PSMD2 Structure bound to MC1 and Fab8/14. Determined by electron microscopy at 2.5 Å resolution. Released 11 Jan 2023.
Explore 7UJD in 3D Show helices and sheets RCSB PDB PDBe
7UJD contains 38 α-helices and 24 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 | 262-272 | 11 | |
| α-helix | 275-282 | 8 | |
| α-helix | 288-301 | 14 | |
| α-helix | 314-321 | 8 | |
| α-helix | 326-337 | 12 | |
| α-helix | 345-348 | 4 | |
| α-helix | 368-381 | 14 | |
| α-helix | 396-399 | 4 | |
| α-helix | 405-417 | 13 | |
| α-helix | 422-429 | 8 | |
| α-helix | 430-434 | 5 | |
| α-helix | 438-450 | 13 | |
| α-helix | 461-466 | 6 | |
| α-helix | 475-488 | 14 | |
| α-helix | 495-501 | 7 | |
| α-helix | 502-505 | 4 | |
| α-helix | 512-525 | 14 | |
| α-helix | 532-544 | 13 | |
| α-helix | 553-556 | 4 | |
| α-helix | 557-565 | 9 | |
| α-helix | 570-573 | 4 | |
| α-helix | 574-579 | 6 | |
| α-helix | 580-582 | 3 | |
| α-helix | 585-599 | 15 | |
| α-helix | 606-612 | 7 | |
| α-helix | 650-661 | 12 | |
| α-helix | 665-681 | 17 | |
| α-helix | 686-689 | 4 | |
| α-helix | 690-697 | 8 | |
| α-helix | 704-713 | 10 | |
| α-helix | 719-732 | 14 | |
| α-helix | 739-751 | 13 | |
| α-helix | 756-769 | 14 | |
| α-helix | 771-774 | 4 | |
| β-strand | 776-777 | 2 | 1 |
| β-strand | 781-782 | 2 | 2 |
| β-strand | 787-788 | 2 | 2 |
| α-helix | 790-803 | 14 | |
| α-helix | 809-813 | 5 | |
| α-helix | 815-824 | 10 | |
| β-strand | 826-827 | 2 | 1 |
| β-strand | 829-830 | 2 | 3 |
| β-strand | 831-833 | 3 | 4 |
| β-strand | 839 | 1 | 4 |
| β-strand | 843-847 | 5 | 5 |
| β-strand | 866-869 | 4 | 5 |
| β-strand | 872-873 | 2 | 3 |
| β-strand | 879-882 | 4 | 5 |
| β-strand | 888-889 | 2 | 6 |
| β-strand | 897-899 | 3 | 4 |
| β-strand | 900-901 | 2 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 37 | 1 | 7 |
| β-strand | 54-55 | 2 | 7 |
| α-helix | 56-58 | 3 | |
| β-strand | 60-61 | 2 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 32 | 1 | 8 |
| β-strand | 93 | 1 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 37 | 1 | 9 |
| β-strand | 54-55 | 2 | 9 |
| β-strand | 60-61 | 2 | 9 |
| β-strand | 103 | 1 | 10 |
| β-strand | 106 | 1 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 26S proteasome non-ATPase regulatory subunit 2 | A | protein | 644 | Homo sapiens | Q13200 (AlphaFold model) |
| Fab 14 LC CDRs | C | protein | 217 | Homo sapiens | |
| Fab 14 HC CDRs | D | protein | 231 | Homo sapiens | |
| Fab 8 LC CDRs | E | protein | 217 | Homo sapiens | |
| Fab 8 HC CDRs | F | protein | 229 | Homo sapiens | |
| Acy-phe-pro-asp-val-sar-leu-his-arg-tyr-trp-gly-trp-asp-cys-gly-NH2 | Z | protein | 17 | synthetic construct |
>7UJD_1 26S proteasome non-ATPase regulatory subunit 2 (chains A) SRFPEALRLALMLNDMELVEDIFTSCKDVVVQKQMAFMLGRHGVFLELSEDVEEYEDLTE IMSNVQLNSNFLALARELDIMEPKVPDDIYKTHLENNRFGGSGSQVDSARMNLASSFVNG FVNAAFGQDKLLTDDGNKWLYKNKDHGMLSAAASLGMILLWDVDGGLTQIDKYLYSSEDY IKSGALLACGIVNSGVRNECDPALALLSDFVLHNSNTMRLGSIFGLGLAYAGSNREDVLT LLLPVMGDSKSSMEVAGVTALACGMIAVGSCNGDVTSTILQTIMEKSETELKDTYARWLP LGLGLNHLGKGEAIEAILAALEVVSEPFRSFANTLVDVCAYAGSGNVLKVQQLLHICSEH FDSKEKEEDKDKKEKKDKDKKEAPADMGAHQGVAVLGIALIAMGEEIGAEMALRTFGHLL RYGEPTLRRAVPLALALISVSNPRLNILDTLSKFSHDADPEVSYNSIFAMGMVGSGTNNA RLAAMLRQLAQYHAKDPNNLFMVRLAQGLTHLGKGTLTLCPYHSDRQLMSQVAVAGLLTV LVSFLDVRNIILGKSHYVLYGLVAAMQPRMLVTFDEELRPLPVSVRVGQAVDVVGQAGKP KTITGFQTHTTPVLLAHGERAELATEEFLPVTPILEGFVILRKN
>7UJD_2 Fab 14 LC CDRs (chains C) SDIQMTQSPSSLSASVGDRVTITCRASQSVSSAVAWYQQKPGKAPKLLIYSASSLYSGVP SRFSGSRSGTDFTLTISSLQPEDFATYYCQQYYSYYYPVTFGQGTKVEIKRTVAAPSVFI FPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSS TLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
>7UJD_3 Fab 14 HC CDRs (chains D) EISEVQLVESGGGLVQPGGSLRLSCAASGFNVYYYSIHWVRQAPGKGLEWVASIYPYYSY TSYADSVKGRFTISADTSKNTAYLQMNSLRAEDTAVYYCARYQSSSYGYGLDYWGQGTLV TVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAV LQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTH
>7UJD_4 Fab 8 LC CDRs (chains E) SDIQMTQSPSSLSASVGDRVTITCRASQSVSSAVAWYQQKPGKAPKLLIYSASSLYSGVP SRFSGSRSGTDFTLTISSLQPEDFATYYCQQYYYSSSLVTFGQGTKVEIKRTVAAPSVFI FPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSS TLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
>7UJD_5 Fab 8 HC CDRs (chains F) EISEVQLVESGGGLVQPGGSLRLSCAASGFNFSSYSMHWVRQAPGKGLEWVAYIYPYSSY TYYADSVKGRFTISADTSKNTAYLQMNSLRAEDTAVYYCARKYQWRGALDYWGQGTLVTV SSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQ SSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTH
>7UJD_6 ACY-PHE-PRO-ASP-VAL-SAR-LEU-HIS-ARG-TYR-TRP-GLY-TRP-ASP-CYS-GLY-NH2 (chains Z) XFPDVGLHRYWGWDCGX
Targeted degradation via direct 26S proteasome recruitment. Bashore, C., Prakash, S., Johnson, M.C. et al. Nat Chem Biol (2023) 19:55-63. DOI 10.1038/s41589-022-01218-w · PubMed
Other PDB entries of the same protein (UniProt Q13200 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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