4GIZ: Full-length human papillomavirus oncoprotein E6

Crystal structure of full-length human papillomavirus oncoprotein E6 in complex with LXXLL peptide of ubiquitin ligase E6AP at 2.55 A resolution. Determined by X-ray diffraction at 2.55 Å resolution. Released 23 Jan 2013.

Method
X-ray diffraction
Resolution
2.55 Å
Organisms
Escherichia coli, HOMO SAPIENS, Human papillomavirus type 16
Chains
4
Atoms
9,036
Mol. weight
119.86 kDa
Ligands
ZN
Released
23 Jan 2013

Explore 4GIZ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4GIZ contains 80 α-helices and 72 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.

Chains A and B: 26 helices, 23 β-strands

ElementResiduesLengthSheet
α-helix3-42
β-strand7-1151
α-helix14-163
α-helix20-3213
β-strand35-3951
α-helix44-529
β-strand60-6451
α-helix65-673
α-helix68-736
β-strand7712
α-helix78-803
α-helix84-874
β-strand9013
α-helix92-976
β-strand99-10024
β-strand103-10424
β-strand107-11261
β-strand115-11955
β-strand12916
α-helix130-1323
α-helix133-1419
β-strand146-14835
α-helix155-16410
β-strand168-17367
β-strand176-18387
α-helix187-20115
α-helix211-2199
β-strand223-22865
α-helix230-2323
α-helix233-2397
β-strand243-24645
α-helix247-2493
β-strand250-25126
β-strand254-25526
α-helix2561
β-strand259-26028
β-strand261-26771
β-strand26812
α-helix274-2807
α-helix281-2855
α-helix288-29710
β-strand302-30321
β-strand30513
α-helix306-3127
α-helix316-32611
β-strand329-33028
α-helix331-3322
α-helix337-35216
α-helix358-37922
Chain C: 14 helices, 13 β-strands
ElementResiduesLengthSheet
β-strand11117
α-helix12-198
β-strand29118
β-strand30119
α-helix351
β-strand36118
α-helix37-382
α-helix39-479
α-helix501
β-strand51117
α-helix521
β-strand53-55320
β-strand58-60320
β-strand61119
α-helix64-7815
β-strand79-83521
α-helix85-928
α-helix96-983
β-strand102-103221
α-helix1081
β-strand109121
α-helix110-1112
α-helix112-1209
α-helix123-1242
β-strand125-128421
β-strand131-134421
α-helix137-1415
Chain D: 14 helices, 13 β-strands
ElementResiduesLengthSheet
β-strand11122
α-helix12-198
β-strand29123
β-strand30124
α-helix351
β-strand36123
α-helix37-382
α-helix39-479
α-helix501
β-strand51122
α-helix521
β-strand53-55325
β-strand58-60325
β-strand61124
α-helix64-7815
β-strand79-83526
α-helix85-928
α-helix96-983
β-strand101-103326
α-helix1081
β-strand109126
α-helix110-1112
α-helix112-1209
α-helix123-1242
β-strand125-128426
β-strand131-134426
α-helix137-1404

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Maltose-binding periplasmic protein, UBIQUITIN LIGASE EA6P: chimeric proteinA, Bprotein382Escherichia coli, HOMO SAPIENSP0AEX9 (AlphaFold model), Q05086 (AlphaFold model)
Protein E6C, Dprotein142Human papillomavirus type 16P03126 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>4GIZ_1 Maltose-binding periplasmic protein, UBIQUITIN LIGASE EA6P: chimeric protein (chains A, B)
KIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDII
FWAHDRFGGYAQSGLLAEITPAAAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKD
LLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKD
VGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSAV
NYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLG
AVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDAA
LAAAQTNAAAELTLQELLGEER
Sequence of entity 2 (C, D), FASTA
>4GIZ_2 Protein E6 (chains C, D)
FQDPQERPRKLPQLCTELQTTIHDIILECVYCKQQLLRREVYDFARRDLCIVYRDGNPYA
VCDKCLKFYSKISEYRHYSYSLYGTTLEQQYNKPLSDLLIRCINCQKPLSPEEKQRHLDK
KQRFHNIRGRWTGRCMSCSRSS

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn4

Primary citation

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

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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