Crystal Structure of an RBR E3 ubiquitin ligase in complex with an E2-Ub thioester intermediate mimic. Determined by X-ray diffraction at 3.5 Å resolution. Released 23 Aug 2017.
Explore 5TTE in 3D Show helices and sheets RCSB PDB PDBe
5TTE contains 27 α-helices and 32 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 |
|---|---|---|---|
| β-strand | 102-104 | 3 | 1 |
| α-helix | 106-124 | 19 | |
| α-helix | 128-137 | 10 | |
| α-helix | 142-150 | 9 | |
| α-helix | 154-161 | 8 | |
| α-helix | 165-168 | 4 | |
| β-strand | 183-185 | 3 | 2 |
| α-helix | 186 | 1 | |
| β-strand | 192-194 | 3 | 2 |
| α-helix | 195-197 | 3 | |
| β-strand | 198-200 | 3 | 3 |
| β-strand | 206-208 | 3 | 3 |
| α-helix | 209-221 | 13 | |
| β-strand | 230 | 1 | 4 |
| β-strand | 239 | 1 | 4 |
| α-helix | 243-246 | 4 | |
| α-helix | 252-268 | 17 | |
| β-strand | 273-275 | 3 | 1 |
| β-strand | 284-286 | 3 | 1 |
| β-strand | 294-296 | 3 | 5 |
| β-strand | 302-304 | 3 | 5 |
| β-strand | 310 | 1 | 5 |
| α-helix | 317-329 | 13 | |
| β-strand | 341-343 | 3 | 6 |
| β-strand | 350-352 | 3 | 6 |
| β-strand | 359-361 | 3 | 7 |
| β-strand | 370-372 | 3 | 7 |
| β-strand | 378 | 1 | 7 |
| α-helix | 403-431 | 29 | |
| α-helix | 434-438 | 5 | |
| α-helix | 444-448 | 5 | |
| α-helix | 456-480 | 25 | |
| α-helix | 486-507 | 22 | |
| α-helix | 508-512 | 5 | |
| α-helix | 518-547 | 30 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-17 | 12 | |
| β-strand | 22-27 | 6 | 8 |
| β-strand | 34-39 | 6 | 8 |
| β-strand | 50 | 1 | 9 |
| β-strand | 51-56 | 6 | 8 |
| β-strand | 67-70 | 4 | 8 |
| β-strand | 79 | 1 | 10 |
| β-strand | 85 | 1 | 10 |
| α-helix | 88-90 | 3 | |
| α-helix | 101-113 | 13 | |
| α-helix | 123-131 | 9 | |
| α-helix | 133-147 | 15 | |
| β-strand | 149 | 1 | 9 |
| α-helix | 150-152 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 1-6 | 6 | 11 |
| β-strand | 12-17 | 6 | 11 |
| β-strand | 22 | 1 | 12 |
| α-helix | 23-34 | 12 | |
| α-helix | 38-40 | 3 | |
| β-strand | 42-45 | 4 | 11 |
| β-strand | 48-50 | 3 | 11 |
| β-strand | 55 | 1 | 12 |
| β-strand | 65-70 | 6 | 11 |
| α-helix | 71-73 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| E3 ubiquitin-protein ligase ARIH1 | B | protein | 558 | Homo sapiens | Q9Y4X5 (AlphaFold model) |
| Ubiquitin-conjugating enzyme E2 L3 | E | protein | 167 | Homo sapiens | P68036 (AlphaFold model) |
| ubiquitin | F | protein | 86 | Triticum aestivum | P69326 (AlphaFold model) |
>5TTE_1 E3 ubiquitin-protein ligase ARIH1 (chains B) SMDSDEGYNYEFDEDEECSEEDSGAEEEEDEDDDEPDDDTLDLGEVELVEPGLGVGGERD GLLCGETGGGGGSALGPGGGGGGGGGGGGGGPGHEQEEDYRYEVLTAEQILQHMVECIRE VNEVIQNPATITRILLSHFNWDKEKLMERYFDGNLEKLFAECHVINPSKKSRTRQMNTRS SAQDMPCQICYLNYPNSYFTGLECGHKFCMQCWSEYLTTKIMEEGMGQTISCPAHGCDIL VDDNTVMRLITDSKVKLKYQHLITNSFVECNRLLKWCPAPDCHHVVKVQYPDAKPVRCKC GRQFCFNCGENWHDPVKCKWLKKWIKKCDDDSETSNWIAANTKECPKCHVTIEKDGGCNH MVCRNQNCKAEFCWVCLGPWEPHGSAWYNCNRYNEDDAKAARDAQERSRAALQRYLFYCN RYMNHMQSLRFEHKLYAQVKQKMEEMQQHNMSWIEVQFLKKAVDVLCQCRATLMYTYVFA FYLKKNNQSIIFENNQADLENATEVLSGYLERDISQDSLQDIKQKVQDKYRYCESRRRVL LQHVHEGYEKDLWEYIED
>5TTE_2 Ubiquitin-conjugating enzyme E2 L3 (chains E) MAASRRLMKELEEIRKSGMKNFRNIQVDEANLLTWQGLIVPDNPPYDKGAFRIEINFPAE YPFKPPKITFKTKIYHPNIDEKGQVKLPVISAENWKPATKTDQVIQSLIALVNDPQPEHP LRADLAEEYSKDRKKFCKNAEEFTKKYGEKRPVDKLAAALEHHHHHH
>5TTE_3 ubiquitin (chains F) MHHHHHHGSHMQIFVRTLTGRTITLEVESSDTIDNVRARIQDREGIPPDQQRLIFAGRQL EDGRTLADYNIQRESTLHLVLRLRGG
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 6 |
Structural insights into the mechanism and E2 specificity of the RBR E3 ubiquitin ligase HHARI. Yuan, L., Lv, Z., Atkison, J.H. et al. Nat Commun (2017) 8:211-211. DOI 10.1038/s41467-017-00272-6 · PubMed
Other PDB entries of the same protein (UniProt Q9Y4X5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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