6NPI: Epstein-Barr Virus Nuclear Antigen-1, EBNA1

Crystal structure of Epstein-Barr Virus Nuclear Antigen-1, EBNA1, bound to fragments. Determined by X-ray diffraction at 1.5 Å resolution. Released 20 Mar 2019.

Method
X-ray diffraction
Resolution
1.5 Å
Organism
Epstein-Barr virus (strain B95-8)
Chains
2
Atoms
2,623
Mol. weight
31.11 kDa
Ligands
KW1, 60Q
Released
20 Mar 2019

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

Secondary structure: helices and β-sheets

6NPI contains 16 α-helices and 10 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 A: 8 helices, 5 β-strands

ElementResiduesLengthSheet
α-helix477-48913
β-strand503-51191
α-helix514-52714
β-strand532-53321
α-helix534-5363
β-strand537-54041
α-helix5411
α-helix552-5543
β-strand556-566111
α-helix569-58315
α-helix5871
α-helix590-5923
β-strand593-604121
Chain B: 8 helices, 5 β-strands
ElementResiduesLengthSheet
α-helix476-48914
β-strand503-51191
α-helix514-52714
β-strand532-53321
α-helix534-5363
β-strand537-54041
α-helix5411
α-helix543-5442
α-helix549-5524
β-strand556-566111
α-helix569-58315
α-helix590-5923
β-strand593-604121

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Epstein-Barr nuclear antigen 1A, Bprotein141Epstein-Barr virus (strain B95-8)P03211 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>6NPI_1 Epstein-Barr nuclear antigen 1 (chains A, B)
SHMGQGGSNPKFENIAEGLRALLARSHVERTTDEGTWVAGVFVYGGSKTSLYNLRRGTAL
AIPQCRLTPLSRLPFGMAPGPGPQPGPLRESIVCYFMVFLQTHIFAEVLKDAIKDLVMTK
PAPTCNIRVTVCSFDDGVDLP

Ligands and cofactors

IDNameFormulaCopies
KW1({2-[(4-bromo-5-methyl-1,2-oxazol-3-yl)amino]-2-oxoethyl}sulfanyl)acetic acidC8 H9 Br N2 O4 S1
60Q2-pyrrol-1-ylbenzoic acidC11 H9 N O21

Primary citation

Structure-based design of small-molecule inhibitors of EBNA1 DNA binding blocks Epstein-Barr virus latent infection and tumor growth. Messick, T.E., Smith, G.R., Soldan, S.S. et al. Sci Transl Med (2019) 11. DOI 10.1126/scitranslmed.aau5612 · PubMed

Other PDB entries of the same protein (UniProt P03211 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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