Cryo-EM structure of Ufd4 in complex with K29/48 triUb. Determined by electron microscopy at 3.31 Å resolution. Released 17 Apr 2024.
Explore 8J1P in 3D Show helices and sheets RCSB PDB PDBe
8J1P contains 83 α-helices and 45 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 | 165-180 | 16 | |
| α-helix | 181-183 | 3 | |
| α-helix | 188-201 | 14 | |
| α-helix | 205-209 | 5 | |
| α-helix | 214-226 | 13 | |
| α-helix | 234-250 | 17 | |
| α-helix | 254-259 | 6 | |
| α-helix | 263-272 | 10 | |
| α-helix | 277-291 | 15 | |
| α-helix | 295-301 | 7 | |
| α-helix | 311-313 | 3 | |
| α-helix | 317-329 | 13 | |
| α-helix | 335-337 | 3 | |
| α-helix | 338-353 | 16 | |
| α-helix | 358-361 | 4 | |
| α-helix | 364-375 | 12 | |
| α-helix | 387-395 | 9 | |
| α-helix | 404-419 | 16 | |
| α-helix | 423-430 | 8 | |
| α-helix | 435-443 | 9 | |
| α-helix | 453-459 | 7 | |
| α-helix | 462-474 | 13 | |
| β-strand | 485 | 1 | 1 |
| α-helix | 505-520 | 16 | |
| α-helix | 525-538 | 14 | |
| α-helix | 544-547 | 4 | |
| α-helix | 548-550 | 3 | |
| α-helix | 551-561 | 11 | |
| α-helix | 565-568 | 4 | |
| β-strand | 569 | 1 | 2 |
| β-strand | 575 | 1 | 2 |
| α-helix | 577-596 | 20 | |
| α-helix | 598-608 | 11 | |
| α-helix | 611-623 | 13 | |
| α-helix | 665-667 | 3 | |
| α-helix | 671-673 | 3 | |
| β-strand | 680 | 1 | 1 |
| α-helix | 682-684 | 3 | |
| α-helix | 685-701 | 17 | |
| α-helix | 713-725 | 13 | |
| α-helix | 734-748 | 15 | |
| β-strand | 749 | 1 | 3 |
| β-strand | 754 | 1 | 3 |
| α-helix | 757-762 | 6 | |
| α-helix | 765-775 | 11 | |
| α-helix | 780-790 | 11 | |
| α-helix | 795-809 | 15 | |
| α-helix | 812-815 | 4 | |
| α-helix | 825-827 | 3 | |
| β-strand | 831-835 | 5 | 4 |
| β-strand | 837-838 | 2 | 5 |
| β-strand | 855-859 | 5 | 4 |
| β-strand | 863 | 1 | 6 |
| α-helix | 864-875 | 12 | |
| α-helix | 906-909 | 4 | |
| β-strand | 913 | 1 | 7 |
| β-strand | 926 | 1 | 6 |
| α-helix | 929-937 | 9 | |
| α-helix | 942-947 | 6 | |
| β-strand | 950 | 1 | 4 |
| β-strand | 953-954 | 2 | 5 |
| β-strand | 955 | 1 | 7 |
| α-helix | 975-976 | 2 | |
| α-helix | 979-981 | 3 | |
| α-helix | 992-994 | 3 | |
| α-helix | 995-1005 | 11 | |
| α-helix | 1017-1027 | 11 | |
| α-helix | 1030-1033 | 4 | |
| α-helix | 1040-1048 | 9 | |
| α-helix | 1055-1066 | 12 | |
| α-helix | 1069-1071 | 3 | |
| β-strand | 1100-1105 | 6 | 8 |
| α-helix | 1107-1109 | 3 | |
| α-helix | 1110-1121 | 12 | |
| β-strand | 1127-1132 | 6 | 8 |
| α-helix | 1140-1153 | 14 | |
| β-strand | 1156 | 1 | 9 |
| α-helix | 1157-1159 | 3 | |
| β-strand | 1162 | 1 | 10 |
| β-strand | 1181 | 1 | 9 |
| β-strand | 1188 | 1 | 10 |
| α-helix | 1200-1216 | 17 | |
| α-helix | 1227-1237 | 11 | |
| α-helix | 1249-1255 | 7 | |
| α-helix | 1260-1271 | 12 | |
| α-helix | 1276-1282 | 7 | |
| β-strand | 1287 | 1 | 11 |
| β-strand | 1295 | 1 | 11 |
| α-helix | 1310-1321 | 12 | |
| α-helix | 1327-1340 | 14 | |
| α-helix | 1343-1348 | 6 | |
| α-helix | 1351-1353 | 3 | |
| α-helix | 1355 | 1 | |
| α-helix | 1356-1360 | 5 | |
| α-helix | 1361-1364 | 4 | |
| α-helix | 1367-1371 | 5 | |
| α-helix | 1388-1394 | 7 | |
| α-helix | 1399-1409 | 11 | |
| α-helix | 1420-1422 | 3 | |
| β-strand | 1429-1432 | 4 | 12 |
| β-strand | 1446 | 1 | 12 |
| β-strand | 1454-1457 | 4 | 12 |
| α-helix | 1462-1476 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-6 | 3 | 13 |
| β-strand | 12-14 | 3 | 13 |
| β-strand | 22 | 1 | 14 |
| α-helix | 23-34 | 12 | |
| α-helix | 38-40 | 3 | |
| β-strand | 42-44 | 3 | 13 |
| β-strand | 49 | 1 | 13 |
| β-strand | 55 | 1 | 14 |
| β-strand | 66-70 | 5 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-6 | 3 | 15 |
| β-strand | 12-14 | 3 | 15 |
| α-helix | 24-33 | 10 | |
| α-helix | 38-40 | 3 | |
| β-strand | 42-45 | 4 | 15 |
| β-strand | 48-49 | 2 | 15 |
| β-strand | 66-70 | 5 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-6 | 5 | 16 |
| β-strand | 12-16 | 5 | 16 |
| β-strand | 22 | 1 | 17 |
| α-helix | 25-33 | 9 | |
| α-helix | 38-40 | 3 | |
| β-strand | 42-44 | 3 | 16 |
| β-strand | 49 | 1 | 16 |
| β-strand | 55 | 1 | 17 |
| β-strand | 66-70 | 5 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ubiquitin fusion degradation protein 4 | A | protein | 1483 | Saccharomyces cerevisiae | P33202 (AlphaFold model) |
| Ubiquitin | C, E | protein | 76 | Homo sapiens | P0CG47 (AlphaFold model) |
| Ubiquitin | D | protein | 76 | Homo sapiens | P0CG47 (AlphaFold model) |
>8J1P_1 Ubiquitin fusion degradation protein 4 (chains A) MSENNSHNLDEHESHSENSDYMMDTQVEDDYDEDGHVQGEYSYYPDEDEDEHMLSSVGSF EADDGEDDDNDYHHEDDSGLLYGYHRTQNGSDEDRNEEEDGLERSHDNNEFGSNPLHLPD ILETFAQRLEQRRQTSEGLGQHPVGRTLPEILSMIGGRMERSAESSARNERISKLIENTG NASEDPYIAMESLKELSENILMMNQMVVDRIIPMETLIGNIAAILSDKILREELELQMQA CRCMYNLFEVCPESISIAVDEHVIPILQGKLVEISYIDLAEQVLETVEYISRVHGRDILK TGQLSIYVQFFDFLTIHAQRKAIAIVSNACSSIRTDDFKTIVEVLPTLKPIFSNATDQPI LTRLVNAMYGICGALHGVDKFETLFSLDLIERIVQLVSIQDTPLENKLKCLDILTVLAMS SDVLSRELREKTDIVDMATRSFQHYSKSPNAGLHETLIYVPNSLLISISRFIVVLFPPED ERILSADKYTGNSDRGVISNQEKFDSLVQCLIPILVEIYTNAADFDVRRYVLIALLRVVS CINNSTAKAINDQLIKLIGSILAQKETASNANGTYSSEAGTLLVGGLSLLDLICKKFSEL FFPSIKREGIFDLVKDLSVDFNNIDLKEDGNENISLSDEEGDLHSSIEECDEGDEEYDYE FTDMEIPDSVKPKKISIHIFRTLSLAYIKNKGVNLVNRVLSQMNVEQEAITEELHQIEGV VSILENPSTPDKTEEDWKGIWSVLKKCIFHEDFDVSGFEFTSTGLASSITKRITSSTVSH FILAKSFLEVFEDCIDRFLEILQSALTRLENFSIVDCGLHDGGGVSSLAKEIKIKLVYDG DASKDNIGTDLSSTIVSVHCIASFTSLNEFLRHRMVRMRFLNSLIPNLTSSSTEADREEE ENCLDHMRKKNFDFFYDNEKVDMESTVFGVIFNTFVRRNRDLKTLWDDTHTIKFCKSLEG NNRESEAAEEANEGKKLRDFYKKREFAQVDTGSSADILTLLDFLHSCGVKSDSFINSKLS AKLARQLDEPLVVASGALPDWSLFLTRRFPFLFPFDTRMLFLQCTSFGYGRLIQLWKNKS KGSKDLRNDEALQQLGRITRRKLRISRKTIFATGLKILSKYGSSPDVLEIEYQEEAGTGL GPTLEFYSVVSKYFARKSLNMWRCNSYSYRSEMDVDTTDDYITTLLFPEPLNPFSNNEKV IELFGYLGTFVARSLLDNRILDFRFSKVFFELLHRMSTPNVTTVPSDVETCLLMIELVDP LLAKSLKYIVANKDDNMTLESLSLTFTVPGNDDIELIPGGCNKSLNSSNVEEYIHGVIDQ ILGKGIEKQLKAFIEGFSKVFSYERMLILFPDELVDIFGRVEEDWSMATLYTNLNAEHGY TMDSSIIHDFISIISAFGKHERRLFLQFLTGSPKLPIGGFKSLNPKFTVVLKHAEDGLTA DEYLPSVMTCANYLKLPKYTSKDIMRSRLCQAIEEGAGAFLLS
>8J1P_2 Ubiquitin (chains C, E) MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN IQKESTLHLVLRLRGG
>8J1P_3 Ubiquitin (chains D) MQIFVKTLTGKTITLEVEPSDTIENVKACIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN IQKESTLHLVLRLRGG
Structural visualization of HECT-type E3 ligase Ufd4 accepting and transferring ubiquitin to form K29/K48-branched polyubiquitination. Wu, X., Ai, H., Mao, J. et al. Nat Commun (2025) 16:4313-4313. DOI 10.1038/s41467-025-59569-6 · PubMed
Other PDB entries of the same protein (UniProt P33202 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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