Structure of HPV18 E6 oncoprotein in complex with mutant E6AP LxxLL motif. Determined by X-ray diffraction at 2.03 Å resolution. Released 4 Sept 2019.
Explore 6SJV in 3D Show helices and sheets RCSB PDB PDBe
6SJV contains 39 α-helices and 36 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 | 3-4 | 2 | |
| β-strand | 7-11 | 5 | 1 |
| α-helix | 18-32 | 15 | |
| β-strand | 35-39 | 5 | 1 |
| α-helix | 44-52 | 9 | |
| β-strand | 60-64 | 5 | 1 |
| α-helix | 65-67 | 3 | |
| α-helix | 68-73 | 6 | |
| β-strand | 77 | 1 | 2 |
| α-helix | 78-80 | 3 | |
| α-helix | 84-87 | 4 | |
| β-strand | 90 | 1 | 3 |
| α-helix | 92-97 | 6 | |
| β-strand | 99-100 | 2 | 4 |
| β-strand | 103-104 | 2 | 4 |
| β-strand | 107-112 | 6 | 1 |
| β-strand | 115-119 | 5 | 5 |
| β-strand | 129 | 1 | 6 |
| α-helix | 133-142 | 10 | |
| β-strand | 146-148 | 3 | 5 |
| α-helix | 155-164 | 10 | |
| α-helix | 168 | 1 | |
| β-strand | 169-173 | 5 | 7 |
| β-strand | 176-180 | 5 | 7 |
| α-helix | 187-201 | 15 | |
| α-helix | 211-219 | 9 | |
| β-strand | 223-228 | 6 | 5 |
| α-helix | 230-232 | 3 | |
| α-helix | 233-238 | 6 | |
| β-strand | 243-246 | 4 | 5 |
| α-helix | 247-249 | 3 | |
| β-strand | 250-251 | 2 | 6 |
| β-strand | 254-255 | 2 | 6 |
| α-helix | 256 | 1 | |
| α-helix | 258 | 1 | |
| β-strand | 259-260 | 2 | 8 |
| β-strand | 261-267 | 7 | 1 |
| β-strand | 268 | 1 | 2 |
| α-helix | 274-280 | 7 | |
| α-helix | 281-285 | 5 | |
| α-helix | 288-297 | 10 | |
| β-strand | 302-303 | 2 | 1 |
| β-strand | 305 | 1 | 3 |
| α-helix | 306-308 | 3 | |
| α-helix | 309-312 | 4 | |
| α-helix | 316-327 | 12 | |
| β-strand | 329-330 | 2 | 8 |
| α-helix | 331-332 | 2 | |
| α-helix | 337-352 | 16 | |
| α-helix | 358-1002 | 16 | |
| α-helix | 1003-1005 | 3 | |
| β-strand | 1013 | 1 | 9 |
| α-helix | 1014-1020 | 7 | |
| β-strand | 1031-1032 | 2 | 10 |
| α-helix | 1037 | 1 | |
| β-strand | 1038 | 1 | 10 |
| α-helix | 1039-1040 | 2 | |
| α-helix | 1041-1049 | 9 | |
| β-strand | 1053 | 1 | 9 |
| β-strand | 1055-1057 | 3 | 10 |
| β-strand | 1060-1063 | 4 | 10 |
| α-helix | 1066-1079 | 14 | |
| β-strand | 1081-1085 | 5 | 11 |
| α-helix | 1087-1094 | 8 | |
| β-strand | 1104 | 1 | 12 |
| β-strand | 1105 | 1 | 13 |
| α-helix | 1110 | 1 | |
| β-strand | 1111 | 1 | 12 |
| α-helix | 1112-1113 | 2 | |
| α-helix | 1114-1122 | 9 | |
| β-strand | 1127-1130 | 4 | 11 |
| β-strand | 1133-1135 | 3 | 11 |
| β-strand | 1136 | 1 | 13 |
| α-helix | 1139-1142 | 4 | |
| α-helix | 2382-2389 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Maltodextrin-binding protein,Protein E6,Ubiquitin-protein ligase E3A | A | protein | 543 | Escherichia coli, Human papillomavirus type 18, Homo sapiens | P06463 (AlphaFold model), Q05086 (AlphaFold model) |
>6SJV_1 Maltodextrin-binding protein,Protein E6,Ubiquitin-protein ligase E3A (chains A) MKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDI IFWAHDRFGGYAQSGLLAEITPAAAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNK DLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIK DVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSA VNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPL GAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDA ALAAAQTNAAAMARFEDPTRRPYKLPDLCTELNTSLQDIEITCVYCKTVLELTEVFEFAR KDLFVVYRDSIPHAACHKCIDFYSRIRELRHYSDSVYGDTLEKLTNTGLYNLLIRCLRCQ KPLNPAEKLRHLNEKRRFHNIAGHYRGQCHSCCNRARQERLQRGSAAAESSELTFQELLG ERR
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 2 |
Cellular target recognition by HPV18 and HPV49 oncoproteins. Suarez, I.P., Bonhoure, A., Cousido-Siah, A. et al. To be published.
Other PDB entries of the same protein (UniProt P06463 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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