Cryo-EM structure of neddylated PCMTD1-ELOBC-CUL5-RBX2 (N8-CRL5-PCMTD1). Determined by electron microscopy at 9.72 Å resolution. Released 4 Jun 2025.
Explore 9OMF in 3D Show helices and sheets RCSB PDB PDBe
9OMF contains 64 α-helices and 46 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 12-20 | 9 | |
| α-helix | 28-35 | 8 | |
| α-helix | 37 | 1 | |
| α-helix | 49-51 | 3 | |
| β-strand | 58 | 1 | 1 |
| β-strand | 61 | 1 | 1 |
| α-helix | 67-75 | 9 | |
| β-strand | 83-87 | 5 | 2 |
| α-helix | 93-101 | 9 | |
| β-strand | 107-112 | 6 | 2 |
| α-helix | 115-131 | 17 | |
| α-helix | 135-137 | 3 | |
| β-strand | 144-147 | 4 | 2 |
| β-strand | 160-165 | 6 | 2 |
| β-strand | 168 | 1 | 3 |
| β-strand | 169 | 1 | 2 |
| α-helix | 171-173 | 3 | |
| α-helix | 175-178 | 4 | |
| β-strand | 181-191 | 11 | 2 |
| β-strand | 194-200 | 7 | 2 |
| β-strand | 206-213 | 8 | 2 |
| α-helix | 217 | 1 | |
| β-strand | 218 | 1 | 3 |
| α-helix | 219 | 1 | |
| α-helix | 243-262 | 20 | |
| α-helix | 332-335 | 4 | |
| α-helix | 343-349 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 23-30 | 8 | |
| α-helix | 37-52 | 16 | |
| α-helix | 57-81 | 25 | |
| α-helix | 86-103 | 18 | |
| α-helix | 134-146 | 13 | |
| α-helix | 148-166 | 19 | |
| α-helix | 175-186 | 12 | |
| α-helix | 197-198 | 2 | |
| α-helix | 199-204 | 6 | |
| α-helix | 205-217 | 13 | |
| α-helix | 219-222 | 4 | |
| α-helix | 227-248 | 22 | |
| α-helix | 257-266 | 10 | |
| α-helix | 267-271 | 5 | |
| α-helix | 272-286 | 15 | |
| α-helix | 293-300 | 8 | |
| α-helix | 304-333 | 30 | |
| α-helix | 337-358 | 22 | |
| α-helix | 363-373 | 11 | |
| α-helix | 407-416 | 10 | |
| β-strand | 417 | 1 | 4 |
| α-helix | 420-424 | 5 | |
| α-helix | 427-441 | 15 | |
| β-strand | 446 | 1 | 5 |
| α-helix | 448-464 | 17 | |
| β-strand | 467 | 1 | 4 |
| α-helix | 470-483 | 14 | |
| α-helix | 487-490 | 4 | |
| α-helix | 492-511 | 20 | |
| α-helix | 523-525 | 3 | |
| β-strand | 526-532 | 7 | 6 |
| α-helix | 533-535 | 3 | |
| α-helix | 549-552 | 4 | |
| α-helix | 555-565 | 11 | |
| β-strand | 570-573 | 4 | 6 |
| β-strand | 579-585 | 7 | 6 |
| β-strand | 590-596 | 7 | 6 |
| α-helix | 597-607 | 11 | |
| β-strand | 614-615 | 2 | 7 |
| α-helix | 616-623 | 8 | |
| α-helix | 627-638 | 12 | |
| β-strand | 648-650 | 3 | 7 |
| α-helix | 657-659 | 3 | |
| β-strand | 665-668 | 4 | 7 |
| β-strand | 675-676 | 2 | 8 |
| β-strand | 679-680 | 2 | 8 |
| β-strand | 685-687 | 3 | 6 |
| α-helix | 690-693 | 4 | |
| α-helix | 698-725 | 28 | |
| β-strand | 728-730 | 3 | 9 |
| α-helix | 731-741 | 11 | |
| α-helix | 742-744 | 3 | |
| β-strand | 746 | 1 | 5 |
| α-helix | 750-762 | 13 | |
| β-strand | 767-769 | 3 | 9 |
| β-strand | 772-777 | 6 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 34-42 | 9 | 6 |
| α-helix | 62-64 | 3 | |
| β-strand | 75-76 | 2 | 10 |
| β-strand | 84-85 | 2 | 10 |
| α-helix | 89-92 | 4 | |
| β-strand | 98 | 1 | 11 |
| β-strand | 105 | 1 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-9 | 7 | 12 |
| β-strand | 10 | 1 | 13 |
| β-strand | 12-18 | 7 | 12 |
| α-helix | 24-35 | 12 | |
| β-strand | 46 | 1 | 14 |
| β-strand | 49 | 1 | 14 |
| β-strand | 52 | 1 | 15 |
| β-strand | 54 | 1 | 15 |
| α-helix | 64-66 | 3 | |
| α-helix | 72 | 1 | |
| β-strand | 73-75 | 3 | 12 |
| β-strand | 90 | 1 | 13 |
| α-helix | 91-96 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-6 | 5 | 12 |
| β-strand | 12-16 | 5 | 12 |
| α-helix | 17-20 | 4 | |
| α-helix | 24-28 | 5 | |
| β-strand | 43-45 | 3 | 12 |
| α-helix | 51-66 | 16 | |
| α-helix | 84-91 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein-L-isoaspartate O-methyltransferase domain-containing protein 1 | A | protein | 358 | Homo sapiens | Q96MG8 (AlphaFold model) |
| Cullin-5 | B | protein | 783 | Homo sapiens | Q93034 (AlphaFold model) |
| RING-box protein 2 | C | protein | 113 | Mus musculus | Q9WTZ1 (AlphaFold model) |
| Elongin-B | D | protein | 118 | Homo sapiens | Q15370 (AlphaFold model) |
| Elongin-C | E | protein | 96 | Homo sapiens | Q15369 |
>9OMF_1 Protein-L-isoaspartate O-methyltransferase domain-containing protein 1 (chains A) SMGGAVSAGEDNDDLIDNLKEAQYIRTERVEQAFRAIDRGDYYLEGYRDNAYKDLAWKHG NIHLSAPCIYSEVMEALKLQPGLSFLNLGSGTGYLSTMVGLILGPFGINHGIELHSDVVE YAKEKLESFIKNSDSFDKFEFCEPAFVVGNCLQIASDSHQYDRIYCGAGVQKDHENYMKI LLKVGGILVMPIEDQLTQIMRTGQNTWESKNILAVSFAPLVQPSKNDNGKPDSVGLPPCA VRNLQDLARIYIRRTLRNFINDEMQAKGIPQRAPPKRKRKRVKQRINTYVFVGNQLIPQP LDSEEDEKMEEDIKEEEEKDHNEAMKPEEPPQNLLREKIMKLPLPESLKAYLTYFRDK
>9OMF_2 Cullin-5 (chains B) GEFMATSNLLKNKGSLQFEDKWDFMRPIVLKLLRQESVTKQQWFDLFSDVHAVCLWDDKG PAKIHQALKEDILEFIKQAQARVLSHQDDTALLKAYIVEWRKFFTQCDILPKPFCQLEIT LMGKQGSNKKSNVEDSIVRKLMLDTWNESIFSNIKNRLQDSAMKLVHAERLGEAFDSQLV IGVRESYVNLCSNPEDKLQIYRDNFEKAYLDSTERFYRTQAPSYLQQNGVQNYMKYADAK LKEEEKRALRYLETRRECNSVEALMECCVNALVTSFKETILAECQGMIKRNETEKLHLMF SLMDKVPNGIEPMLKDLEEHIISAGLADMVAAAETITTDSEKYVEQLLTLFNRFSKLVKE AFQDDPRFLTARDKAYKAVVNDATIFKLELPLKQKGVGLKTQPESKCPELLANYCDMLLR KTPLSKKLTSEEIEAKLKEVLLVLKYVQNKDVFMRYHKAHLTRRLILDISADSEIEENMV EWLREVGMPADYVNKLARMFQDIKVSEDLNQAFKEMHKNNKLALPADSVNIKILNAGAWS RSSEKVFVSLPTELEDLIPEVEEFYKKNHYGRKLHWHHLMSNGIITFKNEVGQYDLEVTT FQLAVLFAWNQRPREKISFENVKLATELPDAELRRTLWSLVAFPKLKRQVLLYEPQVNSP KDFTEGTLFSVNQEFSLIKNAKVQKRGKINLIGRLQLTTERMREEENEGIVQLRILRTQE AIIQIMKMRKKISNAQLQTELVEILKNMFLPQKKMIKEQIEWLIEHKYILRDESDINTFI YMA
>9OMF_3 RING-box protein 2 (chains C) MADVEDGEEPCVLSSHSGSAGSKSGGDKMFSLKKWNAVAMWSWDVECDTCAICRVQVMDA CLRCQAENKQEDCVVVWGECNHSFHNCCMSLWVKQNNRCPLCQQDWVVQRIGK
>9OMF_4 Elongin-B (chains D) MDVFLMIRRHKTTIFTDAKESSTVFELKRIVEGILKRPPDEQRLYKDDQLLDDGKTLGEC GFTSQTARPQAPATVGLAFRADDTFEALCIEPFSSPPELPDVMKPQDSGSSANEQAVQ
>9OMF_5 Elongin-C (chains E) MYVKLISSDGHEFIVKREHALTSGTIKAMLSGPGQFAENETNEVNFREIPSHVLSKVCMY FTYKVRYTNSSTEIPEFPIAPEIALELLMAANFLDC
Structural basis for L-isoaspartyl-containing protein recognition by the human PCMTD1 cullin-RING E3 ubiquitin ligase. Pang, E.Z., Zhao, B., Flowers, C. et al. J Biol Chem (2025) 301:110735-110735. DOI 10.1016/j.jbc.2025.110735 · PubMed
Other PDB entries of the same protein (UniProt Q96MG8 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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