Crystal structure of the RNA-binding domain of the mRNA export factor tap. Determined by X-ray diffraction at 3.15 Å resolution. Released 11 Dec 2000.
Explore 1FT8 in 3D Show helices and sheets RCSB PDB PDBe
1FT8 contains 50 α-helices and 43 β-strands across 5 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 | 157-163 | 7 | 1 |
| α-helix | 166-173 | 8 | |
| β-strand | 179-180 | 2 | 2 |
| α-helix | 185 | 1 | |
| β-strand | 186-187 | 2 | 2 |
| α-helix | 188 | 1 | |
| β-strand | 190-194 | 5 | 1 |
| α-helix | 206-218 | 13 | |
| β-strand | 220-221 | 2 | 3 |
| β-strand | 226-228 | 3 | 3 |
| α-helix | 232-234 | 3 | |
| α-helix | 250-263 | 14 | |
| β-strand | 269-271 | 3 | 3 |
| α-helix | 280-283 | 4 | |
| α-helix | 286-289 | 4 | |
| β-strand | 295-297 | 3 | 3 |
| α-helix | 307-312 | 6 | |
| β-strand | 319-321 | 3 | 3 |
| α-helix | 326-330 | 5 | |
| α-helix | 334-344 | 11 | |
| β-strand | 350-351 | 2 | 3 |
| β-strand | 354-355 | 2 | 3 |
| α-helix | 356-357 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 206-218 | 13 | |
| β-strand | 220-221 | 2 | 4 |
| β-strand | 226-228 | 3 | 4 |
| α-helix | 232-234 | 3 | |
| α-helix | 236-240 | 5 | |
| α-helix | 250-263 | 14 | |
| β-strand | 269-271 | 3 | 4 |
| α-helix | 280-283 | 4 | |
| α-helix | 286-289 | 4 | |
| β-strand | 295-297 | 3 | 4 |
| α-helix | 306-312 | 7 | |
| β-strand | 319-321 | 3 | 4 |
| α-helix | 326-330 | 5 | |
| α-helix | 334-342 | 9 | |
| β-strand | 350-351 | 2 | 4 |
| β-strand | 354-355 | 2 | 4 |
| α-helix | 356-357 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 119-124 | 6 | 5 |
| α-helix | 127-129 | 3 | |
| α-helix | 132-142 | 11 | |
| β-strand | 150-155 | 6 | 5 |
| β-strand | 157-163 | 7 | 5 |
| α-helix | 166-173 | 8 | |
| β-strand | 179-180 | 2 | 6 |
| β-strand | 186-187 | 2 | 6 |
| α-helix | 188 | 1 | |
| β-strand | 190-194 | 5 | 5 |
| α-helix | 195-197 | 3 | |
| α-helix | 204-205 | 2 | |
| α-helix | 206-217 | 12 | |
| β-strand | 220-221 | 2 | 7 |
| β-strand | 226-228 | 3 | 7 |
| α-helix | 236-241 | 6 | |
| α-helix | 250-263 | 14 | |
| β-strand | 269-271 | 3 | 7 |
| α-helix | 280-283 | 4 | |
| α-helix | 286-289 | 4 | |
| β-strand | 295-297 | 3 | 7 |
| α-helix | 307-312 | 6 | |
| β-strand | 319-321 | 3 | 7 |
| α-helix | 326-330 | 5 | |
| α-helix | 334-344 | 11 | |
| β-strand | 350-351 | 2 | 7 |
| β-strand | 354-355 | 2 | 7 |
| α-helix | 356-357 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 206-217 | 12 | |
| β-strand | 220-221 | 2 | 8 |
| α-helix | 222-224 | 3 | |
| β-strand | 226-228 | 3 | 8 |
| α-helix | 238-240 | 3 | |
| 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 |
| α-helix | 326-330 | 5 | |
| α-helix | 334-344 | 11 | |
| β-strand | 350-351 | 2 | 8 |
| β-strand | 354-355 | 2 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 120-122 | 3 | 9 |
| α-helix | 132-142 | 11 | |
| β-strand | 150 | 1 | 9 |
| β-strand | 161-163 | 3 | 9 |
| α-helix | 166-173 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Tip associating protein | A, B, C, D, E | protein | 271 | Homo sapiens | Q9UBU9 (AlphaFold model) |
>1FT8_1 TIP ASSOCIATING PROTEIN (chains A, B, C, D, E) PPERGGAGTSQDGTSKNWFKITIPYGRKYDKAWLLSMIQSKCSVPFTPIEFHYENTRAQF FVEDASTASALKAVNYKILDRENRRISIIINSSAPPHTILNELKPEQVEQLKLIMSKRYD GSQQVLDLKGLRSDPDLVAQNIDVVLNRRSCMAATLRIIEENIPELLSLNLSNNRLYRLD DMSSIVQKAPNLKILNLSGNELKSERELDKIKGLKLEELWLDGNSLCDTFRDQSTYISAI RERFPKLLRLDGHELPPPIAFDVEAPTTLPP
The structure of the mRNA export factor TAP reveals a cis arrangement of a non-canonical RNP domain and an LRR domain. Liker, E., Fernandez, E., Izaurralde, E. et al. EMBO J (2000) 19:5587-5598. DOI 10.1093/emboj/19.21.5587 · PubMed
Other PDB entries of the same protein (UniProt Q9UBU9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 1FT8 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.