Vaccinia C16 N-terminal domains. Determined by electron microscopy at 3.47 Å resolution. Released 9 Nov 2022.
Explore 8AG3 in 3D Show helices and sheets RCSB PDB PDBe
8AG3 contains 5 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-4 | 3 | 1 |
| β-strand | 10-14 | 5 | 1 |
| α-helix | 21-30 | 10 | |
| β-strand | 38-42 | 5 | 1 |
| α-helix | 48-59 | 12 | |
| β-strand | 64-69 | 6 | 1 |
| β-strand | 72-78 | 7 | 1 |
| β-strand | 85-86 | 2 | 2 |
| β-strand | 98-108 | 11 | 1 |
| β-strand | 113 | 1 | 3 |
| β-strand | 116-119 | 4 | 2 |
| β-strand | 124-127 | 4 | 2 |
| β-strand | 131-134 | 4 | 1 |
| β-strand | 138-141 | 4 | 2 |
| α-helix | 142-143 | 2 | |
| β-strand | 144 | 1 | 3 |
| β-strand | 149-160 | 12 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-4 | 2 | 1 |
| β-strand | 10-15 | 6 | 1 |
| α-helix | 23-30 | 8 | |
| β-strand | 38-41 | 4 | 1 |
| α-helix | 47-60 | 14 | |
| β-strand | 64-69 | 6 | 1 |
| β-strand | 73-78 | 6 | 1 |
| β-strand | 98-108 | 11 | 1 |
| β-strand | 112-113 | 2 | 4 |
| β-strand | 116-118 | 3 | 2 |
| β-strand | 124-127 | 4 | 2 |
| β-strand | 130-134 | 5 | 1 |
| β-strand | 139-141 | 3 | 2 |
| β-strand | 144-146 | 3 | 4 |
| β-strand | 149-160 | 12 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein C10 | C, D | protein | 369 | Vaccinia virus Western Reserve | P03296 (AlphaFold model) |
>8AG3_1 Protein C10 (chains C, D) MDIYDDKGLQTIKLFNNEFDCIRNDIRELFKHVTDSDSIQLPMEDNSDIIENIRKILYRR LKNVECVDIDSTITFMKYDPNDDNKRTCSNWVPLTNNYMEYCLVIYLETPICGGKIKLYH PTGNIKSDKDIMFAKTLDFKSKKVLTGRKTIAVLDISVSYNRSMTTIHYNDDVDIDIHTD KNGKELCYCYITIDDHYLVDVETIGVIVNRSGKCLLVNNHLGIGIVKDKRISDSFGDVCM DTIFDFSEARELFSLTNDDNRNIAWDTDKLDDDTDIWTPVTEDDYKFLSRLVLYAKSQSD TVFDYYVLTGDTEPPTVFIFKVTRFYFNMPKGGENLYFQGWSHPQFEKGGGSGGGSGGSS AWSHPQFEK
Structural basis for the inactivation of cytosolic DNA sensing by the vaccinia virus. Rivera-Calzada, A., Arribas-Bosacoma, R., Ruiz-Ramos, A. et al. Nat Commun (2022) 13:7062-7062. DOI 10.1038/s41467-022-34843-z · PubMed
Other PDB entries of the same protein (UniProt P03296 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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