Structure of N-terminal domain of nuclear RNA export factor TAP. Determined by X-ray diffraction at 3.0 Å resolution. Released 10 Aug 2011.
Explore 3RW7 in 3D Show helices and sheets RCSB PDB PDBe
3RW7 contains 44 α-helices and 42 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 |
|---|---|---|---|
| β-strand | 119-124 | 6 | 1 |
| α-helix | 127-129 | 3 | |
| α-helix | 132-142 | 11 | |
| β-strand | 150-155 | 6 | 1 |
| β-strand | 158-163 | 6 | 1 |
| α-helix | 166-173 | 8 | |
| β-strand | 180 | 1 | 2 |
| β-strand | 186 | 1 | 2 |
| β-strand | 190-194 | 5 | 1 |
| α-helix | 195-196 | 2 | |
| α-helix | 206-218 | 13 | |
| β-strand | 220-221 | 2 | 3 |
| β-strand | 226-228 | 3 | 3 |
| α-helix | 236-239 | 4 | |
| α-helix | 250-263 | 14 | |
| β-strand | 269-271 | 3 | 3 |
| α-helix | 280-282 | 3 | |
| α-helix | 286-289 | 4 | |
| β-strand | 295-297 | 3 | 3 |
| α-helix | 307-311 | 5 | |
| β-strand | 319-321 | 3 | 3 |
| α-helix | 334-342 | 9 | |
| β-strand | 350-351 | 2 | 4 |
| β-strand | 354-355 | 2 | 4 |
| α-helix | 358-360 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 206-218 | 13 | |
| β-strand | 220-221 | 2 | 5 |
| β-strand | 226-228 | 3 | 5 |
| α-helix | 232-234 | 3 | |
| α-helix | 236-239 | 4 | |
| α-helix | 250-263 | 14 | |
| β-strand | 269-271 | 3 | 5 |
| α-helix | 280-283 | 4 | |
| α-helix | 286-289 | 4 | |
| β-strand | 295-297 | 3 | 5 |
| α-helix | 306-312 | 7 | |
| β-strand | 319-321 | 3 | 5 |
| α-helix | 326-330 | 5 | |
| α-helix | 334-342 | 9 | |
| β-strand | 350-351 | 2 | 5 |
| β-strand | 354-355 | 2 | 5 |
| α-helix | 357-360 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 119-124 | 6 | 6 |
| α-helix | 127-129 | 3 | |
| α-helix | 132-140 | 9 | |
| β-strand | 150-155 | 6 | 6 |
| β-strand | 158-163 | 6 | 6 |
| α-helix | 168-174 | 7 | |
| β-strand | 180 | 1 | 7 |
| β-strand | 186 | 1 | 7 |
| β-strand | 190-194 | 5 | 6 |
| α-helix | 195-197 | 3 | |
| α-helix | 206-218 | 13 | |
| β-strand | 220-221 | 2 | 8 |
| β-strand | 226-228 | 3 | 8 |
| α-helix | 232-234 | 3 | |
| α-helix | 236-241 | 6 | |
| α-helix | 250-263 | 14 | |
| β-strand | 269-271 | 3 | 8 |
| α-helix | 280-283 | 4 | |
| α-helix | 286-289 | 4 | |
| β-strand | 295-297 | 3 | 8 |
| α-helix | 306-312 | 7 | |
| β-strand | 319-321 | 3 | 8 |
| β-strand | 323 | 1 | 9 |
| β-strand | 325 | 1 | 9 |
| α-helix | 326-328 | 3 | |
| α-helix | 334-344 | 11 | |
| β-strand | 350-351 | 2 | 8 |
| β-strand | 354-355 | 2 | 8 |
| α-helix | 356-359 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 208-217 | 10 | |
| β-strand | 220-221 | 2 | 10 |
| β-strand | 226-228 | 3 | 10 |
| α-helix | 236-239 | 4 | |
| α-helix | 250-263 | 14 | |
| β-strand | 269-271 | 3 | 10 |
| α-helix | 280-288 | 9 | |
| β-strand | 295-297 | 3 | 10 |
| α-helix | 306-312 | 7 | |
| β-strand | 319-321 | 3 | 10 |
| α-helix | 326-330 | 5 | |
| α-helix | 334-344 | 11 | |
| β-strand | 350-351 | 2 | 10 |
| β-strand | 354-355 | 2 | 10 |
| α-helix | 356-359 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Nuclear RNA export factor 1 | A, B, C, D | protein | 267 | Homo sapiens | Q9UBU9 (AlphaFold model) |
>3RW7_1 Nuclear RNA export factor 1 (chains A, B, C, D) VRRDRAPPERGGAGTSQDGTSKNWFKITIPYGRKYDKAWLLSMIQSKCSVPFTPIEFHYE NTRAQFFVEDASTASALKAVNYKILDRENRRISIIINSSAPPHTILNELKPEQVEQLKLI MSKRYDGSQQALDLKGLRSDPDLVAQNIDVVLNRRSCMAATLRIIEENIPELLSLNLSNN RLYRLDDMSSIVQKAPNLKILNLSGNELKSERELDKIKGLKLEELWLDGNSLCDTFRDQS TYISAIRERFPKLLRLDGHELPPPIAF
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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