Structure of nuclear RNA export factor TAP bound to CTE RNA. Determined by X-ray diffraction at 2.3 Å resolution. Released 10 Aug 2011.
Explore 3RW6 in 3D Show helices and sheets RCSB PDB PDBe
3RW6 contains 37 α-helices and 26 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 | 120-124 | 5 | 1 |
| α-helix | 127-129 | 3 | |
| α-helix | 132-141 | 10 | |
| β-strand | 150-155 | 6 | 1 |
| β-strand | 158-163 | 6 | 1 |
| α-helix | 166-174 | 9 | |
| β-strand | 180 | 1 | 2 |
| β-strand | 186 | 1 | 2 |
| β-strand | 190-193 | 4 | 1 |
| α-helix | 195-197 | 3 | |
| α-helix | 198-201 | 4 | |
| α-helix | 204-205 | 2 | |
| α-helix | 206-218 | 13 | |
| β-strand | 220-221 | 2 | 3 |
| β-strand | 226-228 | 3 | 3 |
| α-helix | 232-234 | 3 | |
| α-helix | 236-240 | 5 | |
| α-helix | 250-263 | 14 | |
| β-strand | 269-271 | 3 | 3 |
| α-helix | 281-283 | 3 | |
| α-helix | 286-289 | 4 | |
| β-strand | 295-297 | 3 | 3 |
| α-helix | 306-312 | 7 | |
| β-strand | 319-321 | 3 | 3 |
| α-helix | 328-330 | 3 | |
| α-helix | 334-344 | 11 | |
| β-strand | 350-351 | 2 | 3 |
| β-strand | 355 | 1 | 3 |
| α-helix | 356-359 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 119-124 | 6 | 4 |
| α-helix | 127-129 | 3 | |
| α-helix | 132-142 | 11 | |
| β-strand | 150-155 | 6 | 4 |
| β-strand | 158-163 | 6 | 4 |
| α-helix | 166-174 | 9 | |
| α-helix | 179 | 1 | |
| β-strand | 180 | 1 | 5 |
| α-helix | 181 | 1 | |
| α-helix | 185 | 1 | |
| β-strand | 186 | 1 | 5 |
| α-helix | 187-188 | 2 | |
| β-strand | 190-194 | 5 | 4 |
| α-helix | 195-197 | 3 | |
| α-helix | 198-201 | 4 | |
| α-helix | 204-205 | 2 | |
| α-helix | 206-218 | 13 | |
| β-strand | 220-221 | 2 | 6 |
| α-helix | 222-224 | 3 | |
| β-strand | 226-228 | 3 | 6 |
| α-helix | 232-234 | 3 | |
| α-helix | 236-240 | 5 | |
| α-helix | 250-263 | 14 | |
| β-strand | 269-271 | 3 | 6 |
| α-helix | 281-283 | 3 | |
| α-helix | 286-289 | 4 | |
| β-strand | 295-297 | 3 | 6 |
| α-helix | 306-311 | 6 | |
| β-strand | 319-321 | 3 | 6 |
| α-helix | 328-330 | 3 | |
| α-helix | 334-342 | 9 | |
| β-strand | 350-351 | 2 | 6 |
| β-strand | 354-355 | 2 | 6 |
| α-helix | 356-358 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Nuclear RNA export factor 1 | A, B | protein | 267 | Homo sapiens | Q9UBU9 (AlphaFold model) |
| constitutive transport element(CTE)of Mason-Pfizer monkey virus RNA | F, H | RNA | 62 |
>3RW6_1 Nuclear RNA export factor 1 (chains A, B) VRRDRAPPERGGAGTSQDGTSKNWFKITIPYGRKYDKAWLLSMIQSKCSVPFTPIEFHYE NTRAQFFVEDASTASALKAVNYKILDRENRRISIIINSSAPPHTILNELKPEQVEQLKLI MSKRYDGSQQALDLKGLRSDPDLVAQNIDVVLNRRSCMAATLRIIEENIPELLSLNLSNN RLYRLDDMSSIVQKAPNLKILNLSGNELKSERELDKIKGLKLEELWLDGNSLCDTFRDQS TYISAIRERFPKLLRLDGHELPPPIAF
>3RW6_2 constitutive transport element(CTE)of Mason-Pfizer monkey virus RNA (chains F, H) GGCACUAACCUAAGACAGGAGGGCCGGGAAACCUGCCUAAUCCAAUGACGGGUAAUAGUG UC
Structure-function studies of nucleocytoplasmic transport of retroviral genomic RNA by mRNA export factor TAP. Teplova, M., Wohlbold, L., Khin, N.W. et al. Nat Struct Mol Biol (2011) 18:990-998. DOI 10.1038/nsmb.2094 · PubMed
Other PDB entries of the same protein (UniProt Q9UBU9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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