6SLM: Full-length HPV31 E6 oncoprotein

Crystal structure of full-length HPV31 E6 oncoprotein in complex with LXXLL peptide of ubiquitin ligase E6AP. Determined by X-ray diffraction at 2.8 Å resolution. Released 9 Sept 2020.

Method
X-ray diffraction
Resolution
2.8 Å
Organisms
Escherichia coli (strain K12), Human papillomavirus type 31, Homo sapiens
Chains
1
Atoms
4,281
Mol. weight
61.62 kDa
Ligands
ZN
Released
9 Sept 2020

Explore 6SLM in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6SLM contains 36 α-helices and 33 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.

Chain A: 36 helices, 33 β-strands

ElementResiduesLengthSheet
β-strand637-64041
α-helix647-66115
β-strand665-66841
α-helix673-6819
β-strand689-69351
α-helix694-6963
α-helix697-7026
β-strand70612
α-helix707-7082
β-strand71913
α-helix721-7255
β-strand728-72924
β-strand732-73324
β-strand736-74161
β-strand744-74855
β-strand75816
α-helix762-7709
β-strand775-77735
α-helix784-7918
β-strand797-80267
β-strand805-81287
α-helix816-83015
α-helix840-8489
β-strand852-85765
α-helix859-8613
α-helix862-8676
β-strand872-87545
α-helix876-8783
β-strand87916
β-strand88018
β-strand88318
α-helix884-8852
β-strand888-88929
β-strand890-89671
β-strand89712
α-helix905-9095
α-helix910-9145
α-helix917-92610
β-strand931-93221
β-strand93413
α-helix935-9406
α-helix945-95612
β-strand958-95929
α-helix960-9612
α-helix966-98116
α-helix987-99711
α-helix1012-10198
α-helix1023-10253
β-strand1029-1030210
α-helix10351
β-strand1036110
α-helix10371
α-helix1039-10479
α-helix1050-10523
β-strand1053-1055310
β-strand1058-1061410
α-helix1064-107714
β-strand1079-1083511
α-helix1085-10928
α-helix1096-10983
β-strand1102-1103211
α-helix11081
β-strand1109111
α-helix1110-11112
α-helix1112-112110
β-strand1125-1128411
β-strand1131-1134411
α-helix1147-11493
α-helix1167-117610

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Maltose/maltodextrin-binding periplasmic protein,Protein E6,Ubiquitin-protein ligase E3AAprotein551Escherichia coli (strain K12), Human papillomavirus type 31, Homo sapiensP0AEX9 (AlphaFold model), P17386 (AlphaFold model), Q05086 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>6SLM_1 Maltose/maltodextrin-binding periplasmic protein,Protein E6,Ubiquitin-protein ligase E3A (chains A)
MKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDI
IFWAHDRFGGYAQSGLLAEITPAAAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNK
DLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIK
DVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSA
VNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPL
GAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDA
ALAAAQTNAAAMFKNPAERPRKLHELSSALEIPYDELRLNCVYCKGQLTETEVLDFAFTD
LTIVYRDDTPHGVCTKCLRFYSKVSEFRWYRYSVYGTTLEKLTNKGISDLLIRCITCQRP
LSPEEKQRHLDKKKRFHNIGGRWTGRCIACWRRPRTETQVGSSGSGSGSGSGSAAAESSE
LTLQELLGEER

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn2

Water and common crystallization additives (GOL) are not listed.

Primary citation

Structure of High-Risk Papillomavirus 31 E6 Oncogenic Protein and Characterization of E6/E6AP/p53 Complex Formation. Conrady, M.C., Suarez, I., Gogl, G. et al. J Virol (2020) 95. DOI 10.1128/JVI.00730-20 · PubMed

Other PDB entries of the same protein (UniProt P0AEX9 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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