8URJ: HIV-1 nuclear export complex
Cryo-EM structure of the HIV-1 nuclear export complex. Determined by electron microscopy at 4.25 Å resolution. Released 30 Apr 2025.
- Method
- Electron microscopy
- Resolution
- 4.25 Å
- Organisms
- Homo sapiens, Human immunodeficiency virus 1
- Chains
- 7
- Atoms
- 21,963
- Mol. weight
- 422.31 kDa
- Released
- 30 Apr 2025
Explore 8URJ in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
8URJ contains 164 α-helices and 24 β-strands across 6 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.
Chain A: 67 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 10-15 | 6 | |
| α-helix | 25-37 | 13 | |
| α-helix | 40-54 | 15 | |
| α-helix | 60-69 | 10 | |
| α-helix | 73-90 | 18 | |
| α-helix | 96-115 | 20 | |
| α-helix | 117-122 | 6 | |
| α-helix | 124-141 | 18 | |
| α-helix | 149-159 | 11 | |
| α-helix | 161-175 | 15 | |
| α-helix | 176-180 | 5 | |
| α-helix | 188-215 | 28 | |
| α-helix | 219-232 | 14 | |
| α-helix | 239-242 | 4 | |
| α-helix | 246-249 | 4 | |
| α-helix | 250-254 | 5 | |
| α-helix | 258-272 | 15 | |
| α-helix | 277-279 | 3 | |
| α-helix | 280-297 | 18 | |
| α-helix | 304-310 | 7 | |
| α-helix | 313-338 | 26 | |
| α-helix | 341-343 | 3 | |
| α-helix | 344-358 | 15 | |
| α-helix | 363-388 | 26 | |
| α-helix | 397-400 | 4 | |
| α-helix | 404-423 | 20 | |
| α-helix | 424-426 | 3 | |
| β-strand | 430-434 | 5 | 1 |
| β-strand | 440-444 | 5 | 1 |
| α-helix | 449-467 | 19 | |
| α-helix | 469-484 | 16 | |
| α-helix | 491-503 | 13 | |
| α-helix | 510-530 | 21 | |
| α-helix | 534-550 | 17 | |
| α-helix | 552-557 | 6 | |
| α-helix | 559-573 | 15 | |
| α-helix | 580-600 | 21 | |
| α-helix | 602-603 | 2 | |
| α-helix | 610-616 | 7 | |
| α-helix | 618-622 | 5 | |
| α-helix | 627-642 | 16 | |
| α-helix | 647-657 | 11 | |
| α-helix | 659-674 | 16 | |
| α-helix | 677-680 | 4 | |
| α-helix | 682-702 | 21 | |
| α-helix | 706-735 | 30 | |
| α-helix | 736-741 | 6 | |
| α-helix | 743-764 | 22 | |
| α-helix | 769-771 | 3 | |
| α-helix | 772-776 | 5 | |
| α-helix | 777-780 | 4 | |
| α-helix | 781-786 | 6 | |
| α-helix | 787-790 | 4 | |
| α-helix | 793-795 | 3 | |
| α-helix | 798-811 | 14 | |
| α-helix | 812-818 | 7 | |
| α-helix | 819-834 | 16 | |
| α-helix | 842-858 | 17 | |
| α-helix | 860-865 | 6 | |
| α-helix | 868-882 | 15 | |
| α-helix | 887-906 | 20 | |
| α-helix | 908-931 | 24 | |
| α-helix | 933-938 | 6 | |
| α-helix | 939-954 | 16 | |
| α-helix | 970-985 | 16 | |
| α-helix | 991-1003 | 13 | |
| α-helix | 1008-1022 | 15 | |
| α-helix | 1031-1033 | 3 | |
| α-helix | 1035-1055 | 21 | |
Chain B: 5 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 15-25 | 11 | |
| α-helix | 27-30 | 4 | |
| α-helix | 35-61 | 27 | |
| α-helix | 72-76 | 5 | |
| α-helix | 77-85 | 9 | |
Chain C: 68 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 10-15 | 6 | |
| α-helix | 25-37 | 13 | |
| α-helix | 40-55 | 16 | |
| α-helix | 57-59 | 3 | |
| α-helix | 60-69 | 10 | |
| α-helix | 73-90 | 18 | |
| α-helix | 96-115 | 20 | |
| α-helix | 117-122 | 6 | |
| α-helix | 124-141 | 18 | |
| α-helix | 149-159 | 11 | |
| α-helix | 161-175 | 15 | |
| α-helix | 176-180 | 5 | |
| α-helix | 188-200 | 13 | |
| α-helix | 202-215 | 14 | |
| α-helix | 219-232 | 14 | |
| α-helix | 239-242 | 4 | |
| α-helix | 246-249 | 4 | |
| α-helix | 250-255 | 6 | |
| α-helix | 258-272 | 15 | |
| α-helix | 280-297 | 18 | |
| α-helix | 304-310 | 7 | |
| α-helix | 313-338 | 26 | |
| α-helix | 341-343 | 3 | |
| α-helix | 344-358 | 15 | |
| α-helix | 363-379 | 17 | |
| α-helix | 385-390 | 6 | |
| α-helix | 397-400 | 4 | |
| α-helix | 404-422 | 19 | |
| α-helix | 424-426 | 3 | |
| β-strand | 430-434 | 5 | 2 |
| β-strand | 440-444 | 5 | 2 |
| α-helix | 449-467 | 19 | |
| α-helix | 469-484 | 16 | |
| α-helix | 491-503 | 13 | |
| α-helix | 510-530 | 21 | |
| α-helix | 534-550 | 17 | |
| α-helix | 552-556 | 5 | |
| α-helix | 559-573 | 15 | |
| α-helix | 580-600 | 21 | |
| α-helix | 602-603 | 2 | |
| α-helix | 610-621 | 12 | |
| α-helix | 622-624 | 3 | |
| α-helix | 627-642 | 16 | |
| α-helix | 647-657 | 11 | |
| α-helix | 659-674 | 16 | |
| α-helix | 676-680 | 5 | |
| α-helix | 682-702 | 21 | |
| α-helix | 704-706 | 3 | |
| α-helix | 707-735 | 29 | |
| α-helix | 736-741 | 6 | |
| α-helix | 743-764 | 22 | |
| α-helix | 769-775 | 7 | |
| α-helix | 777-780 | 4 | |
| α-helix | 781-786 | 6 | |
| α-helix | 787-790 | 4 | |
| α-helix | 798-811 | 14 | |
| α-helix | 813-816 | 4 | |
| α-helix | 819-834 | 16 | |
| α-helix | 842-858 | 17 | |
| α-helix | 860-865 | 6 | |
| α-helix | 868-882 | 15 | |
| α-helix | 887-906 | 20 | |
| α-helix | 908-931 | 24 | |
| α-helix | 933-938 | 6 | |
| α-helix | 939-954 | 16 | |
| β-strand | 963 | 1 | 3 |
| β-strand | 966 | 1 | 3 |
| α-helix | 970-985 | 16 | |
| α-helix | 991-1003 | 13 | |
| α-helix | 1008-1022 | 15 | |
| α-helix | 1031-1033 | 3 | |
| α-helix | 1035-1055 | 21 | |
Chain D: 10 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 10-16 | 7 | 4 |
| α-helix | 23-31 | 9 | |
| α-helix | 41-43 | 3 | |
| β-strand | 45-54 | 10 | 4 |
| β-strand | 57-66 | 10 | 4 |
| α-helix | 70-72 | 3 | |
| α-helix | 76-80 | 5 | |
| β-strand | 85-91 | 7 | 4 |
| α-helix | 95-99 | 5 | |
| α-helix | 101-111 | 11 | |
| β-strand | 117-122 | 6 | 4 |
| α-helix | 133-135 | 3 | |
| α-helix | 138-142 | 5 | |
| α-helix | 144 | 1 | |
| β-strand | 145-148 | 4 | 4 |
| β-strand | 150 | 1 | 5 |
| β-strand | 155 | 1 | 5 |
| α-helix | 159-169 | 11 | |
| β-strand | 176-177 | 2 | 4 |
Chain E: 5 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 13-24 | 12 | |
| α-helix | 35-59 | 25 | |
| α-helix | 60-64 | 5 | |
| α-helix | 65-68 | 4 | |
| α-helix | 70-82 | 13 | |
Chain H: 9 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 10-17 | 8 | 6 |
| α-helix | 23-31 | 9 | |
| β-strand | 45-54 | 10 | 6 |
| β-strand | 57-66 | 10 | 6 |
| α-helix | 70-72 | 3 | |
| α-helix | 76-80 | 5 | |
| β-strand | 85-91 | 7 | 6 |
| α-helix | 95-99 | 5 | |
| α-helix | 101-111 | 11 | |
| β-strand | 117-122 | 6 | 6 |
| α-helix | 133-135 | 3 | |
| α-helix | 138-142 | 5 | |
| α-helix | 144 | 1 | |
| β-strand | 145-148 | 4 | 6 |
| β-strand | 150 | 1 | 7 |
| β-strand | 155 | 1 | 7 |
| α-helix | 159-169 | 11 | |
| β-strand | 176-177 | 2 | 6 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Exportin-1 | A, C | protein | 1062 | Homo sapiens | O14980 (AlphaFold model) |
| Rev HIV-1 | B | protein | 92 | Human immunodeficiency virus 1 | |
| GTP-binding nuclear protein Ran | D, H | protein | 181 | Homo sapiens | P62826 (AlphaFold model) |
| Rev HIV-1 | E | protein | 92 | Human immunodeficiency virus 1 | P69718 |
| HIV-1 rre | G | RNA | 355 | Human immunodeficiency virus 1 | |
Sequence of entity 1 (A, C), FASTA
>8URJ_1 Exportin-1 (chains A, C)
GAMGSGMPAIMTMLADHAARQLLDFSQKLDINLLDNVVNCLYHGEGAQQRMAQEVLTHLK
EHPDAWTRVDTILEFSQNMNTKYYGLQILENVIKTRWKILPRNQCEGIKKYVVGLIIKTS
SDPTCVEKEKVYIGKLNMILVQILKQEWPKHWPTFISDIVGASRTSESLCQNNMVILKLL
SEEVFDFSSGQITQVKSKHLKDSMCNEFSQIFQLCQFVMENSQNAPLVHATLETLLRFLN
WIPLGYIFETKLISTLIYKFLNVPMFRNVSLKCLTEIAGVSVSQYEEQFVTLFTLTMMQL
KQMLPLNTNIRLAYSNGKDDEQNFIQNLSLFLCTFLKEHDQLIEKRLNLRETLMEALHYM
LLVSEVEETEIFKICLEYWNHLAAELYRESPFSTSASPLLSGSQHFDVPPRRQLYLPMLF
KVRLLMVSRMAKPEEVLVVENDQGEVVREFMKDTDSINLYKNMRETLVYLTHLDYVDTER
IMTEKLHNQVNGTEWSWKNLNTLCWAIGSISGAMHEEDEKRFLVTVIKDLLGLCEQKRGK
DNKAIIASNIMYIVGQYPRFLRAHWKFLKTVVNKLFEFMHETHDGVQDMACDTFIKIAQK
CRRHFVQVQVGEVMPFIDEILNNINTIICDLQPQQVHTFYEAVGYMIGAQTDQTVQEHLI
EKYMLLPNQVWDSIIQQATKNVDILKDPETVKQLGSILKTNVRACKAVGHPFVIQLGRIY
LDMLNVYKCLSENISAAIQANGEMVTKQPLIRSMRTVKRETLKLISGWVSRSNDPQMVAE
NFVPPLLDAVLIDYQRNVPAAREPEVLSTMAIIVNKLGGHITAEIPQIFDAVFECTLNMI
NKDFEEYPEHRTNFFLLLQAVNSHCFPAFLAIPPTQFKLVLDSIIWAFKHTMRNVADTGL
QILFTLLQNVAQEEAAAQSFYQTYFCDILQHIFSVVTDTSHTAGLTMHASILAYMFNLVE
EGKISTSLNPGNPVNNQIFLQEYVANLLKSAFPHLQDAQVKLFVTGLFSLNQDIPAFKEH
LRDFLVQIKEFAGEDTSDLFLEEREIALRQADEEKHKRQMSV
Sequence of entity 2 (B), FASTA
>8URJ_2 Rev HIV-1 (chains B)
AMAGRSGDSDEDLLKAVRLIKFLYQSNPPPNPEGTRQARRNRRRRWRARQRQIHSISERI
RSTYLGRSAEPVPLQTVDEMTKKFGTLTIDCN
Sequence of entity 3 (D, H), FASTA
>8URJ_3 GTP-binding nuclear protein Ran (chains D, H)
GHMTAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGP
IKFNVWDTAGLEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIV
LCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVA
M
Sequence of entity 4 (E), FASTA
>8URJ_4 Rev HIV-1 (chains E)
GAMAGRSGDSDEDLLKAVRLIKFLYQSNPPPNPEGTRQARRNRRRRWRERQRQIHSISER
ILSTYLGRSAEPVPLQTVDEMTKKFGTLTIDC
Sequence of entity 5 (G), FASTA
>8URJ_5 HIV-1 RRE (chains G)
UGAACCAUUAGGAAUAGCACCCACCAAGGCAAAGAGAAGAGUGGUGCAGAGAGAAAAAAG
AGCAGUGGGAAUAGUAGGAGCUAUGUUCCUUGGGUUCUUGGGAGCAGCAGGAAGCACUAU
GGGCGCAGUGUCAUUGACGCUGACGGUACAGGCCAGACAAUUAUUGUCUGGUAUAGUGCA
ACAGCAGAACAAUUUGCUGAGGGCUAUUGAGGCGCAACAACAUCUGUUGCAACUCACAGU
CUGGGGCAUCAAGCAGCUCCAAGCAAGAAUCCUGGCUGUGGAAAGAUACCUAAGGGAUCA
ACAGCUCCUAGGGGAAUUCGGUUGCUCUGGAAAACUCAUUUGCACCACUGCUGUG
Primary citation
Structure of the HIV-1 RNA Nuclear Export Complex Reveals Crm1 Versatility. Smith, A.M., Cheng, Y., Frankel, A.D. et al. To be published.
Other PDB entries of the same protein (UniProt O14980 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 1W9C 2.3 Å, Proteolytic fragment of CRM1 spanning six C-terminal HEAT repeats
- 9OGD 2.49 Å, Cryo-EM structure of human exportin-1 conjugated with selinexor and bound to human…
- 7B51 2.58 Å, Crystal structure of human CRM1 covalently modified by 2-mercaptoethanol at Cys528
- 9HFL 2.62 Å, Cryo-EM structure of the human snRNA export complex comprising CBC-PHAX-CRM1-RanGTP and…
- 5DIS 2.85 Å, Crystal structure of a CRM1-RanGTP-SPN1 export complex bound to a 113 amino acid…
- 3GB8 2.9 Å, Crystal structure of CRM1/Snurportin-1 complex
- 9B62 2.9 Å, Human RANBP2/RAN(GTP)/RANGAP1-SUMO1/UBC9/CRM1/RAN(GTP) - composite map and model
- 9OG9 2.93 Å, Cryo-EM structure of human full-length XPO1 (unliganded)
- 11RM 2.95 Å, Cryo-EM structure of human exportin-1 conjugated with FR-027*
- 6TVO 3.2 Å, Human CRM1-RanGTP in complex with Leptomycin B
- 9OGB 3.25 Å, Cryo-EM structure of human exportin-1 conjugated with selinexor and bound to yeast…
- 9OGE 3.28 Å, Cryo-EM structure of human exportin-1 conjugated with KPT-127 and bound to human…
Browse structure collections
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