix | 54-78 | 25 | |
| α-helix | 83-104 | 22 | |
| α-helix | 106-108 | 3 | |
| α-helix | 109-113 | 5 | |
| α-helix | 139-147 | 9 | |
| α-helix | 148-152 | 5 | |
| α-helix | 156-163 | 8 | |
| α-helix | 165-171 | 7 | |
| α-helix | 178-190 | 13 | |
| α-helix | 191-194 | 4 | |
| α-helix | 201-206 | 6 | |
| α-helix | 208-226 | 19 | |
| α-helix | 232-253 | 22 | |
| α-helix | 256-258 | 3 | |
| α-helix | 259-270 | 12 | |
| α-helix | 272-274 | 3 | |
| α-helix | 275-280 | 6 | |
| α-helix | 282-287 | 6 | |
| α-helix | 291-303 | 13 | |
| α-helix | 308-326 | 19 | |
| α-helix | 335-352 | 18 | |
| α-helix | 362-376 | 15 | |
| α-helix | 379-380 | 2 | |
| α-helix | 387-399 | 13 | |
| β-strand | 400 | 1 | 18 |
| α-helix | 408-416 | 9 | |
| α-helix | 418-422 | 5 | |
| α-helix | 428-443 | 16 | |
| β-strand | 448 | 1 | 18 |
| α-helix | 451-465 | 15 | |
| α-helix | 471-495 | 25 | |
| β-strand | 506-507 | 2 | 2 |
| β-strand | 510-513 | 4 | 3 |
| α-helix | 534-547 | 14 | |
| β-strand | 551-555 | 5 | 3 |
| α-helix | 556 | 1 | |
| β-strand | 561-563 | 3 | 2 |
| β-strand | 576-578 | 3 | 2 |
| α-helix | 579-590 | 12 | |
| β-strand | 594 | 1 | 19 |
| α-helix | 596-602 | 7 | |
| α-helix | 609-619 | 11 | |
| β-strand | 623-625 | 3 | 19 |
| β-strand | 638-640 | 3 | 19 |
| α-helix | 660-661 | 2 | |
| α-helix | 662-689 | 28 | |
| β-strand | 693-694 | 2 | 20 |
| α-helix | 696-705 | 10 | |
| α-helix | 715-727 | 13 | |
| β-strand | 731-733 | 3 | 20 |
| β-strand | 741-743 | 3 | 20 |
Chain B: 36 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 10-25 | 16 | |
| α-helix | 32-46 | 15 | |
| α-helix | 55-78 | 24 | |
| α-helix | 80-82 | 3 | |
| α-helix | 83-104 | 22 | |
| α-helix | 106-108 | 3 | |
| α-helix | 109-113 | 5 | |
| α-helix | 139-147 | 9 | |
| α-helix | 148-152 | 5 | |
| α-helix | 156-171 | 16 | |
| α-helix | 178-186 | 9 | |
| α-helix | 201-203 | 3 | |
| α-helix | 204-208 | 5 | |
| α-helix | 209-229 | 21 | |
| α-helix | 232-253 | 22 | |
| α-helix | 256-258 | 3 | |
| α-helix | 259-270 | 12 | |
| α-helix | 275-288 | 14 | |
| α-helix | 291-303 | 13 | |
| α-helix | 308-327 | 20 | |
| α-helix | 335-357 | 23 | |
| α-helix | 362-376 | 15 | |
| α-helix | 387-399 | 13 | |
| β-strand | 400 | 1 | 6 |
| α-helix | 408-423 | 16 | |
| α-helix | 428-445 | 18 | |
| β-strand | 448 | 1 | 6 |
| α-helix | 451-465 | 15 | |
| α-helix | 471-481 | 11 | |
| α-helix | 483-495 | 13 | |
| β-strand | 507 | 1 | 7 |
| β-strand | 510-513 | 4 | 8 |
| α-helix | 531-547 | 17 | |
| β-strand | 551-555 | 5 | 8 |
| α-helix | 557-559 | 3 | |
| β-strand | 561-566 | 6 | 9 |
| β-strand | 574-578 | 5 | 9 |
| α-helix | 579-590 | 12 | |
| α-helix | 596-602 | 7 | |
| α-helix | 607-619 | 13 | |
| β-strand | 652 | 1 | 9 |
| α-helix | 662-691 | 30 | |
| α-helix | 696-707 | 12 | |
| α-helix | 715-727 | 13 | |
Chain C: 5 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 18-22 | 5 | 10 |
| β-strand | 28-32 | 5 | 10 |
| α-helix | 33-36 | 4 | |
| α-helix | 40-46 | 7 | |
| β-strand | 60-61 | 2 | 10 |
| α-helix | 67-82 | 16 | |
| α-helix | 91-93 | 3 | |
| α-helix | 103-110 | 8 | |
Chain D: 4 helices, 5 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-9 | 7 | 10 |
| β-strand | 12-18 | 7 | 10 |
| α-helix | 25-35 | 11 | |
| β-strand | 43-45 | 3 | 10 |
| β-strand | 50 | 1 | 10 |
| α-helix | 72 | 1 | |
| β-strand | 73-78 | 6 | 10 |
| α-helix | 79-80 | 2 | |
| α-helix | 91-97 | 7 | |
Chain E: 2 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 22-28 | 7 | 9 |
| β-strand | 30-35 | 6 | 8 |
| β-strand | 41 | 1 | 13 |
| β-strand | 48 | 1 | 13 |
| α-helix | 54-57 | 4 | |
| β-strand | 70-72 | 3 | 14 |
| β-strand | 78-80 | 3 | 14 |
| α-helix | 81-88 | 8 | |
| β-strand | 93 | 1 | 15 |
| β-strand | 100 | 1 | 15 |
Chain F: 36 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-13 | 12 | |
| α-helix | 17-22 | 6 | |
| α-helix | 29-36 | 8 | |
| β-strand | 40-42 | 3 | 16 |
| β-strand | 45-47 | 3 | 16 |
| α-helix | 49-55 | 7 | |
| α-helix | 59-68 | 10 | |
| β-strand | 77 | 1 | 17 |
| β-strand | 89 | 1 | 17 |
| α-helix | 91-97 | 7 | |
| α-helix | 101-109 | 9 | |
| α-helix | 124-131 | 8 | |
| α-helix | 134-142 | 9 | |
| α-helix | 157-163 | 7 | |
| α-helix | 167-173 | 7 | |
| α-helix | 174-176 | 3 | |
| α-helix | 194-196 | 3 | |
| α-helix | 200-209 | 10 | |
| α-helix | 222-228 | 7 | |
| α-helix | 232-238 | 7 | |
| α-helix | 247-261 | 15 | |
| α-helix | 269-283 | 15 | |
| α-helix | 292-294 | 3 | |
| α-helix | 296-298 | 3 | |
| α-helix | 311-316 | 6 | |
| α-helix | 321-336 | 16 | |
| α-helix | 345-355 | 11 | |
| α-helix | 361-376 | 16 | |
| α-helix | 382-397 | 16 | |
| α-helix | 404-427 | 24 | |
| α-helix | 433-455 | 23 | |
| α-helix | 461-477 | 17 | |
| α-helix | 487-492 | 6 | |
| α-helix | 503-506 | 4 | |
| α-helix | 512-521 | 10 | |
| α-helix | 536-539 | 4 | |
| α-helix | 549-562 | 14 | |
| α-helix | 585-590 | 6 | |
| α-helix | 597-608 | 12 | |
| α-helix | 618-624 | 7 | |
Chain G: 4 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 18-22 | 5 | 1 |
| β-strand | 28-32 | 5 | 1 |
| α-helix | 33-36 | 4 | |
| α-helix | 40-46 | 7 | |
| β-strand | 60-61 | 2 | 1 |
| α-helix | 67-82 | 16 | |
| α-helix | 103-110 | 8 | |
Chain H: 2 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-8 | 6 | 1 |
| β-strand | 13-18 | 6 | 1 |
| α-helix | 24-35 | 12 | |
| β-strand | 43-45 | 3 | 1 |
| β-strand | 75-78 | 4 | 1 |
| α-helix | 91-96 | 6 | |
4 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Elongin-C | C, G | protein | 96 | Homo sapiens | Q15369 (AlphaFold model) |
| Elongin-B | D, H | protein | 121 | Homo sapiens | Q15370 (AlphaFold model) |
| E3 ubiquitin-protein ligase RBX1, N-terminally processed | E, I | protein | 96 | Homo sapiens | P62877 (AlphaFold model) |
| Cullin-2 | A, B | protein | 749 | Homo sapiens | Q13617 (AlphaFold model) |
| Protein fem-1 homolog B | F, J | protein | 627 | Homo sapiens | Q9UK73 |
| Poly-UNK | K, L | protein | 10 | Homo sapiens | |
Sequence of entity 1 (C, G), FASTA
>9J77_1 Elongin-C (chains C, G)
MYVKLISSDGHEFIVKREHALTSGTIKAMLSGPGQFAENETNEVNFREIPSHVLSKVCMY
FTYKVRYTNSSTEIPEFPIAPEIALELLMAANFLDC
Sequence of entity 2 (D, H), FASTA
>9J77_2 Elongin-B (chains D, H)
GGSMDVFLMIRRHKTTIFTDAKESSTVFELKRIVEGILKRPPDEQRLYKDDQLLDDGKTL
GECGFTSQTARPQAPATVGLAFRADDTFEALCIEPFSSPPELPDVMKPQDSGSSANEQAV
Q
Sequence of entity 3 (E, I), FASTA
>9J77_3 E3 ubiquitin-protein ligase RBX1, N-terminally processed (chains E, I)
SHMGAGKKRFEVKKWNAVALWAWDIVVDNCAICRNHIMDLCIECQANQASATSEECTVAW
GVCNHAFHFHCISRWLKTRQVCPLDNREWEFQKYGH
Sequence of entity 4 (A, B), FASTA
>9J77_4 Cullin-2 (chains A, B)
SASWSHPQFEKGGGSGGGSGTSLKPRVVDFDETWNKLLTTIKAVVMLEYVERATWNDRFS
DIYALCVAYPEPLGERLYTETKIFLENHVRHLHKRVLESEEQVLVMYHRYWEEYSKGADY
MDCLYRYLNTQFIKKNGGGPLMEIGELALDMWRKLMVEPLQAILIRMLLREIKNDRGGED
PNQKVIHGVINSFVHVEQYKKKFPLKFYQEIFESPFLTETGEYYKQEASNLLQESNCSQY
MEKVLGRLKDEEIRCRKYLHPSSYTKVIHECQQRMVADHLQFLHAECHNIIRQEKKNDMA
NMYVLLRAVSTGLPHMIQELQNHIHDEGLRATSNLTQENMPTLFVESVLEVHGKFVQLIN
TVLNGDQHFMSALDKALTSVVNYREPKSVCKAPELLAKYCDNLLKKSAKGMTENEVEDRL
TSFITVFKYIDDKDVFQKFYARMLAKRLIHGLSMSMDSEEAMINKLKQACGYEFTSKLHR
MYTDMSVSADLNNKFNNFIKNQDTVIDLGISFQIYVLQAGAWPLTQAPSSTFAIPQELEK
SVQMFELFYSQHFSGRKLTWLHYLCTGEVKMNYLGKPYVAMVTTYQMAVLLAFNNSETVS
YKELQDSTQMNEKELTKTIKSLLDVKMINHDSEKEDIDAESSFSLNMNFSSKRTKFKITT
SMQKDTPQEMEQTRSAVDEDRKMYLQAAIVRIMKARKVLRHNALIQEVISQSRARFNPSI
SMIKKCIEVLIDKQYIERSQASADEYSYV
Sequence of entity 5 (F, J), FASTA
>9J77_5 Protein fem-1 homolog B (chains F, J)
MEGLAGYVYKAASEGKVLTLAALLLNRSESDIRYLLGYVSQQGGQRSTPLIIAARNGHAK
VVRLLLEHYRVQTQQTGTVRFDGYVIDGATALWCAAGAGHFEVVKLLVSHGANVNHTTVT
NSTPLRAACFDGRLDIVKYLVENNANISIANKYDNTCLMIAAYKGHTDVVRYLLEQRADP
NAKAHCGATALHFAAEAGHIDIVKELIKWRAAIVVNGHGMTPLKVAAESCKADVVELLLS
HADCDRRSRIEALELLGASFANDRENYDIIKTYHYLYLAMLERFQDGDNILEKEVLPPIH
AYGNRTECRNPQELESIRQDRDALHMEGLIVRERILGADNIDVSHPIIYRGAVYADNMEF
EQCIKLWLHALHLRQKGNRNTHKDLLRFAQVFSQMIHLNETVKAPDIECVLRCSVLEIEQ
SMNRVKNISDADVHNAMDNYECNLYTFLYLVCISTKTQCSEEDQCKINKQIYNLIHLDPR
TREGFTLLHLAVNSNTPVDDFHTNDVCSFPNALVTKLLLDCGAEVNAVDNEGNSALHIIV
QYNRPISDFLTLHSIIISLVEAGAHTDMTNKQNKTPLDKSTTGVSEILLKTQMKMSLKCL
AARAVRANDINYQDQIPRTLEEFVGFH
Sequence of entity 6 (K, L), FASTA
>9J77_6 Poly-UNK (chains K, L)
XXXXXXXXXX
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| ZN | Zinc ion | Zn | 6 |
Primary citation
TOM20-driven E3 ligase recruitment regulates mitochondrial dynamics through PLD6. Raiff, A., Zhao, S., Bekturova, A. et al. Nat Chem Biol (2026) 22:37-47. DOI 10.1038/s41589-025-01894-4 · PubMed
Other PDB entries of the same protein (UniProt Q15369 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 7Z76 1.32 Å, Crystal structure of compound 10 in complex with the bromodomain of human SMARCA2 and…
- 9GIO 1.49 Å, Crystal structure of the VHL-EloC-EloB complex with a covalent compound bound to C77 of…
- 7JTO 1.7 Å, Crystal structure of Protac MS33 in complex with the WD repeat-containing protein 5 and…
- 8BDS 1.72 Å, Ternary complex between VCB, BRD4-BD1 and PROTAC 48
- 4AJY 1.73 Å, von Hippel-Lindau protein-ElonginB-ElonginC complex, bound to Hif1- alpha peptide
- 6GMR 1.75 Å, pVHL:EloB:EloC in complex with (4-(1H-pyrrol-1-yl)phenyl)methanol
- 6HR2 1.76 Å, Crystal structure of PROTAC 2 in complex with the bromodomain of human SMARCA4 and…
- 7ZLM 1.79 Å, Crystal structure of SOCS2:ElonginB:ElonginC in complex with compound MN551
- 8BB3 1.8 Å, Structure of human WDR5 and pVHL:ElonginC:ElonginB bound to PROTAC with PEG linker…
- 6GFX 1.83 Å, pVHL:EloB:EloC in complex with modified HIF-1a CODD peptide containing…
- 1LM8 1.85 Å, Structure of a HIF-1a-pVHL-ElonginB-ElonginC Complex
- 9D1Z 1.88 Å, Structure of G75Q Ubiquitin bound to KLHDC3-EloB/C
Browse structure collections
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