Structure of RBR E2 variant binding to CUL5-RBX2 bound ARIH2. Determined by electron microscopy at 3.06 Å resolution. Released 24 Dec 2025.
Explore 9SDY in 3D Show helices and sheets RCSB PDB PDBe
9SDY contains 55 α-helices and 35 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 156-168 | 13 | |
| α-helix | 175-187 | 13 | |
| α-helix | 196-200 | 5 | |
| α-helix | 203-248 | 46 | |
| α-helix | 257-269 | 13 | |
| α-helix | 271-273 | 3 | |
| α-helix | 274-278 | 5 | |
| α-helix | 281-285 | 5 | |
| α-helix | 290-300 | 11 | |
| α-helix | 308-328 | 21 | |
| α-helix | 338-359 | 22 | |
| α-helix | 363-377 | 15 | |
| α-helix | 404-416 | 13 | |
| β-strand | 417 | 1 | 8 |
| α-helix | 420-423 | 4 | |
| α-helix | 427-441 | 15 | |
| α-helix | 447-464 | 18 | |
| β-strand | 467 | 1 | 8 |
| α-helix | 471-483 | 13 | |
| α-helix | 487-513 | 27 | |
| α-helix | 523-525 | 3 | |
| β-strand | 526-532 | 7 | 4 |
| α-helix | 549-565 | 17 | |
| β-strand | 569-573 | 5 | 4 |
| β-strand | 579-585 | 7 | 4 |
| β-strand | 590-596 | 7 | 4 |
| α-helix | 597-603 | 7 | |
| α-helix | 604-606 | 3 | |
| β-strand | 614-615 | 2 | 9 |
| α-helix | 616-623 | 8 | |
| α-helix | 627-638 | 12 | |
| β-strand | 648-650 | 3 | 9 |
| α-helix | 657-659 | 3 | |
| β-strand | 665-668 | 4 | 9 |
| β-strand | 685-687 | 3 | 4 |
| α-helix | 697-699 | 3 | |
| α-helix | 701-724 | 24 | |
| α-helix | 734-741 | 8 | |
| α-helix | 750-763 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 5-17 | 13 | |
| β-strand | 22 | 1 | 1 |
| β-strand | 26 | 1 | 2 |
| β-strand | 34-37 | 4 | 2 |
| β-strand | 39 | 1 | 1 |
| β-strand | 53-56 | 4 | 2 |
| α-helix | 61-63 | 3 | |
| α-helix | 65-66 | 2 | |
| β-strand | 67-70 | 4 | 2 |
| β-strand | 79 | 1 | 3 |
| β-strand | 85 | 1 | 3 |
| α-helix | 101-113 | 13 | |
| α-helix | 123-129 | 7 | |
| α-helix | 134-137 | 4 | |
| α-helix | 139-146 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 62-64 | 3 | 10 |
| α-helix | 66-83 | 18 | |
| α-helix | 88-97 | 10 | |
| α-helix | 102-119 | 18 | |
| α-helix | 124-125 | 2 | |
| α-helix | 148-150 | 3 | |
| β-strand | 151-153 | 3 | 11 |
| β-strand | 159-161 | 3 | 11 |
| α-helix | 162-175 | 14 | |
| β-strand | 182 | 1 | 12 |
| β-strand | 191 | 1 | 12 |
| α-helix | 192-193 | 2 | |
| α-helix | 194-196 | 3 | |
| α-helix | 209-221 | 13 | |
| β-strand | 225-227 | 3 | 10 |
| β-strand | 236-238 | 3 | 10 |
| β-strand | 246-248 | 3 | 13 |
| β-strand | 255-257 | 3 | 13 |
| α-helix | 270-279 | 10 | |
| α-helix | 353-398 | 46 | |
| α-helix | 404-406 | 3 | |
| α-helix | 409-425 | 17 | |
| α-helix | 428-431 | 4 | |
| α-helix | 434-435 | 2 | |
| α-helix | 438-462 | 25 | |
| α-helix | 469-486 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 31-43 | 13 | 4 |
| β-strand | 49 | 1 | 5 |
| β-strand | 56 | 1 | 5 |
| α-helix | 62-66 | 5 | |
| β-strand | 75-78 | 4 | 6 |
| β-strand | 83-85 | 3 | 6 |
| α-helix | 86-93 | 8 | |
| β-strand | 98 | 1 | 7 |
| β-strand | 105 | 1 | 7 |
| β-strand | 108-111 | 4 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| L3A2-1 | G | protein | 155 | synthetic construct | |
| RING-box protein 2 | R | protein | 113 | Homo sapiens | Q9UBF6 (AlphaFold model) |
| Cullin-5 | C | protein | 780 | Homo sapiens | Q93034 (AlphaFold model) |
| E3 ubiquitin-protein ligase ARIH2 | H | protein | 493 | Homo sapiens | O95376 (AlphaFold model) |
>9SDY_1 L3A2-1 (chains G) MVAASSRLMKELEEIRKAGMKNFRNIQVDEANLLTWQGLIVPDNPPYDKGAFRIEINFPA EYPFKPPKITFKTKIYHPNIDEKGQVCLPVISAENWKPATKTDQVIQSLIALVNDPQPEH PLRADLAEEYSKDRKKFAKNAEEFTKKYGEKRPVD
>9SDY_2 RING-box protein 2 (chains R) MADVEDGEETCALASHSGSSGSKSGGDKMFSLKKWNAVAMWSWDVECDTCAICRVQVMDA CLRCQAENKQEDCVVVWGECNHSFHNCCMSLWVKQNNRCPLCQQDWVVQRIGK
>9SDY_3 Cullin-5 (chains C) MATSNLLKNKGSLQFEDKWDFMRPIVLKLLRQESVTKQQWFDLFSDVHAVCLWDDKGPAK IHQALKEDILEFIKQAQARVLSHQDDTALLKAYIVEWRKFFTQCDILPKPFCQLEITLMG KQGSNKKSNVEDSIVRKLMLDTWNESIFSNIKNRLQDSAMKLVHAERLGEAFDSQLVIGV RESYVNLCSNPEDKLQIYRDNFEKAYLDSTERFYRTQAPSYLQQNGVQNYMKYADAKLKE EEKRALRYLETRRECNSVEALMECCVNALVTSFKETILAECQGMIKRNETEKLHLMFSLM DKVPNGIEPMLKDLEEHIISAGLADMVAAAETITTDSEKYVEQLLTLFNRFSKLVKEAFQ DDPRFLTARDKAYKAVVNDATIFKLELPLKQKGVGLKTQPESKCPELLANYCDMLLRKTP LSKKLTSEEIEAKLKEVLLVLKYVQNKDVFMRYHKAHLTRRLILDISADSEIEENMVEWL REVGMPADYVNKLARMFQDIKVSEDLNQAFKEMHKNNKLALPADSVNIKILNAGAWSRSS EKVFVSLPTELEDLIPEVEEFYKKNHSGRKLHWHHLMSNGIITFKNEVGQYDLEVTTFQL AVLFAWNQRPREKISFENLKLATELPDAELRRTLWSLVAFPKLKRQVLLYEPQVNSPKDF TEGTLFSVNQEFSLIKNAKVQKRGKINLIGRLQLTTERMREEENEGIVQLRILRTQEAII QIMKMRKKISNAQLQTELVEILKNMFLPQKKMIKEQIEWLIEHKYIRRDESDINTFIYMA
>9SDY_4 E3 ubiquitin-protein ligase ARIH2 (chains H) MSVDMNSQGSDSNEEDYDPNCEEEEEEEEDDPGDIEDYYVGVASDVEQQGADAFDPEEYQ FTCLTYKESEGALNEHMTSLASVLKVSHSVAKLILVNFHWQVSEILDRYKSNSAQLLVEA RVQPNPSKHVPTSHPPHHCAVCMQFVRKENLLSLACQHQFCRSCWEQHCSVLVKDGVGVG VSCMAQDCPLRTPEDFVFPLLPNEELREKYRRYLFRDYVESHYQLQLCPGADCPMVIRVQ EPRARRVQCNRCNEVFCFKCRQMYHAPTDCATIRKWLTKCADDSETANYISAHTKDCPKC NICIEKNGGCNHMQCSKCKHDFCWMCLGDWKTHGSEYYECSRYKENPDIVNQSQQAQARE ALKKYLFYFERWENHNKSLQLEAQTYQRIHEKIQERVMNNLGTWIDWQYLQNAAKLLAKC RYTLQYTYPYAYYMESGPRKKLFEYQQAQLEAEIENLSWKVERADSYDRGDLENQMHIAE QRRRTLLKDFHDT
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 7 |
E2 variants for probing E3 ubiquitin ligase activities. Du, J., Andree, G.A., Horn-Ghetko, D. et al. Proc Natl Acad Sci U S A (2026) 123:e2524899122-e2524899122. DOI 10.1073/pnas.2524899122 · PubMed
Other PDB entries of the same protein (UniProt Q9UBF6 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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