Cryo-EM structure of the human TREX complex. Determined by electron microscopy at 4.12 Å resolution. Released 11 Jun 2025.
Explore 8R7L in 3D Show helices and sheets RCSB PDB PDBe
8R7L contains 92 α-helices and 46 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 |
|---|---|---|---|
| α-helix | 45-64 | 20 | |
| α-helix | 72-83 | 12 | |
| α-helix | 92-103 | 12 | |
| α-helix | 107-119 | 13 | |
| α-helix | 134-146 | 13 | |
| α-helix | 153-166 | 14 | |
| α-helix | 232-246 | 15 | |
| α-helix | 248-250 | 3 | |
| α-helix | 255-274 | 20 | |
| α-helix | 310-313 | 4 | |
| α-helix | 315-333 | 19 | |
| α-helix | 347-365 | 19 | |
| α-helix | 371-388 | 18 | |
| α-helix | 436-442 | 7 | |
| α-helix | 490-502 | 13 | |
| α-helix | 518-527 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 143-155 | 13 | |
| α-helix | 169-179 | 11 | |
| α-helix | 189-203 | 15 | |
| α-helix | 207-220 | 14 | |
| α-helix | 226-236 | 11 | |
| α-helix | 243-253 | 11 | |
| α-helix | 264-275 | 12 | |
| α-helix | 281-286 | 6 | |
| α-helix | 293-307 | 15 | |
| α-helix | 344-352 | 9 | |
| α-helix | 359-365 | 7 | |
| α-helix | 373-375 | 3 | |
| α-helix | 377-398 | 22 | |
| α-helix | 401 | 1 | |
| α-helix | 426 | 1 | |
| α-helix | 427-431 | 5 | |
| α-helix | 432-436 | 5 | |
| α-helix | 442-444 | 3 | |
| α-helix | 446-463 | 18 | |
| α-helix | 474-486 | 13 | |
| α-helix | 487-491 | 5 | |
| α-helix | 492-495 | 4 | |
| α-helix | 504-512 | 9 | |
| α-helix | 517-529 | 13 | |
| α-helix | 536-553 | 18 | |
| α-helix | 565-574 | 10 | |
| α-helix | 576-590 | 15 | |
| α-helix | 594-600 | 7 | |
| α-helix | 606-621 | 16 | |
| α-helix | 637-652 | 16 | |
| α-helix | 659-670 | 12 | |
| α-helix | 676-685 | 10 | |
| α-helix | 697-701 | 5 | |
| α-helix | 708-712 | 5 | |
| α-helix | 723-736 | 14 | |
| α-helix | 739-755 | 17 | |
| α-helix | 765-787 | 23 | |
| α-helix | 790-796 | 7 | |
| α-helix | 800-806 | 7 | |
| α-helix | 811-822 | 12 | |
| α-helix | 861-868 | 8 | |
| α-helix | 878-886 | 9 | |
| α-helix | 900-907 | 8 | |
| α-helix | 929-960 | 32 | |
| α-helix | 973-977 | 5 | |
| α-helix | 978-982 | 5 | |
| α-helix | 983-988 | 6 | |
| α-helix | 990-998 | 9 | |
| α-helix | 999-1003 | 5 | |
| α-helix | 1004-1005 | 2 | |
| α-helix | 1013-1022 | 10 | |
| α-helix | 1024-1029 | 6 | |
| α-helix | 1035-1054 | 20 | |
| α-helix | 1091-1112 | 22 | |
| α-helix | 1118-1129 | 12 | |
| α-helix | 1138-1153 | 16 | |
| α-helix | 1161-1175 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 33-44 | 12 | |
| β-strand | 47 | 1 | 4 |
| β-strand | 50-54 | 5 | 5 |
| β-strand | 58-63 | 6 | 6 |
| β-strand | 69-74 | 6 | 6 |
| β-strand | 78-84 | 7 | 6 |
| β-strand | 89-96 | 8 | 6 |
| β-strand | 104-107 | 4 | 7 |
| β-strand | 114-118 | 5 | 7 |
| β-strand | 123-128 | 6 | 7 |
| β-strand | 133-139 | 7 | 7 |
| β-strand | 144-149 | 6 | 8 |
| β-strand | 155-160 | 6 | 8 |
| β-strand | 164-169 | 6 | 8 |
| β-strand | 175-180 | 6 | 8 |
| β-strand | 185-190 | 6 | 9 |
| β-strand | 196-201 | 6 | 9 |
| β-strand | 205-210 | 6 | 9 |
| β-strand | 215-221 | 7 | 9 |
| β-strand | 227-232 | 6 | 10 |
| β-strand | 238-243 | 6 | 10 |
| β-strand | 248-252 | 5 | 10 |
| β-strand | 258-262 | 5 | 10 |
| β-strand | 269-274 | 6 | 11 |
| β-strand | 280-285 | 6 | 11 |
| β-strand | 289-294 | 6 | 11 |
| β-strand | 303-305 | 3 | 11 |
| β-strand | 313-315 | 3 | 5 |
| β-strand | 322-324 | 3 | 5 |
| β-strand | 340-345 | 6 | 5 |
| β-strand | 346 | 1 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-6 | 3 | |
| α-helix | 9-20 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 54-63 | 10 | |
| α-helix | 70-79 | 10 | |
| β-strand | 85-88 | 4 | 1 |
| α-helix | 96-106 | 11 | |
| β-strand | 116-119 | 4 | 1 |
| α-helix | 123-136 | 14 | |
| β-strand | 145-148 | 4 | 1 |
| α-helix | 154-162 | 9 | |
| β-strand | 168-171 | 4 | 1 |
| α-helix | 173-180 | 8 | |
| β-strand | 192-196 | 5 | 1 |
| α-helix | 198-203 | 6 | |
| α-helix | 205-217 | 13 | |
| β-strand | 223-228 | 6 | 1 |
| α-helix | 236-239 | 4 | |
| α-helix | 240-242 | 3 | |
| β-strand | 247-249 | 3 | 1 |
| β-strand | 258 | 1 | 2 |
| β-strand | 262-268 | 7 | 3 |
| α-helix | 274-284 | 11 | |
| β-strand | 289-293 | 5 | 3 |
| α-helix | 297-309 | 13 | |
| β-strand | 314-317 | 4 | 3 |
| α-helix | 323-334 | 12 | |
| β-strand | 340-343 | 4 | 3 |
| β-strand | 356-361 | 6 | 3 |
| α-helix | 368-375 | 8 | |
| β-strand | 377 | 1 | 2 |
| β-strand | 385-391 | 7 | 3 |
| α-helix | 394-407 | 14 | |
| β-strand | 411-413 | 3 | 3 |
| α-helix | 414 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Spliceosome RNA helicase DDX39B | H | protein | 428 | Homo sapiens | Q13838 (AlphaFold model) |
| THO complex subunit 1 | A | protein | 657 | Homo sapiens | Q96FV9 (AlphaFold model) |
| THO complex subunit 2 | B | protein | 1593 | Homo sapiens | Q8NI27 (AlphaFold model) |
| THO complex subunit 3 | C | protein | 351 | Homo sapiens | Q96J01 (AlphaFold model) |
| THO complex subunit 4 | D | protein | 183 | Homo sapiens | Q86V81 |
>8R7L_1 Spliceosome RNA helicase DDX39B (chains H) MAENDVDNELLDYEDDEVETAAGGDGAEAPAKKDVKGSYVSIHSSGFRDFLLKPELLRAI VDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLATLQQLEPVTGQVSVLVMC HTRELAFQISKEYERFSKYMPNVKVAVFFGGLSIKKDEEVLKKNCPHIVVGTPGRILALA RNKSLNLKHIKHFILDECDKMLEQLDMRRDVQEIFRMTPHEKQVMMFSATLSKEIRPVCR KFMQDPMEIFVDDETKLTLHGLQQYYVKLKDNEKNRKLFDLLDVLEFNQVVIFVKSVQRC IALAQLLVEQNFPAIAIHRGMPQEERLSRYQQFKDFQRRILVATNLFGRGMDIERVNIAF NYDMPEDSDTYLHRVARAGRFGTKGLAITFVSDENDAKILNDVQDRFEVNISELPDEIDI SSYIEQTR
>8R7L_2 THO complex subunit 1 (chains A) MSPTPPLFSLPEARTRFTKSTREALNNKNIKPLLSTFSQVPGSENEKKCTLDQAFRGILE EEIINHSSCENVLAIISLAIGGVTEGICTASTPFVLLGDVLDCLPLDQCDTIFTFVEKNV ATWKSNTFYSAGKNYLLRMCNDLLRRLSKSQNTVFCGRIQLFLARLFPLSEKSGLNLQSQ FNLENVTVFNTNEQESTLGQKHTEDREEGMDVEEGEMGDEEAPTTCSIPIDYNLYRKFWS LQDYFRNPVQCYEKISWKTFLKYSEEVLAVFKSYKLDDTQASRKKMEELKTGGEHVYFAK FLTSEKLMDLQLSDSNFRRHILLQYLILFQYLKGQVKFKSSNYVLTDEQSLWIEDTTKSV YQLLSENPPDGERFSKMVEHILNTEENWNSWKNEGCPSFVKERTSDTKPTRIIRKRTAPE DFLGKGPTKKILMGNEELTRLWNLCPDNMEACKSETREHMPTLEEFFEEAIEQADPENMV ENEYKAVNNSNYGWRALRLLARRSPHFFQPTNQQFKSLPEYLENMVIKLAKELPPPSEEI KTGEDEDEEDNDALLKENESPDVRRDKPVTGEQIEVFANKLGEQWKILAPYLEMKDSEIR QIECDSEDMKMRAKQLLVAWQDQEGVHATPENLINALNKSGLSDLAESLTNDNETNS
>8R7L_3 THO complex subunit 2 (chains B) MAAAAVVVPAEWIKNWEKSGRGEFLHLCRILSENKSHDSSTYRDFQQALYELSYHVIKGN LKHEQASNVLSDISEFREDMPSILADVFCILDIETNCLEEKSKRDYFTQLVLACLYLVSD TVLKERLDPETLESLGLIKQSQQFNQKSVKIKTKLFYKQQKFNLLREENEGYAKLIAELG QDLSGSITSDLILENIKSLIGCFNLDPNRVLDVILEVFECRPEHDDFFISLLESYMSMCE PQTLCHILGFKFKFYQEPNGETPSSLYRVAAVLLQFNLIDLDDLYVHLLPADNCIMDEHK REIAEAKQIVRKLTMVVLSSEKMDEREKEKEKEEEKVEKPPDNQKLGLLEALLKIGDWQH AQNIMDQMPPYYAASHKLIALAICKLIHITIEPLYRRVGVPKGAKGSPVNALQNKRAPKQ AESFEDLRRDVFNMFCYLGPHLSHDPILFAKVVRIGKSFMKEFQSDGSKQEDKEKTEVIL SCLLSITDQVLLPSLSLMDCNACMSEELWGMFKTFPYQHRYRLYGQWKNETYNSHPLLVK VKAQTIDRAKYIMKRLTKENVKPSGRQIGKLSHSNPTILFDYILSQIQKYDNLITPVVDS LKYLTSLNYDVLAYCIIEALANPEKERMKHDDTTISSWLQSLASFCGAVFRKYPIDLAGL LQYVANQLKAGKSFDLLILKEVVQKMAGIEITEEMTMEQLEAMTGGEQLKAEGGYFGQIR NTKKSSQRLKDALLDHDLALPLCLLMAQQRNGVIFQEGGEKHLKLVGKLYDQCHDTLVQF GGFLASNLSTEDYIKRVPSIDVLCNEFHTPHDAAFFLSRPMYAHHISSKYDELKKSEKGS KQQHKVHKYITSCEMVMAPVHEAVVSLHVSKVWDDISPQFYATFWSLTMYDLAVPHTSYE REVNKLKVQMKAIDDNQEMPPNKKKKEKERCTALQDKLLEEEKKQMEHVQRVLQRLKLEK DNWLLAKSTKNETITKFLQLCIFPRCIFSAIDAVYCARFVELVHQQKTPNFSTLLCYDRV FSDIIYTVASCTENEASRYGRFLCCMLETVTRWHSDRATYEKECGNYPGFLTILRATGFD GGNKADQLDYENFRHVVHKWHYKLTKASVHCLETGEYTHIRNILIVLTKILPWYPKVLNL GQALERRVHKICQEEKEKRPDLYALAMGYSGQLKSRKSYMIPENEFHHKDPPPRNAVASV QNGPGGGPSSSSIGSASKSDESSTEETDKSRERSQCGVKAVNKASSTTPKGNSSNGNSGS NSNKAVKENDKEKGKEKEKEKKEKTPATTPEARVLGKDGKEKPKEERPNKDEKARETKER TPKSDKEKEKFKKEEKAKDEKFKTTVPNAESKSTQEREREKEPSRERDIAKEMKSKENVK GGEKTPVSGSLKSPVPRSDIPEPEREQKRRKIDTHPSPSHSSTVKDSLIELKESSAKLYI NHTPPPLSKSKEREMDKKDLDKSRERSREREKKDEKDRKERKRDHSNNDREVPPDLTKRR KEENGTMGVSKHKSESPCESPYPNEKDKEKNKSKSSGKEKGSDSFKSEKMDKISSGGKKE SRHDKEKIEKKEKRDSSGGKEEKKHHKSSDKHR
>8R7L_4 THO complex subunit 3 (chains C) MAVPAAAMGPSALGQSGPGSMAPWCSVSSGPSRYVLGMQELFRGHSKTREFLAHSAKVHS VAWSCDGRRLASGSFDKTASVFLLEKDRLVKENNYRGHGDSVDQLCWHPSNPDLFVTASG DKTIRIWDVRTTKCIATVNTKGENINICWSPDGQTIAVGNKDDVVTFIDAKTHRSKAEEQ FKFEVNEISWNNDNNMFFLTNGNGCINILSYPELKPVQSINAHPSNCICIKFDPMGKYFA TGSADALVSLWDVDELVCVRCFSRLDWPVRTLSFSHDGKMLASASEDHFIDIAEVETGDK LWEVQCESPTFTVAWHPKRPLLAFACDDKDGKYDSSREAGTVKLFGLPNDS
>8R7L_5 THO complex subunit 4 (chains D) MADKMDMSLDDIIKLNRSQRGGRGGGRGRGRAGSQGGRGGGAQAAARVNRGGGPIRNRPA IARGAAGGGGRNRPAPYSRPKQLPDKWQHDLFDSGFGGGAGVETGGKLLVSNLDFGVSDA DIQELFAEFGTLKKAAVHYDRSGRSLGTADVHFERKADALKAMKQYNGVPLDGRPMNIQL VTS
An ATP-gated molecular switch orchestrates human messenger RNA export. Hohmann, U., Graf, M., Tirian, L. et al. Nature (2025). DOI 10.1038/s41586-025-09832-z · 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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