9SDX: NEDD8
Structure of RBR binding E2 variant crosslinked with NEDD8-CUL5-RBX2 bound ARIH2 and Ub. Determined by electron microscopy at 2.97 Å resolution. Released 24 Dec 2025.
- Method
- Electron microscopy
- Resolution
- 2.97 Å
- Organisms
- Homo sapiens, synthetic construct
- Chains
- 6
- Atoms
- 10,572
- Mol. weight
- 197.84 kDa
- Ligands
- SY8, ZN
- Released
- 24 Dec 2025
Explore 9SDX in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9SDX contains 61 α-helices and 46 β-strands across 6 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 C: 29 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 159-168 | 10 | |
| α-helix | 176-180 | 5 | |
| α-helix | 204-247 | 44 | |
| α-helix | 257-266 | 10 | |
| α-helix | 267-271 | 5 | |
| α-helix | 274-282 | 9 | |
| α-helix | 290-301 | 12 | |
| α-helix | 308-327 | 20 | |
| α-helix | 330-333 | 4 | |
| α-helix | 337-354 | 18 | |
| α-helix | 355-359 | 5 | |
| 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 | 447-460 | 14 | |
| β-strand | 467 | 1 | 8 |
| α-helix | 470-483 | 14 | |
| α-helix | 487-514 | 28 | |
| α-helix | 523-525 | 3 | |
| β-strand | 526-532 | 7 | 2 |
| α-helix | 533-536 | 4 | |
| α-helix | 549-552 | 4 | |
| α-helix | 554-565 | 12 | |
| β-strand | 569-573 | 5 | 2 |
| β-strand | 579-585 | 7 | 2 |
| β-strand | 590-596 | 7 | 2 |
| α-helix | 597-603 | 7 | |
| α-helix | 604-606 | 3 | |
| β-strand | 614 | 1 | 9 |
| α-helix | 616-622 | 7 | |
| α-helix | 627-638 | 12 | |
| β-strand | 648-650 | 3 | 9 |
| β-strand | 666-668 | 3 | 9 |
| β-strand | 685-687 | 3 | 2 |
| α-helix | 701-725 | 25 | |
| β-strand | 728-730 | 3 | 10 |
| α-helix | 732-741 | 10 | |
| α-helix | 750-762 | 13 | |
| β-strand | 766-768 | 3 | 10 |
| β-strand | 775-778 | 4 | 10 |
Chain G: 7 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-16 | 14 | |
| β-strand | 22-25 | 4 | 6 |
| β-strand | 34-39 | 6 | 6 |
| β-strand | 51-56 | 6 | 6 |
| α-helix | 61-63 | 3 | |
| β-strand | 67-70 | 4 | 6 |
| β-strand | 79 | 1 | 7 |
| β-strand | 85 | 1 | 7 |
| α-helix | 92-94 | 3 | |
| α-helix | 101-113 | 13 | |
| α-helix | 123-131 | 9 | |
| α-helix | 135-138 | 4 | |
| α-helix | 141-143 | 3 | |
Chain H: 17 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 47-49 | 3 | |
| β-strand | 61-64 | 4 | 11 |
| α-helix | 66-84 | 19 | |
| α-helix | 88-97 | 10 | |
| α-helix | 102-111 | 10 | |
| α-helix | 115-119 | 5 | |
| α-helix | 124-125 | 2 | |
| α-helix | 166-175 | 10 | |
| β-strand | 182 | 1 | 12 |
| β-strand | 191 | 1 | 12 |
| α-helix | 194-196 | 3 | |
| α-helix | 204-221 | 18 | |
| β-strand | 225-226 | 2 | 11 |
| β-strand | 236-239 | 4 | 11 |
| β-strand | 246-247 | 2 | 13 |
| β-strand | 256-257 | 2 | 13 |
| α-helix | 271-278 | 8 | |
| α-helix | 286-293 | 8 | |
| β-strand | 295-296 | 2 | 5 |
| β-strand | 303-306 | 4 | 5 |
| β-strand | 312-314 | 3 | 14 |
| β-strand | 321-323 | 3 | 14 |
| α-helix | 354-380 | 27 | |
| α-helix | 383-398 | 16 | |
| α-helix | 404-407 | 4 | |
| α-helix | 410-432 | 23 | |
| α-helix | 438-462 | 25 | |
| α-helix | 469-487 | 19 | |
Chain N: 2 helices, 5 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-6 | 5 | 1 |
| β-strand | 12-16 | 5 | 1 |
| α-helix | 23-33 | 11 | |
| β-strand | 42-44 | 3 | 1 |
| β-strand | 49 | 1 | 1 |
| α-helix | 50-51 | 2 | |
| β-strand | 66-70 | 5 | 1 |
Chain R: 3 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 31-43 | 13 | 2 |
| β-strand | 49 | 1 | 3 |
| β-strand | 56 | 1 | 3 |
| α-helix | 60-61 | 2 | |
| α-helix | 62-66 | 5 | |
| β-strand | 75-78 | 4 | 4 |
| β-strand | 83-85 | 3 | 4 |
| α-helix | 86-92 | 7 | |
| β-strand | 108-111 | 4 | 4 |
Chain U: 3 helices, 5 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-6 | 5 | 5 |
| β-strand | 12-16 | 5 | 5 |
| α-helix | 23-33 | 11 | |
| α-helix | 38-40 | 3 | |
| β-strand | 41-44 | 4 | 5 |
| β-strand | 49 | 1 | 5 |
| α-helix | 57-59 | 3 | |
| β-strand | 66-73 | 8 | 5 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| NEDD8 | N | protein | 81 | Homo sapiens | Q15843 (AlphaFold model) |
| RING-box protein 2 | R | protein | 113 | Homo sapiens | Q9UBF6 (AlphaFold model) |
| Ubiquitin | U | protein | 75 | Homo sapiens | P0CG48 (AlphaFold model) |
| L3A2-1 | G | protein | 157 | synthetic construct | |
| Cullin-5 | C | protein | 780 | Homo sapiens | Q93034 (AlphaFold model) |
| E3 ubiquitin-protein ligase ARIH2 | H | protein | 493 | Homo sapiens | O95376 |
Sequence of entity 1 (N), FASTA
>9SDX_1 NEDD8 (chains N)
MLIKVKTLTGKEIEIDIEPTDKVERIKERVEEKEGIPPQQQRLIYSGKQMNDEKTAADYK
ILGGSVLHLVLALRGGGGLRQ
Sequence of entity 2 (R), FASTA
>9SDX_2 RING-box protein 2 (chains R)
MADVEDGEETCALASHSGSSGSKSGGDKMFSLKKWNAVAMWSWDVECDTCAICRVQVMDA
CLRCQAENKQEDCVVVWGECNHSFHNCCMSLWVKQNNRCPLCQQDWVVQRIGK
Sequence of entity 3 (U), FASTA
>9SDX_3 Ubiquitin (chains U)
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN
IQKESTLHLVLRLRG
Sequence of entity 4 (G), FASTA
>9SDX_4 L3A2-1 (chains G)
GSMVAASSRLMKELEEIRKAGMKNFRNIQVDEANLLTWQGLIVPDNPPYDKGAFRIEINF
PAEYPFKPPKITFKTKIYHPNIDEKGQVCLPVISAENWKPATKTDQVIQSLIALVNDPQP
EHPLRADLAEEYSKDRKKFAKNAEEFTKKYGEKRPVD
Sequence of entity 5 (C), FASTA
>9SDX_5 Cullin-5 (chains C)
MATSNLLKNKGSLQFEDKWDFMRPIVLKLLRQESVTKQQWFDLFSDVHAVCLWDDKGPAK
IHQALKEDILEFIKQAQARVLSHQDDTALLKAYIVEWRKFFTQCDILPKPFCQLEITLMG
KQGSNKKSNVEDSIVRKLMLDTWNESIFSNIKNRLQDSAMKLVHAERLGEAFDSQLVIGV
RESYVNLCSNPEDKLQIYRDNFEKAYLDSTERFYRTQAPSYLQQNGVQNYMKYADAKLKE
EEKRALRYLETRRECNSVEALMECCVNALVTSFKETILAECQGMIKRNETEKLHLMFSLM
DKVPNGIEPMLKDLEEHIISAGLADMVAAAETITTDSEKYVEQLLTLFNRFSKLVKEAFQ
DDPRFLTARDKAYKAVVNDATIFKLELPLKQKGVGLKTQPESKCPELLANYCDMLLRKTP
LSKKLTSEEIEAKLKEVLLVLKYVQNKDVFMRYHKAHLTRRLILDISADSEIEENMVEWL
REVGMPADYVNKLARMFQDIKVSEDLNQAFKEMHKNNKLALPADSVNIKILNAGAWSRSS
EKVFVSLPTELEDLIPEVEEFYKKNHSGRKLHWHHLMSNGIITFKNEVGQYDLEVTTFQL
AVLFAWNQRPREKISFENLKLATELPDAELRRTLWSLVAFPKLKRQVLLYEPQVNSPKDF
TEGTLFSVNQEFSLIKNAKVQKRGKINLIGRLQLTTERMREEENEGIVQLRILRTQEAII
QIMKMRKKISNAQLQTELVEILKNMFLPQKKMIKEQIEWLIEHKYIRRDESDINTFIYMA
Sequence of entity 6 (H), FASTA
>9SDX_6 E3 ubiquitin-protein ligase ARIH2 (chains H)
MSVDMNSQGSDSNEEDYDPNCEEEEEEEEDDPGDIEDYYVGVASDVEQQGADAFDPEEYQ
FTCLTYKESEGALNEHMTSLASVLKVSHSVAKLILVNFHWQVSEILDRYKSNSAQLLVEA
RVQPNPSKHVPTSHPPHHCAVCMQFVRKENLLSLACQHQFCRSCWEQHCSVLVKDGVGVG
VSCMAQDCPLRTPEDFVFPLLPNEELREKYRRYLFRDYVESHYQLQLCPGADCPMVIRVQ
EPRARRVQCNRCNEVFCFKCRQMYHAPTDCATIRKWLTKCADDSETANYISAHTKDCPKC
NICIEKNGGCNHMQCSKCKHDFCWMCLGDWKTHGSEYYECSRYKENPDIVNQSQQAQARE
ALKKYLFYFERWENHNKSLQLEAQTYQRIHEKIQERVMNNLGTWIDWQYLQNAAKLLAKC
RYTLQYTYPYAYYMESGPRKKLFEYQQAQLEAEIENLSWKVERADSYDRGDLENQMHIAE
QRRRTLLKDFHDT
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| SY8 | 5-azanylpentan-2-one | C5 H11 N O | 1 |
| ZN | Zinc ion | Zn | 7 |
Primary citation
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 Q15843 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 1NDD 1.6 Å, Structure of NEDD8
- 4FBJ 1.6 Å, Structure of the Cif:Nedd8 complex - Photorhabdus luminescens Cycle Inhibiting Factor in…
- 8WZN 1.8 Å, ParkinK211N in complex with phospho NEDD8
- 2BKR 1.9 Å, NEDD8 NEDP1 complex
- 4F8C 1.95 Å, Structure of the Cif:Nedd8 complex - Yersinia pseudotuberculosis Cycle Inhibiting Factor…
- 1XT9 2.2 Å, Crystal Structure of Den1 in complex with Nedd8
- 8WZO 2.25 Å, Parkin in complex with phospho NEDD8
- 4HCP 2.52 Å, crystal structure of Burkholderia pseudomallei effector protein chbp in complex with nedd8
- 8CAF 2.66 Å, N8C_Fab3b in complex with NEDD8-CUL1(WHB)
- 2NVU 2.8 Å, Structure of APPBP1-UBA3~NEDD8-NEDD8-MgATP-Ubc12(C111A), a trapped ubiquitin-like…
- 3DBH 2.85 Å, Structural Dissection of a Gating Mechanism Preventing Misactivation of Ubiquitin by…
- 3DBL 2.9 Å, Structural Dissection of a Gating Mechanism Preventing Misactivation of Ubiquitin by…
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