Recognition of eIF4G by Rotavirus NSP3 reveals a basis for mRNA circularization. Determined by X-ray diffraction at 2.38 Å resolution. Released 5 Jul 2002.
Explore 1LJ2 in 3D Show helices and sheets RCSB PDB PDBe
1LJ2 contains 10 α-helices and 5 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 209-211 | 3 | |
| α-helix | 212-250 | 39 | |
| α-helix | 256-266 | 11 | |
| α-helix | 274-303 | 30 | |
| β-strand | 309-311 | 3 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 209-250 | 42 | |
| α-helix | 256-267 | 12 | |
| α-helix | 274-306 | 33 | |
| β-strand | 309-314 | 6 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 141-143 | 3 | 1 |
| α-helix | 145-147 | 3 | |
| α-helix | 153-156 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 138-144 | 7 | 2 |
| β-strand | 150-151 | 2 | 2 |
| α-helix | 153-157 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Nonstructural RNA-binding protein 34 | A, B | protein | 110 | Simian rotavirus A/SA11 | P03536 |
| eukaryotic protein synthesis initiation factor | C, D | protein | 28 | Q04637 (AlphaFold model) |
>1LJ2_1 NONSTRUCTURAL RNA-BINDING PROTEIN 34 (chains A, B) MHSLQNVIPQQQAHIAELQVYNNKLERDLQNKIGSLTSSIEWYLRSMELDPEIKADIEQQ INSIDAINPLHAFDDLESVIRNLISDYDKLFLMFKGLIQRSNYQYSFGSE
>1LJ2_2 eukaryotic protein synthesis initiation factor (chains C, D) APKRERKTIRIRDPNQGGKDITEEIMSG
| ID | Name | Formula | Copies |
|---|---|---|---|
| AU | Gold ion | Au | 3 |
Recognition of eIF4G by rotavirus NSP3 reveals a basis for mRNA circularization. Groft, C.M., Burley, S.K. Mol Cell (2002) 9:1273-1283. DOI 10.1016/S1097-2765(02)00555-5 · PubMed
Other PDB entries of the same protein (UniProt P03536), best resolution first:
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