Uba1 in complex with ATP. Determined by X-ray diffraction at 1.72 Å resolution. Released 31 Aug 2022.
Explore 7ZH9 in 3D Show helices and sheets RCSB PDB PDBe
7ZH9 contains 66 α-helices and 50 β-strands across 1 chain. 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 | 16-26 | 11 | |
| α-helix | 28-34 | 7 | |
| β-strand | 38-42 | 5 | 1 |
| α-helix | 46-58 | 13 | |
| β-strand | 62-66 | 5 | 1 |
| β-strand | 70 | 1 | 2 |
| α-helix | 71 | 1 | |
| α-helix | 73-77 | 5 | |
| α-helix | 84-86 | 3 | |
| β-strand | 90 | 1 | 2 |
| α-helix | 91-100 | 10 | |
| β-strand | 108-110 | 3 | 1 |
| α-helix | 117-122 | 6 | |
| β-strand | 125-128 | 4 | 1 |
| α-helix | 134-147 | 14 | |
| β-strand | 150-157 | 8 | 1 |
| β-strand | 160-166 | 7 | 1 |
| β-strand | 171-173 | 3 | 3 |
| β-strand | 175 | 1 | 4 |
| α-helix | 179-182 | 4 | |
| β-strand | 183-185 | 3 | 5 |
| β-strand | 186-189 | 4 | 6 |
| β-strand | 194-197 | 4 | 6 |
| β-strand | 210-214 | 5 | 5 |
| β-strand | 217 | 1 | 7 |
| α-helix | 220-223 | 4 | |
| β-strand | 228-229 | 2 | 5 |
| β-strand | 231-232 | 2 | 6 |
| β-strand | 237-239 | 3 | 6 |
| α-helix | 244-246 | 3 | |
| β-strand | 251 | 1 | 7 |
| β-strand | 254-258 | 5 | 5 |
| α-helix | 259-261 | 3 | |
| β-strand | 262-264 | 3 | 3 |
| α-helix | 269-274 | 6 | |
| β-strand | 278 | 1 | 1 |
| α-helix | 283-285 | 3 | |
| α-helix | 288-305 | 18 | |
| α-helix | 309-312 | 4 | |
| α-helix | 316-332 | 17 | |
| α-helix | 334-337 | 4 | |
| α-helix | 341-343 | 3 | |
| α-helix | 345-354 | 10 | |
| α-helix | 360-379 | 20 | |
| β-strand | 381 | 1 | 4 |
| α-helix | 383-385 | 3 | |
| β-strand | 388-392 | 5 | 1 |
| α-helix | 394-396 | 3 | |
| α-helix | 398-399 | 2 | |
| α-helix | 418-424 | 7 | |
| α-helix | 426-433 | 8 | |
| β-strand | 436-440 | 5 | 8 |
| α-helix | 444-456 | 13 | |
| β-strand | 465-469 | 5 | 8 |
| α-helix | 472 | 1 | |
| β-strand | 473 | 1 | 9 |
| α-helix | 474 | 1 | |
| α-helix | 476-480 | 5 | |
| α-helix | 487-489 | 3 | |
| β-strand | 493 | 1 | 9 |
| α-helix | 494-505 | 12 | |
| α-helix | 507-509 | 3 | |
| β-strand | 513-516 | 4 | 8 |
| α-helix | 518-520 | 3 | |
| α-helix | 522-524 | 3 | |
| α-helix | 530-534 | 5 | |
| β-strand | 538-541 | 4 | 8 |
| α-helix | 546-559 | 14 | |
| β-strand | 563-569 | 7 | 8 |
| β-strand | 572-578 | 7 | 8 |
| β-strand | 583 | 1 | 10 |
| α-helix | 590-598 | 9 | |
| α-helix | 599-603 | 5 | |
| α-helix | 609-621 | 13 | |
| α-helix | 622-626 | 5 | |
| α-helix | 627-636 | 10 | |
| α-helix | 640-646 | 7 | |
| α-helix | 651-663 | 13 | |
| α-helix | 669-681 | 13 | |
| α-helix | 682-686 | 5 | |
| α-helix | 687-694 | 8 | |
| β-strand | 700 | 1 | 11 |
| β-strand | 706 | 1 | 11 |
| α-helix | 725-741 | 17 | |
| α-helix | 755-763 | 9 | |
| α-helix | 768-770 | 3 | |
| α-helix | 790-792 | 3 | |
| α-helix | 798-803 | 6 | |
| α-helix | 806-807 | 2 | |
| α-helix | 808-811 | 4 | |
| α-helix | 830-844 | 15 | |
| α-helix | 847-849 | 3 | |
| α-helix | 852-859 | 8 | |
| α-helix | 862-864 | 3 | |
| α-helix | 867-885 | 19 | |
| α-helix | 891-893 | 3 | |
| β-strand | 896-900 | 5 | 8 |
| β-strand | 905-909 | 5 | 8 |
| α-helix | 910-912 | 3 | |
| β-strand | 913 | 1 | 10 |
| α-helix | 914-915 | 2 | |
| β-strand | 916-919 | 4 | 12 |
| β-strand | 922-925 | 4 | 12 |
| β-strand | 930-934 | 5 | 13 |
| β-strand | 938 | 1 | 14 |
| α-helix | 939-945 | 7 | |
| α-helix | 946-950 | 5 | |
| β-strand | 956-959 | 4 | 15 |
| β-strand | 962-966 | 5 | 15 |
| β-strand | 981 | 1 | 14 |
| α-helix | 982-989 | 8 | |
| β-strand | 1000-1003 | 4 | 13 |
| β-strand | 1004-1006 | 3 | 15 |
| β-strand | 1007-1008 | 2 | 16 |
| β-strand | 1014-1015 | 2 | 16 |
| β-strand | 1019-1023 | 5 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ubiquitin-activating enzyme E1 1 | A | protein | 1024 | Saccharomyces cerevisiae | P22515 (AlphaFold model) |
>7ZH9_1 Ubiquitin-activating enzyme E1 1 (chains A) MSSNNSGLSAAGEIDESLYSRQLYVLGKEAMLKMQTSNVLILGLKGLGVEIAKNVVLAGV KSMTVFDPEPVQLADLSTQFFLTEKDIGQKRGDVTRAKLAELNAYVPVNVLDSLDDVTQL SQFQVVVATDTVSLEDKVKINEFCHSSGIRFISSETRGLFGNTFVDLGDEFTVLDPTGEE PRTGMVSDIEPDGTVTMLDDNRHGLEDGNFVRFSEVEGLDKLNDGTLFKVEVLGPFAFRI GSVKEYGEYKKGGIFTEVKVPRKISFKSLKQQLSNPEFVFSDFAKFDRAAQLHLGFQALH QFAVRHNGELPRTMNDEDANELIKLVTDLSVQQPEVLGEGVDVNEDLIKELSYQARGDIP GVVAFFGGLVAQEVLKACSGKFTPLKQFMYFDSLESLPDPKNFPRNEKTTQPVNSRYDNQ IAVFGLDFQKKIANSKVFLVGSGAIGCEMLKNWALLGLGSGSDGYIVVTDNDSIEKSNLN RQFLFRPKDVGKNKSEVAAEAVCAMNPDLKGKINAKIDKVGPETEEIFNDSFWESLDFVT NALDNVDARTYVDRRCVFYRKPLLESGTLGTKGNTQVIIPRLTESYSSSRDPPEKSIPLC TLRSFPNKIDHTIAWAKSLFQGYFTDSAENVNMYLTQPNFVEQTLKQSGDVKGVLESISD SLSSKPHNFEDCIKWARLEFEKKFNHDIKQLLFNFPKDAKTSNGEPFWSGAKRAPTPLEF DIYNNDHFHFVVAGASLRAYNYGIKSDDSNSKPNVDEYKSVIDHMIIPEFTPNANLKIQV NDDDPDPNANAANGSDEIDQLVSSLPDPSTLAGFKLEPVDFEKDDDTNHHIEFITACSNC RAQNYFIETADRQKTKFIAGRIIPAIATTTSLVTGLVNLELYKLIDNKTDIEQYKNGFVN LALPFFGFSEPIASPKGEYNNKKYDKIWDRFDIKGDIKLSDLIEHFEKDEGLEITMLSYG VSLLYASFFPPKKLKERLNLPITQLVKLVTKKDIPAHVSTMILEICADDKEGEDVEVPFI TIHL
Water and common crystallization additives (SO4, CL, K, GOL, ACT) are not listed.
Structures of UBA6 explain its dual specificity for ubiquitin and FAT10. Truongvan, N., Li, S., Misra, M. et al. Nat Commun (2022) 13:4789-4789. DOI 10.1038/s41467-022-32040-6 · PubMed
Other PDB entries of the same protein (UniProt P22515 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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