Cryo-EM structure of a single loaded human UBA7-UBE2L6-ISG15 adenylate complex. Determined by electron microscopy at 3.24 Å resolution. Released 11 Oct 2023.
Explore 8SEB in 3D Show helices and sheets RCSB PDB PDBe
8SEB contains 69 α-helices and 61 β-strands across 3 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 | 25-32 | 8 | |
| β-strand | 34-38 | 5 | 1 |
| α-helix | 42-54 | 13 | |
| β-strand | 58-62 | 5 | 1 |
| β-strand | 66 | 1 | 2 |
| α-helix | 67 | 1 | |
| α-helix | 69-71 | 3 | |
| α-helix | 80-82 | 3 | |
| β-strand | 86 | 1 | 2 |
| α-helix | 87-98 | 12 | |
| β-strand | 103-106 | 4 | 1 |
| α-helix | 116-118 | 3 | |
| β-strand | 121-124 | 4 | 1 |
| α-helix | 129-142 | 14 | |
| β-strand | 145-147 | 3 | 1 |
| β-strand | 150-152 | 3 | 3 |
| β-strand | 155-159 | 5 | 3 |
| β-strand | 160-161 | 2 | 1 |
| β-strand | 166-168 | 3 | 4 |
| β-strand | 170 | 1 | 5 |
| α-helix | 175-177 | 3 | |
| β-strand | 178-183 | 6 | 6 |
| β-strand | 191-192 | 2 | 7 |
| β-strand | 193-194 | 2 | 6 |
| α-helix | 199-202 | 4 | |
| β-strand | 208-216 | 9 | 6 |
| β-strand | 226-227 | 2 | 6 |
| β-strand | 229-230 | 2 | 7 |
| α-helix | 232-234 | 3 | |
| β-strand | 236-237 | 2 | 7 |
| α-helix | 245-246 | 2 | |
| β-strand | 247-256 | 10 | 6 |
| α-helix | 257-259 | 3 | |
| β-strand | 260-262 | 3 | 4 |
| α-helix | 267-272 | 6 | |
| β-strand | 276 | 1 | 3 |
| α-helix | 281-304 | 24 | |
| α-helix | 307-309 | 3 | |
| α-helix | 313-325 | 13 | |
| α-helix | 328-330 | 3 | |
| α-helix | 343-352 | 10 | |
| α-helix | 358-377 | 20 | |
| β-strand | 379 | 1 | 5 |
| α-helix | 381-383 | 3 | |
| β-strand | 386-390 | 5 | 3 |
| α-helix | 392-394 | 3 | |
| α-helix | 396-397 | 2 | |
| α-helix | 401-403 | 3 | |
| α-helix | 416-422 | 7 | |
| α-helix | 424-431 | 8 | |
| β-strand | 436-438 | 3 | 8 |
| α-helix | 442-454 | 13 | |
| β-strand | 464-467 | 4 | 8 |
| β-strand | 471 | 1 | 9 |
| β-strand | 491 | 1 | 9 |
| α-helix | 492-503 | 12 | |
| β-strand | 509-512 | 4 | 8 |
| α-helix | 518-520 | 3 | |
| α-helix | 526-529 | 4 | |
| β-strand | 535-538 | 4 | 8 |
| α-helix | 542-555 | 14 | |
| β-strand | 559-565 | 7 | 8 |
| β-strand | 568-574 | 7 | 8 |
| α-helix | 586-592 | 7 | |
| α-helix | 598-603 | 6 | |
| α-helix | 608-619 | 12 | |
| α-helix | 620-625 | 6 | |
| α-helix | 626-628 | 3 | |
| α-helix | 629-633 | 5 | |
| α-helix | 634-636 | 3 | |
| α-helix | 645-652 | 8 | |
| α-helix | 653-655 | 3 | |
| α-helix | 670-677 | 8 | |
| α-helix | 678-683 | 6 | |
| α-helix | 684-691 | 8 | |
| α-helix | 722-739 | 18 | |
| α-helix | 750-756 | 7 | |
| α-helix | 762-764 | 3 | |
| α-helix | 784-798 | 15 | |
| α-helix | 806-808 | 3 | |
| α-helix | 813-815 | 3 | |
| α-helix | 817-831 | 15 | |
| α-helix | 834-838 | 5 | |
| α-helix | 839-842 | 4 | |
| α-helix | 849-853 | 5 | |
| α-helix | 854-871 | 18 | |
| β-strand | 883-887 | 5 | 8 |
| β-strand | 892-896 | 5 | 8 |
| α-helix | 897-901 | 5 | |
| β-strand | 904-906 | 3 | 10 |
| β-strand | 909-911 | 3 | 10 |
| β-strand | 917-920 | 4 | 11 |
| α-helix | 926 | 1 | |
| β-strand | 927 | 1 | 12 |
| α-helix | 928-939 | 12 | |
| β-strand | 943-948 | 6 | 13 |
| β-strand | 951-955 | 5 | 13 |
| α-helix | 960-966 | 7 | |
| β-strand | 970 | 1 | 12 |
| α-helix | 971-979 | 9 | |
| β-strand | 989-992 | 4 | 11 |
| β-strand | 993-996 | 4 | 13 |
| α-helix | 1005-1007 | 3 | |
| β-strand | 1008-1011 | 4 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 82-87 | 6 | 14 |
| β-strand | 93-98 | 6 | 14 |
| β-strand | 103 | 1 | 15 |
| α-helix | 104-115 | 12 | |
| α-helix | 119-121 | 3 | |
| β-strand | 122-126 | 5 | 14 |
| β-strand | 129-130 | 2 | 14 |
| β-strand | 136 | 1 | 15 |
| α-helix | 137-140 | 4 | |
| β-strand | 147-152 | 6 | 14 |
| β-strand | 156 | 1 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-15 | 13 | |
| β-strand | 22-27 | 6 | 16 |
| β-strand | 34-39 | 6 | 16 |
| α-helix | 46-48 | 3 | |
| β-strand | 50 | 1 | 17 |
| β-strand | 51-56 | 6 | 16 |
| α-helix | 65-66 | 2 | |
| β-strand | 67-70 | 4 | 16 |
| β-strand | 79 | 1 | 18 |
| β-strand | 84 | 1 | 16 |
| β-strand | 85 | 1 | 18 |
| α-helix | 101-113 | 13 | |
| α-helix | 123-131 | 9 | |
| α-helix | 133-147 | 15 | |
| β-strand | 149 | 1 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ubiquitin-like modifier-activating enzyme 7 | A | protein | 1012 | Homo sapiens | P41226 (AlphaFold model) |
| Ubiquitin-like protein ISG15 | B | protein | 157 | Homo sapiens | P05161 (AlphaFold model) |
| Ubiquitin/ISG15-conjugating enzyme E2 L6 | C | protein | 152 | Homo sapiens | O14933 (AlphaFold model) |
>8SEB_1 Ubiquitin-like modifier-activating enzyme 7 (chains A) MDALDASKLLDEELYSRQLYVLGSPAMQRIQGARVLVSGLQGLGAEVAKNLVLMGVGSLT LHDPHPTCWSDLAAQFLLSEQDLERSRAEASQELLAQLNRAVQVVVHTGDITEDLLLDFQ VVVLTAAKLEEQLKVGTLCHKHGVCFLAADTRGLVGQLFCDFGEDFTVQDPTEAEPLTAA IQHISQGSPGILTLRKGANTHYFRDGDLVTFSGIEGMVELNDCDPRSIHVREDGSLEIGD TTTFSRYLRGGAITEVKRPKTVRHKSLDTALLQPHVVAQSSQEVHHAHCLHQAFCALHKF QHLHGRPPQPWDPVDAETVVGLARDLEPLKRTEEEPLEEPLDEALVRTVALSSAGVLSPM VAMLGAVAAQEVLKAISRKFMPLDQWLYFDALDCLPEDGELLPSPEDCALRGSRYDGQIA VFGAGFQEKLRRQHYLLVGAGAIGCELLKVFALVGLGAGNSGGLTVVDMDHIERSNLSRQ FLFRSQDVGRPKAEVAAAAARGLNPDLQVIPLTYPLDPTTEHIYGDNFFSRVDGVAAALD SFQARRYVAARCTHYLKPLLEAGTSGTWGSATVFMPHVTEAYRAPASAAASEDAPYPVCT VRYFPSTAEHTLQWARHEFEELFRLSAETINHHQQAHTSLADMDEPQTLTLLKPVLGVLR VRPQNWQDCVAWALGHWKLCFHYGIKQLLRHFPPNKVLEDGTPFWSGPKQCPQPLEFDTN QDTHLLYVLAAANLYAQMHGLPGSQDWTALRELLKLLPQPDPQQMAPIFASNLELASASA EFGPEQQKELNKALEVWSVGPPLKPLMFEKDDDSNFHVDFVVAAASLRCQNYGIPPVNRA QSKRIVGQIIPAIATTTAAVAGLLGLELYKVVSGPRPRSAFRHSYLHLAENYLIRYMPFA PAIQTFHHLKWTSWDRLKVPAGQPERTLESLLAHLQEQHGLRVRILLHGSALLYAAGWSP EKQAQHLPLRVTELVQQLTGQAPAPGQRVLVLELSCEGDDEDTAFPPLHYEL
>8SEB_2 Ubiquitin-like protein ISG15 (chains B) MGWDLTVKMLAGNEFQVSLSSSMSVSELKAQITQKIGVHAFQQRLAVHPSGVALQDRVPL ASQGLGPGSTVLLVVDKSDEPLSILVRNNKGRSSTYEVRLTQTVAHLKQQVSGLEGVQDD LFWLTFEGKPLEDQLPLGEYGLKPLSTVFMNLRLRGG
>8SEB_3 Ubiquitin/ISG15-conjugating enzyme E2 L6 (chains C) MASMRVVKELEDLQKKPPPYLRNLSSDDANVLVWHALLLPDQPPYHLKAFNLRISFPPEY PFKPPMIKFTTKIYHPNVDENGQICLPIISSENWKPSTKTSQVLEALNVLVNRPNIREPK RMDLADLLTQNPELFRKNAEEFTLRFGVDRPS
| ID | Name | Formula | Copies |
|---|---|---|---|
| AMP | Adenosine monophosphate | C10 H14 N5 O7 P | 1 |
Cryo-EM structures of Uba7 reveal the molecular basis for ISG15 activation and E1-E2 thioester transfer. Afsar, M., Liu, G., Jia, L. et al. Nat Commun (2023) 14:4786-4786. DOI 10.1038/s41467-023-39780-z · PubMed
Other PDB entries of the same protein (UniProt P41226 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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