Crystal structure of UAP56 in complex with Tho1, the yeast homolog of human SARNP. Determined by X-ray diffraction at 2.5 Å resolution. Released 16 Aug 2023.
Explore 8ENK in 3D Show helices and sheets RCSB PDB PDBe
8ENK contains 41 α-helices and 32 β-strands across 3 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 | 48-50 | 3 | |
| α-helix | 54-62 | 9 | |
| α-helix | 70-80 | 11 | |
| β-strand | 85-88 | 4 | 1 |
| α-helix | 95-106 | 12 | |
| β-strand | 116-119 | 4 | 1 |
| α-helix | 123-136 | 14 | |
| β-strand | 145-148 | 4 | 1 |
| α-helix | 154-163 | 10 | |
| β-strand | 168-171 | 4 | 1 |
| α-helix | 173-181 | 9 | |
| β-strand | 192-196 | 5 | 1 |
| α-helix | 198-203 | 6 | |
| α-helix | 205-216 | 12 | |
| β-strand | 223-228 | 6 | 1 |
| α-helix | 236-240 | 5 | |
| β-strand | 247-249 | 3 | 1 |
| α-helix | 254-257 | 4 | |
| β-strand | 262-268 | 7 | 2 |
| α-helix | 271-284 | 14 | |
| β-strand | 289-293 | 5 | 2 |
| α-helix | 297-309 | 13 | |
| β-strand | 314-317 | 4 | 2 |
| β-strand | 319 | 1 | 3 |
| β-strand | 321 | 1 | 3 |
| α-helix | 323-334 | 12 | |
| β-strand | 340-343 | 4 | 2 |
| α-helix | 345-347 | 3 | |
| β-strand | 356-361 | 6 | 2 |
| α-helix | 368-375 | 8 | |
| α-helix | 380-382 | 3 | |
| β-strand | 385-391 | 7 | 2 |
| α-helix | 394-407 | 14 | |
| β-strand | 412-413 | 2 | 2 |
| α-helix | 414-415 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 47-50 | 4 | |
| α-helix | 54-62 | 9 | |
| α-helix | 70-79 | 10 | |
| β-strand | 85-88 | 4 | 4 |
| α-helix | 95-106 | 12 | |
| β-strand | 116-119 | 4 | 4 |
| α-helix | 123-136 | 14 | |
| β-strand | 145-148 | 4 | 4 |
| α-helix | 154-163 | 10 | |
| β-strand | 168-171 | 4 | 4 |
| α-helix | 173-182 | 10 | |
| β-strand | 192-196 | 5 | 4 |
| α-helix | 198-203 | 6 | |
| α-helix | 205-216 | 12 | |
| β-strand | 223-228 | 6 | 4 |
| α-helix | 236-240 | 5 | |
| β-strand | 247-249 | 3 | 4 |
| α-helix | 254-256 | 3 | |
| β-strand | 262-268 | 7 | 5 |
| α-helix | 271-284 | 14 | |
| β-strand | 289-293 | 5 | 5 |
| α-helix | 297-309 | 13 | |
| β-strand | 314-317 | 4 | 5 |
| β-strand | 319 | 1 | 6 |
| β-strand | 321 | 1 | 6 |
| α-helix | 323-334 | 12 | |
| β-strand | 340-343 | 4 | 5 |
| α-helix | 345-347 | 3 | |
| β-strand | 356-361 | 6 | 5 |
| α-helix | 368-375 | 8 | |
| α-helix | 380-382 | 3 | |
| β-strand | 385-391 | 7 | 5 |
| α-helix | 394-407 | 14 | |
| β-strand | 412-413 | 2 | 5 |
| α-helix | 414-415 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 124-142 | 19 | |
| α-helix | 147-162 | 16 | |
| α-helix | 170-174 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Spliceosome RNA helicase DDX39B | A, B | protein | 390 | Homo sapiens | Q13838 (AlphaFold model) |
| Protein THO1 | E | protein | 61 | Saccharomyces cerevisiae | P40040 (AlphaFold model) |
| RNA | M, N | RNA | 15 | synthetic construct |
>8ENK_1 Spliceosome RNA helicase DDX39B (chains A, B) GAMGSSSGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAV FVLATLQQLEPVTGQVSVLVMCHTRELAFQISKEYERFSKYMPNVKVAVFFGGLSIKKDE EVLKKNCPHIVVGTPGRILALARNKSLNLKHIKHFILDECDKMLEQLDMRRDVQEIFRMT PHEKQVMMFSATLSKEIRPVCRKFMQDPMEIFVDDETKLTLHGLQQYYVKLKDNEKNRKL FDLLDVLEFNQVVIFVKSVQRCIALAQLLVEQNFPAIAIHRGMPQEERLSRYQQFKDFQR RILVATNLFGRGMDIERVNIAFNYDMPEDSDTYLHRVARAGRFGTKGLAITFVSDENDAK ILNDVQDRFEVNISELPDEIDISSYIEQTR
>8ENK_2 Protein THO1 (chains E) GAMGSEEIKAKALDLLNKKLHRANKFGQDQADIDSLQRQINRVEKFGVDLNSKLAEELGL V
>8ENK_3 RNA (chains M, N) UUUUUUUUUUUUUUU
| ID | Name | Formula | Copies |
|---|---|---|---|
| BEF | Beryllium trifluoride ion | Be F3 | 2 |
| MG | Magnesium ion | Mg | 2 |
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 2 |
Structural basis for high-order complex of SARNP and DDX39B to facilitate mRNP assembly. Xie, Y., Gao, S., Zhang, K. et al. Cell Rep (2023) 42:112988-112988. DOI 10.1016/j.celrep.2023.112988 · PubMed
Other PDB entries of the same protein (UniProt Q13838 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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