8X8Q: Enterovirus protease in complex host factor

Structure of enterovirus protease in complex host factor. Determined by electron microscopy at 3.14 Å resolution. Released 29 May 2024.

Method
Electron microscopy
Resolution
3.14 Å
Organisms
Homo sapiens, Enterovirus A71
Chains
2
Atoms
4,949
Mol. weight
83.97 kDa
Ligands
ZN
Released
29 May 2024

Explore 8X8Q in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8X8Q contains 28 α-helices and 27 β-strands across 2 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.

Chain B: 24 helices, 15 β-strands

ElementResiduesLengthSheet
α-helix24-3613
α-helix46-6318
α-helix75-773
α-helix79-8810
β-strand96-10161
β-strand105-11061
β-strand11412
β-strand119-12463
α-helix125-1273
β-strand129-13024
α-helix131-1355
α-helix140-1456
α-helix147-1515
α-helix153-16513
α-helix173-1786
α-helix186-1883
α-helix191-1955
α-helix202-22625
α-helix228-2303
α-helix241-25313
β-strand255-25954
β-strand266-27054
β-strand278-27925
β-strand286-28943
β-strand294-29853
β-strand30312
β-strand30811
β-strand310-31125
α-helix318-3203
α-helix321-3255
β-strand336-34276
α-helix350-36011
β-strand365-37176
α-helix379-38911
α-helix404-4096
α-helix410-4123
α-helix420-44021
α-helix445-45410
α-helix459-49436
Chain F: 4 helices, 12 β-strands
ElementResiduesLengthSheet
β-strand10-1237
β-strand15-1957
α-helix25-295
β-strand31-3557
β-strand40-4457
α-helix48-492
β-strand5313
β-strand60-6563
β-strand70-7563
α-helix77-782
β-strand8013
β-strand98-10253
α-helix1121
β-strand113-11533
β-strand120-12893
β-strand131-13663

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Actin-histidine N-methyltransferaseBprotein594Homo sapiensQ86TU7 (AlphaFold model)
2A protein (Fragment)Fprotein150Enterovirus A71R9YK28
Sequence of entity 1 (B), FASTA
>8X8Q_1 Actin-histidine N-methyltransferase (chains B)
MGKKSRVKTQKSGTGATATVSPKEILNLTSELLQKCSSPAPGPGKEWEEYVQIRTLVEKI
RKKQKGLSVTFDGKREDYFPDLMKWASENGASVEGFEMVNFKEEGFGLRATRDIKAEELF
LWVPRKLLMTVESAKNSVLGPLYSQDRILQAMGNIALAFHLLCERASPNSFWQPYIQTLP
SEYDTPLYFEEDEVRYLQSTQAIHDVFSQYKNTARQYAYFYKVIQTHPHANKLPLKDSFT
YEDYRWAVSSVMTRQNQIPTEDGSRVTLALIPLWDMCNHTNGLITTGYNLEDDRCECVAL
QDFRAGEQIYIFYGTRSNAEFVIHSGFFFDNNSHDRVKIKLGVSKSDRLYAMKAEVLARA
GIPTSSVFALHFTEPPISAQLLAFLRVFCMTEEELKEHLLGDSAIDRIFTLGNSEFPVSW
DNEVKLWTFLEDRASLLLKTYKTTIEEDKSVLKNHDLSVRAKMAIKLRLGEKEILEKAVK
SAAVNREYYRQQMEEKAPLPKYEESNLGLLESSVGDSRLPLVLRNLEEEAGVQDALNIRE
AISKAKATENGLVNGENSIPNGTRSENESLNQESKRAVEDAKGSSSDSTAGVKE
Sequence of entity 2 (F), FASTA
>8X8Q_2 2A protein (Fragment) (chains F)
GKFGQQSGAIYVGNFRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCNCQT
GVYYCNSRRKHYPVSFSKPSLIYVEASEYYPARYQSHLMLAQGHSEPGDAGGILRCQHGV
VGIVSTGGNGLVGFADVRDLLWLDEEAMEQ

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn1

Primary citation

The EV71 2A protease occupies the central cleft of SETD3 and disrupts SETD3-actin interaction. Gao, X., Wang, B., Zhu, K. et al. Nat Commun (2024) 15:4176-4176. DOI 10.1038/s41467-024-48504-w · PubMed

Other PDB entries of the same protein (UniProt Q86TU7 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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