Cryo-EM structure of human TREX-2 complex bound to DDX39B(UAP56). Determined by electron microscopy at 2.79 Å resolution. Released 4 Jun 2025.
Explore 9DLP in 3D Show helices and sheets RCSB PDB PDBe
9DLP contains 66 α-helices and 21 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 | 604-619 | 16 | |
| α-helix | 643-652 | 10 | |
| α-helix | 657-659 | 3 | |
| β-strand | 660 | 1 | 1 |
| β-strand | 667 | 1 | 1 |
| α-helix | 674-676 | 3 | |
| α-helix | 688-690 | 3 | |
| α-helix | 694-703 | 10 | |
| α-helix | 704-708 | 5 | |
| α-helix | 716-736 | 21 | |
| α-helix | 742-761 | 20 | |
| α-helix | 772-795 | 24 | |
| α-helix | 803-812 | 10 | |
| α-helix | 820-824 | 5 | |
| α-helix | 829-832 | 4 | |
| α-helix | 835-848 | 14 | |
| α-helix | 852-860 | 9 | |
| α-helix | 864-870 | 7 | |
| α-helix | 871-873 | 3 | |
| α-helix | 874-888 | 15 | |
| β-strand | 897-900 | 4 | 2 |
| α-helix | 901-908 | 8 | |
| α-helix | 913-921 | 9 | |
| β-strand | 926-928 | 3 | 2 |
| β-strand | 931-934 | 4 | 2 |
| α-helix | 941-942 | 2 | |
| α-helix | 945-948 | 4 | |
| α-helix | 952-957 | 6 | |
| α-helix | 962-967 | 6 | |
| α-helix | 971-975 | 5 | |
| α-helix | 978-980 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-19 | 14 | |
| α-helix | 22-29 | 8 | |
| α-helix | 34-37 | 4 | |
| α-helix | 47-53 | 7 | |
| α-helix | 55 | 1 | |
| α-helix | 58-73 | 16 | |
| α-helix | 77-97 | 21 | |
| α-helix | 105-126 | 22 | |
| α-helix | 136-153 | 18 | |
| α-helix | 160-162 | 3 | |
| α-helix | 164-167 | 4 | |
| α-helix | 168-179 | 12 | |
| α-helix | 188-197 | 10 | |
| α-helix | 206-222 | 17 | |
| α-helix | 228-238 | 11 | |
| β-strand | 241 | 1 | 3 |
| α-helix | 245-261 | 17 | |
| β-strand | 265-266 | 2 | 4 |
| α-helix | 268-273 | 6 | |
| α-helix | 278-288 | 11 | |
| α-helix | 291-300 | 10 | |
| α-helix | 302-308 | 7 | |
| α-helix | 311-314 | 4 | |
| α-helix | 315-317 | 3 | |
| α-helix | 318-333 | 16 | |
| β-strand | 337-339 | 3 | 5 |
| α-helix | 340-349 | 10 | |
| α-helix | 357-370 | 14 | |
| β-strand | 375-378 | 4 | 5 |
| β-strand | 383-386 | 4 | 5 |
| α-helix | 395-397 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 20-22 | 3 | |
| β-strand | 32 | 1 | 3 |
| β-strand | 39-40 | 2 | 4 |
| α-helix | 51-62 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 11-13 | 3 | |
| α-helix | 47-50 | 4 | |
| α-helix | 54-63 | 10 | |
| α-helix | 70-80 | 11 | |
| β-strand | 85-88 | 4 | 6 |
| α-helix | 95-105 | 11 | |
| β-strand | 116-119 | 4 | 6 |
| α-helix | 123-136 | 14 | |
| β-strand | 145-148 | 4 | 6 |
| β-strand | 150 | 1 | 7 |
| β-strand | 152 | 1 | 7 |
| α-helix | 154-163 | 10 | |
| β-strand | 168-171 | 4 | 6 |
| α-helix | 173-181 | 9 | |
| α-helix | 187-189 | 3 | |
| β-strand | 192-196 | 5 | 6 |
| α-helix | 198-203 | 6 | |
| α-helix | 205-217 | 13 | |
| β-strand | 223-228 | 6 | 6 |
| α-helix | 236-241 | 6 | |
| β-strand | 247-250 | 4 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Germinal-center associated nuclear protein | A | protein | 648 | Homo sapiens | O60318 (AlphaFold model) |
| PCI domain-containing protein 2 | B | protein | 399 | Homo sapiens | Q5JVF3 (AlphaFold model) |
| 26S proteasome complex subunit SEM1 | C | protein | 70 | Homo sapiens | P60896 (AlphaFold model) |
| Spliceosome RNA helicase DDX39B | D | protein | 433 | Homo sapiens | Q13838 (AlphaFold model) |
>9DLP_1 Germinal-center associated nuclear protein (chains A) GAMGSKEAKKETGFVESAESDHMAIPGGNQSVLAPSRIPGVNKEEETESREKKEDSLRGT PARQSNRSESTDSLGGLSPSEVTAIQCKNIPDYLNDRTILENHFGKIAKVQRIFTRRSKK LAVVHFFDHASAALARKKGKSLHKDMAIFWHRKKISPNKKPFSLKEKKPGDGEVSPSTED APFQHSPLGKAAGRTGASSLLNKSSPVKKPSLLKAHQFEGDSFDSASEGSEGLGPCVLSL STLIGTVAETSKEKYRLLDQRDRIMRQARVKRTDLDKARTFVGTCLDMCPEKERYMRETR SQLSVFEVVPGTDQVDHAAAVKEYSRSSADQEEPLPHELRPLPVLSRTMDYLVTQIMDQK EGSLRDWYDFVWNRTRGIRKDITQQHLCDPLTVSLIEKCTRFHIHCAHFMCEEPMSSFDA KINNENMTKCLQSLKEMYQDLRNKGVFCASEAEFQGYNVLLSLNKGDILREVQQFHPAVR NSSEVKFAVQAFAALNSNNFVRFFKLVQSASYLNACLLHCYFSQIRKDALRALNFAYTVS TQRSTIFPLDGVVRMLLFRDCEEATDFLTCHGLTVSDGCVELNRSAFLEPEGLSKTRKSV FITRKLTVSVGEIVNGGPLPPVPRHTPVCSFNSQNKYIGESLAAELPV
>9DLP_2 PCI domain-containing protein 2 (chains B) MAHITINQYLQQVYEAIDSRDGASCAELVSFKHPHVANPRLQMASPEEKCQQVLEPPYDE MFAAHLRCTYAVGNHDFIEAYKCQTVIVQSFLRAFQAHKEENWALPVMYAVALDLRVFAN NADQQLVKKGKSKVGDMLEKAAELLMSCFRVCASDTRAGIEDSKKWGMLFLVNQLFKIYF KINKLHLCKPLIRAIDSSNLKDDYSTAQRVTYKYYVGRKAMFDSDFKQAEEYLSFAFEHC HRSSQKNKRMILIYLLPVKMLLGHMPTVELLKKYHLMQFAEVTRAVSEGNLLLLHEALAK HEAFFIRCGIFLILEKLKIITYRNLFKKVYLLLKTHQLSLDAFLVALKFMQVEDVDIDEV QCILANLIYMGHVKGYISHQHQKLVVSKQNPFPPLSTVC
>9DLP_3 26S proteasome complex subunit SEM1 (chains C) MSEKKQPVDLGLLEEDDEFEEFPAEDWAGLDEDEDAHVWEDNWDDDNVEDDFSNQLRAEL EKHGYKMETS
>9DLP_4 Spliceosome RNA helicase DDX39B (chains D) GAMGSMAENDVDNELLDYEDDEVETAAGGDGAEAPAKKDVKGSYVSIHSSGFRDFLLKPE LLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLATLQQLXPVTGQVS VLVMCHTRELAFQISKEYERFSKYMPNVKVAVFFGGLSIKKDEEVLKKNCPHIVVGTPGR ILALARNKSLNLKHIKHFILDECDKMLEQLDMRRDVQEIFRMTPHEKQVMMFSATLSKEI RPVCRKFMQDPMEIFVDDETKLTLHGLQQYYVKLKDNEKNRKLFDLLDVLEFNQVVIFVK SVQRCIALAQLLVEQNFPAIAIHRGMPQEERLSRYQQFKDFQRRILVATNLFGRGMDIER VNIAFNYDMPEDSDTYLHRVARAGRFGTKGLAITFVSDENDAKILNDVQDRFEVNISELP DEIDISSYIEQTR
Structural mechanism of DDX39B regulation by human TREX-2 and a related complex in mRNP remodeling. Clarke, B.P., Gao, S., Mei, M. et al. Nat Commun (2025) 16:5471-5471. DOI 10.1038/s41467-025-60547-1 · PubMed
Other PDB entries of the same protein (UniProt O60318 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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