3NC0: HIV-1 Rev NES-CRM1-RanGTP nuclear export complex
Crystal structure of the HIV-1 Rev NES-CRM1-RanGTP nuclear export complex (crystal II). Determined by X-ray diffraction at 2.9 Å resolution. Released 27 Oct 2010.
- Method
- X-ray diffraction
- Resolution
- 2.9 Å
- Organisms
- Mus musculus, Homo sapiens
- Chains
- 6
- Atoms
- 25,190
- Mol. weight
- 373.37 kDa
- Ligands
- MG, GTP, IPH
- Released
- 27 Oct 2010
Explore 3NC0 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
3NC0 contains 165 α-helices and 52 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: 68 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 27-34 | 8 | |
| α-helix | 39-48 | 10 | |
| α-helix | 58-65 | 8 | |
| α-helix | 73-89 | 17 | |
| α-helix | 91-93 | 3 | |
| α-helix | 96-114 | 19 | |
| α-helix | 124-145 | 22 | |
| α-helix | 149-159 | 11 | |
| α-helix | 162-175 | 14 | |
| α-helix | 176-180 | 5 | |
| β-strand | 183 | 1 | 1 |
| β-strand | 186 | 1 | 1 |
| α-helix | 188-200 | 13 | |
| α-helix | 202-215 | 14 | |
| α-helix | 219-230 | 12 | |
| α-helix | 239-242 | 4 | |
| α-helix | 246-249 | 4 | |
| α-helix | 250-254 | 5 | |
| α-helix | 258-260 | 3 | |
| α-helix | 261-271 | 11 | |
| α-helix | 280-297 | 18 | |
| α-helix | 304-309 | 6 | |
| α-helix | 315-339 | 25 | |
| α-helix | 346-357 | 12 | |
| α-helix | 363-379 | 17 | |
| α-helix | 387-388 | 2 | |
| α-helix | 392-393 | 2 | |
| α-helix | 406-423 | 18 | |
| α-helix | 424-426 | 3 | |
| β-strand | 430-432 | 3 | 2 |
| β-strand | 442-444 | 3 | 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 | 552-555 | 4 | |
| α-helix | 559-572 | 14 | |
| α-helix | 580-595 | 16 | |
| α-helix | 596-599 | 4 | |
| α-helix | 602-603 | 2 | |
| α-helix | 610-615 | 6 | |
| α-helix | 618-622 | 5 | |
| α-helix | 627-641 | 15 | |
| α-helix | 647-657 | 11 | |
| α-helix | 659-672 | 14 | |
| α-helix | 678-680 | 3 | |
| α-helix | 682-702 | 21 | |
| α-helix | 704-706 | 3 | |
| α-helix | 707-735 | 29 | |
| α-helix | 737-740 | 4 | |
| α-helix | 743-764 | 22 | |
| α-helix | 769-775 | 7 | |
| α-helix | 778-780 | 3 | |
| α-helix | 781-785 | 5 | |
| α-helix | 786-790 | 5 | |
| α-helix | 793-795 | 3 | |
| α-helix | 798-811 | 14 | |
| α-helix | 812-814 | 3 | |
| α-helix | 819-831 | 13 | |
| α-helix | 842-858 | 17 | |
| α-helix | 862-865 | 4 | |
| α-helix | 868-881 | 14 | |
| α-helix | 887-906 | 20 | |
| α-helix | 908-930 | 23 | |
| α-helix | 936-938 | 3 | |
| α-helix | 939-953 | 15 | |
| α-helix | 970-985 | 16 | |
| α-helix | 991-1003 | 13 | |
| α-helix | 1008-1022 | 15 | |
| α-helix | 1035-1041 | 7 | |
| α-helix | 1043-1046 | 4 | |
Chain B: 8 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 9-11 | 3 | |
| β-strand | 20 | 1 | 3 |
| α-helix | 42-50 | 9 | |
| α-helix | 58-67 | 10 | |
| β-strand | 103-107 | 5 | 3 |
| α-helix | 115-118 | 4 | |
| β-strand | 119-125 | 7 | 3 |
| β-strand | 128-135 | 8 | 4 |
| β-strand | 138-142 | 5 | 4 |
| β-strand | 148-152 | 5 | 4 |
| β-strand | 170-177 | 8 | 4 |
| β-strand | 182-191 | 10 | 4 |
| β-strand | 194-195 | 2 | 4 |
| α-helix | 201-211 | 11 | |
| β-strand | 228-231 | 4 | 4 |
| α-helix | 232-233 | 2 | |
| β-strand | 235-236 | 2 | 3 |
| α-helix | 239-245 | 7 | |
| β-strand | 254-261 | 8 | 3 |
| β-strand | 269-277 | 9 | 3 |
| α-helix | 279-282 | 4 | |
Chain C: 8 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 10-17 | 8 | 5 |
| α-helix | 23-32 | 10 | |
| α-helix | 41-43 | 3 | |
| β-strand | 45-54 | 10 | 5 |
| β-strand | 57-66 | 10 | 5 |
| α-helix | 77-79 | 3 | |
| β-strand | 85-91 | 7 | 5 |
| α-helix | 96-99 | 4 | |
| α-helix | 101-109 | 9 | |
| β-strand | 117-122 | 6 | 5 |
| α-helix | 133-135 | 3 | |
| α-helix | 138-142 | 5 | |
| β-strand | 145-148 | 4 | 5 |
| β-strand | 150 | 1 | 6 |
| β-strand | 155 | 1 | 6 |
| α-helix | 159-168 | 10 | |
| β-strand | 176 | 1 | 5 |
Chain D: 66 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 27-34 | 8 | |
| α-helix | 39-48 | 10 | |
| α-helix | 58-65 | 8 | |
| α-helix | 73-89 | 17 | |
| α-helix | 91-93 | 3 | |
| α-helix | 96-113 | 18 | |
| α-helix | 124-145 | 22 | |
| α-helix | 149-159 | 11 | |
| α-helix | 162-175 | 14 | |
| α-helix | 176-180 | 5 | |
| β-strand | 183 | 1 | 7 |
| β-strand | 186 | 1 | 7 |
| α-helix | 188-200 | 13 | |
| α-helix | 202-215 | 14 | |
| α-helix | 219-230 | 12 | |
| α-helix | 239-242 | 4 | |
| α-helix | 246-249 | 4 | |
| α-helix | 250-254 | 5 | |
| α-helix | 258-260 | 3 | |
| α-helix | 261-271 | 11 | |
| α-helix | 280-297 | 18 | |
| α-helix | 304-309 | 6 | |
| α-helix | 315-333 | 19 | |
| α-helix | 336-339 | 4 | |
| α-helix | 346-357 | 12 | |
| α-helix | 363-379 | 17 | |
| α-helix | 387-388 | 2 | |
| α-helix | 406-423 | 18 | |
| α-helix | 424-426 | 3 | |
| β-strand | 430-434 | 5 | 8 |
| β-strand | 440-444 | 5 | 8 |
| 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 | 552-555 | 4 | |
| α-helix | 559-572 | 14 | |
| α-helix | 580-600 | 21 | |
| α-helix | 602-603 | 2 | |
| α-helix | 610-615 | 6 | |
| α-helix | 618-622 | 5 | |
| α-helix | 627-641 | 15 | |
| α-helix | 647-657 | 11 | |
| α-helix | 659-672 | 14 | |
| α-helix | 676-680 | 5 | |
| α-helix | 682-702 | 21 | |
| α-helix | 704-706 | 3 | |
| α-helix | 707-735 | 29 | |
| α-helix | 737-740 | 4 | |
| α-helix | 743-765 | 23 | |
| α-helix | 769-775 | 7 | |
| α-helix | 778-780 | 3 | |
| α-helix | 781-785 | 5 | |
| α-helix | 786-790 | 5 | |
| α-helix | 793-795 | 3 | |
| α-helix | 798-811 | 14 | |
| α-helix | 812-814 | 3 | |
| α-helix | 819-831 | 13 | |
| α-helix | 842-858 | 17 | |
| α-helix | 862-865 | 4 | |
| α-helix | 868-882 | 15 | |
| α-helix | 887-906 | 20 | |
| α-helix | 908-930 | 23 | |
| α-helix | 936-938 | 3 | |
| α-helix | 939-953 | 15 | |
| α-helix | 970-985 | 16 | |
| α-helix | 991-1003 | 13 | |
| α-helix | 1008-1023 | 16 | |
| α-helix | 1035-1051 | 17 | |
Chain E: 8 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 9-11 | 3 | |
| β-strand | 20 | 1 | 9 |
| α-helix | 42-50 | 9 | |
| α-helix | 58-67 | 10 | |
| β-strand | 103-107 | 5 | 9 |
| α-helix | 115-118 | 4 | |
| β-strand | 119-125 | 7 | 9 |
| β-strand | 128-135 | 8 | 10 |
| β-strand | 138-142 | 5 | 10 |
| β-strand | 148-152 | 5 | 10 |
| β-strand | 170-177 | 8 | 10 |
| β-strand | 182-191 | 10 | 10 |
| β-strand | 194-195 | 2 | 10 |
| α-helix | 201-211 | 11 | |
| β-strand | 228-231 | 4 | 10 |
| α-helix | 232-233 | 2 | |
| β-strand | 235-236 | 2 | 9 |
| α-helix | 239-245 | 7 | |
| β-strand | 254-261 | 8 | 9 |
| β-strand | 269-277 | 9 | 9 |
| α-helix | 281-285 | 5 | |
Chain F: 7 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 9-17 | 9 | 11 |
| α-helix | 23-31 | 9 | |
| α-helix | 41-43 | 3 | |
| β-strand | 45-54 | 10 | 11 |
| β-strand | 57-66 | 10 | 11 |
| β-strand | 85-91 | 7 | 11 |
| α-helix | 96-99 | 4 | |
| α-helix | 101-109 | 9 | |
| β-strand | 117-122 | 6 | 11 |
| α-helix | 133-135 | 3 | |
| α-helix | 138-142 | 5 | |
| β-strand | 145-148 | 4 | 11 |
| β-strand | 150 | 1 | 12 |
| β-strand | 155 | 1 | 12 |
| α-helix | 159-168 | 10 | |
| β-strand | 176 | 1 | 11 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Exportin-1 | A, D | protein | 1073 | Mus musculus | Q6P5F9 (AlphaFold model) |
| Snurportin-1 | B, E | protein | 362 | Homo sapiens | O95149 (AlphaFold model) |
| GTP-binding nuclear protein Ran | C, F | protein | 176 | Homo sapiens | P62826 (AlphaFold model) |
Sequence of entity 1 (A, D), FASTA
>3NC0_1 Exportin-1 (chains A, D)
GSMPAIMTMLADHAARQLLDFSQKLDINLLDNVVNCLYHGEGAQQRMAQEVLTHLKEHPD
AWTRVDTILEFSQNMNTKYYGLQILENVIKTRWKILPRNQCEGIKKYVVGLIIKTSSDPT
CVEKEKVYIGKLNMILVQILKQEWPKHWPTFISDIVGASRTSESLCQNNMVILKLLSEEV
FDFSSGQITQVKAKHLKDSMCNEFSQIFQLCQFVMENSQNAPLVHATLETLLRFLNWIPL
GYIFETKLISTLIYKFLNVPMFRNVSLKCLTEIAGVSVSQYEEQFETLFTLTMMQLKQML
PLNTNIRLAYSNGKDDEQNFIQNLSLFLCTFLKEHGQLLEKRLNLREALMEALHYMLLVS
EVEETEIFKICLEYWNHLAAELYRESPFSTSASPLLSGSQHFDIPPRRQLYLTVLSKVRL
LMVSRMAKPEEVLVVENDQGEVVREFMKDTDSINLYKNMRETLVYLTHLDYVDTEIIMTK
KLQNQVNGTEWSWKNLNTLCWAIGSISGAMHEEDEKRFLVTVIKDLLGLCEQKRGKDNKA
IIASNIMYIVGQYPRFLRAHWKFLKTVVNKLFEFMHETHDGVQDMACDTFIKIAQKCRRH
FVQVQVGEVMPFIDEILNNINTIICDLQPQQVHTFYEAVGYMIGAQTDQTVQEHLIEKYM
LLPNQVWDSIIQQATKNVDILKDPETVKQLGSILKTNVRACKAVGHPFVIQLGRIYLDML
NVYKCLSENISAAIQANGEMVTKQPLIRSMRTVKRETLKLISGWVSRSNDPQMVAENFVP
PLLDAVLIDYQRNVPAAREPEVLSTMAIIVNKLGGHITAEIPQIFDAVFECTLNMINKDF
EEYPEHRTNFFLLLQAVNSHCFPAFLAIPPAQFKLVLDSIIWAFKHTMRNVADTGLQILF
TLLQNVAQEEAAAQSFYQTYFCDILQHIFSVVTDTSHTAGLTMHASILAYMFNLVEEGKI
STPLNPGNPVNNQMFIQDYVANLLKSAFPHLQDAQVKLFVTGLFSLNQDIPAFKEHLRDF
LVQIKEFAGEDTSDLFLEERETALRQAQEEKHKLQMSVPGILNPHEIPEEMCD
Sequence of entity 2 (B, E), FASTA
>3NC0_2 Snurportin-1 (chains B, E)
GSPVPLQLPPLERLTLSQDLNSTAAPHPRLSQYKSKYSSLEQSERRRRLLELQKSKRLDY
VNHARRLAEDDWTGMESEEENKKDDEEMDIDTVKKLPKHYANQLMLSEWLIDVPSDLGQE
WIVVVCPVGKRALIVASRGSTSAYTKSGYCVNRFSSLLPGGNRRNSTAKDYTILDCIYNE
VNQTYYVLDVMCWRGHPFYDCQTDFRFYWMHSKLPEEEGLGEKTKLNPFKFVGLKNFPCT
PESLCDVLSMDFPFEVDGLLFYHKQTHYSPGSTPLVGWLRPYMVSDVLGVAVPAGPLTTK
PDYAGHQLQQIMEHKKSQKEGMKEKLTHKASENGHYELEHLSTPKLKGSSHSPDHPGCLM
EN
Sequence of entity 3 (C, F), FASTA
>3NC0_3 GTP-binding nuclear protein Ran (chains C, F)
GEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIKFNVW
DTAGLEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKV
DIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVAMP
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| MG | Magnesium ion | Mg | 2 |
| GTP | Guanosine-5'-triphosphate | C10 H16 N5 O14 P3 | 2 |
| IPH | Phenol | C6 H6 O | 1 |
Water and common crystallization additives (PEG, GOL) are not listed.
Primary citation
NES consensus redefined by structures of PKI-type and Rev-type nuclear export signals bound to CRM1. Guttler, T., Madl, T., Neumann, P. et al. Nat Struct Mol Biol (2010) 17:1367-1376. DOI 10.1038/nsmb.1931 · PubMed
Other PDB entries of the same protein (UniProt Q6P5F9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 3GJX 2.5 Å, Crystal Structure of the Nuclear Export Complex CRM1-Snurportin1-RanGTP
- 3NBZ 2.8 Å, Crystal structure of the HIV-1 Rev NES-CRM1-RanGTP nuclear export complex (crystal I)
- 3NC1 3.35 Å, Crystal structure of the CRM1-RanGTP complex
- 3NBY 3.42 Å, Crystal structure of the PKI NES-CRM1-RanGTP nuclear export complex
Browse structure collections
About this viewer
MolViewer shows 3NC0 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.