Crystal structure of full-length Bovine Papillomavirus oncoprotein E6 in complex with LD1 motif of paxillin at 2.3A resolution. Determined by X-ray diffraction at 2.29 Å resolution. Released 14 Dec 2011.
Explore 3PY7 in 3D Show helices and sheets RCSB PDB PDBe
3PY7 contains 39 α-helices and 32 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 |
|---|---|---|---|
| β-strand | 7-11 | 5 | 1 |
| α-helix | 18-32 | 15 | |
| β-strand | 35-39 | 5 | 1 |
| α-helix | 44-53 | 10 | |
| 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 | 130-132 | 3 | |
| α-helix | 133-141 | 9 | |
| β-strand | 146-148 | 3 | 5 |
| α-helix | 155-164 | 10 | |
| β-strand | 168-173 | 6 | 7 |
| β-strand | 176-183 | 8 | 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 | 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 | 306-312 | 7 | |
| α-helix | 316-326 | 11 | |
| β-strand | 329-330 | 2 | 8 |
| α-helix | 331-332 | 2 | |
| α-helix | 337-353 | 17 | |
| α-helix | 358-370 | 13 | |
| α-helix | 373-378 | 6 | |
| α-helix | 401 | 1 | |
| β-strand | 402-403 | 2 | 9 |
| α-helix | 408 | 1 | |
| β-strand | 409 | 1 | 9 |
| α-helix | 410-411 | 2 | |
| α-helix | 412-420 | 9 | |
| α-helix | 425 | 1 | |
| β-strand | 426-428 | 3 | 9 |
| β-strand | 431-434 | 4 | 9 |
| α-helix | 437-450 | 14 | |
| α-helix | 452-453 | 2 | |
| β-strand | 454-456 | 3 | 10 |
| α-helix | 458-464 | 7 | |
| α-helix | 469-471 | 3 | |
| β-strand | 475-476 | 2 | 10 |
| α-helix | 481 | 1 | |
| β-strand | 482 | 1 | 10 |
| α-helix | 483-484 | 2 | |
| α-helix | 485-493 | 9 | |
| β-strand | 498-500 | 3 | 10 |
| α-helix | 502-504 | 3 | |
| β-strand | 506-508 | 3 | 10 |
| α-helix | 511-513 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| maltose-binding periplasmic protein,paxillin LD1,protein E6 chimera | A | protein | 523 | Escherichia coli, bovine papillomavirus type 1, Homo sapiens | P06931 (AlphaFold model), P0AEX9 (AlphaFold model) |
>3PY7_1 maltose-binding periplasmic protein,paxillin LD1,protein E6 chimera (chains A) MKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDI IFWAHDRFGGYAQSGLLAEITPAAAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNK DLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIK DVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSA VNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPL GAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDA ALAAAQTNAAAMDDLDALLADKEGGGMDLKPFARTNPFSGLDCLWCREPLTEVDAFRCMV KDFHVVIREGCRYGACTICLENCLATERRLWQGVPVTGEEAELLHGKTLDRLCIRCCYCG GKLTKNEKHRHVLFNEPFCKTRANIIRGRCYDCCRHGSRSKYP
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 2 |
Structural basis for hijacking of cellular LxxLL motifs by papillomavirus E6 oncoproteins. Zanier, K., Charbonnier, S., Sidi, A.O. et al. Science (2013) 339:694-698. DOI 10.1126/science.1229934 · PubMed
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