Structure of E6AP-E6 complex in Det2 state. Determined by electron microscopy at 4.35 Å resolution. Released 5 Jun 2024.
Explore 8JRR in 3D Show helices and sheets RCSB PDB PDBe
8JRR contains 94 α-helices and 50 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 | 133-135 | 3 | |
| α-helix | 136-139 | 4 | |
| α-helix | 147-151 | 5 | |
| α-helix | 153-156 | 4 | |
| α-helix | 163-166 | 4 | |
| α-helix | 236-245 | 10 | |
| α-helix | 252-258 | 7 | |
| α-helix | 260-269 | 10 | |
| α-helix | 276-278 | 3 | |
| α-helix | 284-287 | 4 | |
| α-helix | 288-291 | 4 | |
| α-helix | 299-314 | 16 | |
| α-helix | 318-329 | 12 | |
| α-helix | 333-342 | 10 | |
| α-helix | 344-353 | 10 | |
| α-helix | 371-384 | 14 | |
| β-strand | 388 | 1 | 1 |
| β-strand | 393 | 1 | 2 |
| α-helix | 398-403 | 6 | |
| α-helix | 404-409 | 6 | |
| α-helix | 427-430 | 4 | |
| β-strand | 439 | 1 | 1 |
| α-helix | 452-457 | 6 | |
| β-strand | 469 | 1 | 3 |
| α-helix | 486-505 | 20 | |
| α-helix | 509-512 | 4 | |
| β-strand | 523-526 | 4 | 4 |
| α-helix | 532-545 | 14 | |
| α-helix | 554 | 1 | |
| β-strand | 555-558 | 4 | 4 |
| α-helix | 574-581 | 8 | |
| β-strand | 590-593 | 4 | 5 |
| β-strand | 598-601 | 4 | 5 |
| α-helix | 608-610 | 3 | |
| α-helix | 612-622 | 11 | |
| α-helix | 635-641 | 7 | |
| β-strand | 644 | 1 | 2 |
| α-helix | 651-654 | 4 | |
| α-helix | 656-667 | 12 | |
| β-strand | 682-684 | 3 | 6 |
| β-strand | 692-694 | 3 | 6 |
| α-helix | 710-719 | 10 | |
| α-helix | 720-724 | 5 | |
| α-helix | 729-741 | 13 | |
| α-helix | 746-749 | 4 | |
| α-helix | 752-759 | 8 | |
| β-strand | 762 | 1 | 7 |
| α-helix | 767-770 | 4 | |
| α-helix | 787-794 | 8 | |
| α-helix | 806-809 | 4 | |
| β-strand | 815 | 1 | 7 |
| β-strand | 826 | 1 | 8 |
| β-strand | 841 | 1 | 8 |
| β-strand | 846 | 1 | 8 |
| α-helix | 855-867 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 19-25 | 7 | |
| β-strand | 36 | 1 | 9 |
| β-strand | 37 | 1 | 10 |
| β-strand | 43 | 1 | 9 |
| α-helix | 47-50 | 4 | |
| α-helix | 57-59 | 3 | |
| β-strand | 60-62 | 3 | 11 |
| β-strand | 65-67 | 3 | 11 |
| β-strand | 68 | 1 | 10 |
| α-helix | 71-82 | 12 | |
| β-strand | 86-91 | 6 | 3 |
| α-helix | 92-95 | 4 | |
| α-helix | 115-118 | 4 | |
| α-helix | 120-122 | 3 | |
| α-helix | 123-126 | 4 | |
| β-strand | 131-135 | 5 | 3 |
| β-strand | 138-140 | 3 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ubiquitin-protein ligase E3A | A, C | protein | 875 | Homo sapiens | Q05086 (AlphaFold model) |
| Protein E6 | B, D | protein | 135 | Human papillomavirus 16 | P03126 (AlphaFold model) |
>8JRR_1 Ubiquitin-protein ligase E3A (chains A, C) MEKLHQCYWKSGEPQSDDIEASRMKRAAAKHLIERYYHQLTEGCGNEACTNEFCASCPTF LRMDNNAAAIKALELYKINAKLCDPHPSKKGASSAYLENSKGAPNNSCSEIKMNKKGARI DFKDVTYLTEEKVYEILELCREREDYSPLIRVIGRVFSSAEALVQSFRKVKQHTKEELKS LQAKDEDKDEDEKEKAACSAAAMEEDSEASSSRIGDSSQGDNNLQKLGPDDVSVDIDAIR RVYTRLLSNEKIETAFLNALVYLSPNVECDLTYHNVYSRDPNYLNLFIIVMENRNLHSPE YLEMALPLFCKAMSKLPLAAQGKLIRLWSKYNADQIRRMMETFQQLITYKVISNEFNSRN LVNDDDAIVAASKCLKMVYYANVVGGEVDTNHNEEDDEEPIPESSELTLQELLGEERRNK KGPRVDPLETELGVKTLDCRKPLIPFEEFINEPLNEVLEMDKDYTFFKVETENKFSFMTC PFILNAVTKNLGLYYDNRIRMYSERRITVLYSLVQGQQLNPYLRLKVRRDHIIDDALVRL EMIAMENPADLKKQLYVEFEGEQGVDEGGVSKEFFQLVVEEIFNPDIGMFTYDESTKLFW FNPSSFETEGQFTLIGIVLGLAIYNNCILDVHFPMVVYRKLMGKKGTFRDLGDSHPVLYQ SLKDLLEYEGNVEDDMMITFQISQTDLFGNPMMYDLKENGDKIPITNENRKEFVNLYSDY ILNKSVEKQFKAFRRGFHMVTNESPLKYLFRPEEIELLICGSRNLDFQALEETTEYDGGY TRDSVLIREFWEIVHSFAAEQKRLFLQFTTGTDRAPVGGLGKLKMIIAKNGPDTERLPTS HTAFNVLLLPEYSSKEKLKERLLKAITYAKGFGML
>8JRR_2 Protein E6 (chains B, D) PQERPRKLPQLCTELQTTIHDIILECVYCKQQLLRREVYDFAFRDLCIVYRDGNPYAVCD KCLKFYSKISEYRHYSYSLYGTTLEQQYNKPLSDLLIRCINCQKPLSPEEKQRHLDKKQR FHNIRGRWTGRCMSC
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 4 |
Structural insights into the functional mechanism of the ubiquitin ligase E6AP. Wang, Z., Fan, F., Li, Z. et al. Nat Commun (2024) 15:3531-3531. DOI 10.1038/s41467-024-47586-w · PubMed
Other PDB entries of the same protein (UniProt Q05086 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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