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.
Explore 6NPI in 3D Show helices and sheets RCSB PDB PDBe
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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 477-489 | 13 | |
| β-strand | 503-511 | 9 | 1 |
| α-helix | 514-527 | 14 | |
| β-strand | 532-533 | 2 | 1 |
| α-helix | 534-536 | 3 | |
| β-strand | 537-540 | 4 | 1 |
| α-helix | 541 | 1 | |
| α-helix | 552-554 | 3 | |
| β-strand | 556-566 | 11 | 1 |
| α-helix | 569-583 | 15 | |
| α-helix | 587 | 1 | |
| α-helix | 590-592 | 3 | |
| β-strand | 593-604 | 12 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 476-489 | 14 | |
| β-strand | 503-511 | 9 | 1 |
| α-helix | 514-527 | 14 | |
| β-strand | 532-533 | 2 | 1 |
| α-helix | 534-536 | 3 | |
| β-strand | 537-540 | 4 | 1 |
| α-helix | 541 | 1 | |
| α-helix | 543-544 | 2 | |
| α-helix | 549-552 | 4 | |
| β-strand | 556-566 | 11 | 1 |
| α-helix | 569-583 | 15 | |
| α-helix | 590-592 | 3 | |
| β-strand | 593-604 | 12 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Epstein-Barr nuclear antigen 1 | A, B | protein | 141 | Epstein-Barr virus (strain B95-8) | P03211 (AlphaFold model) |
>6NPI_1 Epstein-Barr nuclear antigen 1 (chains A, B) SHMGQGGSNPKFENIAEGLRALLARSHVERTTDEGTWVAGVFVYGGSKTSLYNLRRGTAL AIPQCRLTPLSRLPFGMAPGPGPQPGPLRESIVCYFMVFLQTHIFAEVLKDAIKDLVMTK PAPTCNIRVTVCSFDDGVDLP
| ID | Name | Formula | Copies |
|---|---|---|---|
| KW1 | ({2-[(4-bromo-5-methyl-1,2-oxazol-3-yl)amino]-2-oxoethyl}sulfanyl)acetic acid | C8 H9 Br N2 O4 S | 1 |
| 60Q | 2-pyrrol-1-ylbenzoic acid | C11 H9 N O2 | 1 |
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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