3NBY: PKI NES-CRM1-RanGTP nuclear export complex
Crystal structure of the PKI NES-CRM1-RanGTP nuclear export complex. Determined by X-ray diffraction at 3.42 Å resolution. Released 27 Oct 2010.
- Method
- X-ray diffraction
- Resolution
- 3.42 Å
- Organisms
- Homo sapiens, Mus musculus
- Chains
- 6
- Atoms
- 24,084
- Mol. weight
- 370.67 kDa
- Ligands
- MG, GTP
- Released
- 27 Oct 2010
Explore 3NBY in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
3NBY contains 165 α-helices and 47 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: 66 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 27-36 | 10 | |
| α-helix | 41-48 | 8 | |
| α-helix | 59-64 | 6 | |
| α-helix | 72-89 | 18 | |
| α-helix | 90-93 | 4 | |
| α-helix | 96-113 | 18 | |
| α-helix | 124-141 | 18 | |
| α-helix | 149-159 | 11 | |
| α-helix | 162-175 | 14 | |
| α-helix | 176-180 | 5 | |
| α-helix | 182-185 | 4 | |
| β-strand | 186 | 1 | 5 |
| α-helix | 188-200 | 13 | |
| α-helix | 203-215 | 13 | |
| α-helix | 219-230 | 12 | |
| α-helix | 239-242 | 4 | |
| α-helix | 246-248 | 3 | |
| α-helix | 249-255 | 7 | |
| α-helix | 261-271 | 11 | |
| α-helix | 280-296 | 17 | |
| α-helix | 304-309 | 6 | |
| α-helix | 313-332 | 20 | |
| α-helix | 344-357 | 14 | |
| α-helix | 365-383 | 19 | |
| α-helix | 406-408 | 3 | |
| α-helix | 410-423 | 14 | |
| β-strand | 430-433 | 4 | 6 |
| β-strand | 441-444 | 4 | 6 |
| α-helix | 449-466 | 18 | |
| α-helix | 469-484 | 16 | |
| α-helix | 491-503 | 13 | |
| α-helix | 510-530 | 21 | |
| α-helix | 535-549 | 15 | |
| α-helix | 552-557 | 6 | |
| α-helix | 559-572 | 14 | |
| α-helix | 580-594 | 15 | |
| α-helix | 610-615 | 6 | |
| α-helix | 618-621 | 4 | |
| α-helix | 627-641 | 15 | |
| α-helix | 647-657 | 11 | |
| α-helix | 659-673 | 15 | |
| α-helix | 678-680 | 3 | |
| α-helix | 682-702 | 21 | |
| α-helix | 704-706 | 3 | |
| α-helix | 707-733 | 27 | |
| α-helix | 737-740 | 4 | |
| α-helix | 743-764 | 22 | |
| α-helix | 770-775 | 6 | |
| α-helix | 778-780 | 3 | |
| α-helix | 781-786 | 6 | |
| α-helix | 787-790 | 4 | |
| α-helix | 793-795 | 3 | |
| α-helix | 798-809 | 12 | |
| α-helix | 812-815 | 4 | |
| α-helix | 819-834 | 16 | |
| α-helix | 842-859 | 18 | |
| α-helix | 861-864 | 4 | |
| α-helix | 868-882 | 15 | |
| α-helix | 887-906 | 20 | |
| α-helix | 908-914 | 7 | |
| α-helix | 915-919 | 5 | |
| α-helix | 920-930 | 11 | |
| α-helix | 939-953 | 15 | |
| α-helix | 970-985 | 16 | |
| α-helix | 991-1003 | 13 | |
| α-helix | 1004-1006 | 3 | |
| α-helix | 1008-1023 | 16 | |
| α-helix | 1035-1041 | 7 | |
| α-helix | 1043-1052 | 10 | |
Chain B: 9 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-9 | 8 | |
| α-helix | 23-24 | 2 | |
| α-helix | 40-48 | 9 | |
| α-helix | 57-66 | 10 | |
| β-strand | 102-106 | 5 | 1 |
| β-strand | 118-124 | 7 | 1 |
| β-strand | 127-133 | 7 | 2 |
| β-strand | 134 | 1 | 3 |
| β-strand | 137 | 1 | 3 |
| β-strand | 138-141 | 4 | 2 |
| β-strand | 147-151 | 5 | 2 |
| β-strand | 169-176 | 8 | 2 |
| α-helix | 177-179 | 3 | |
| β-strand | 181-189 | 9 | 2 |
| α-helix | 200-210 | 11 | |
| β-strand | 228-230 | 3 | 2 |
| α-helix | 231-232 | 2 | |
| β-strand | 233-235 | 3 | 1 |
| α-helix | 238-244 | 7 | |
| β-strand | 253-260 | 8 | 1 |
| β-strand | 268-276 | 9 | 1 |
| α-helix | 280-282 | 3 | |
Chain C: 9 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 10-17 | 8 | 4 |
| α-helix | 23-29 | 7 | |
| α-helix | 41-43 | 3 | |
| β-strand | 47-54 | 8 | 4 |
| β-strand | 57-65 | 9 | 4 |
| α-helix | 70-72 | 3 | |
| α-helix | 77-80 | 4 | |
| β-strand | 85-91 | 7 | 4 |
| α-helix | 96-99 | 4 | |
| α-helix | 101-109 | 9 | |
| β-strand | 117-122 | 6 | 4 |
| α-helix | 133-135 | 3 | |
| α-helix | 138-142 | 5 | |
| β-strand | 145-148 | 4 | 4 |
| α-helix | 159-169 | 11 | |
| β-strand | 176-177 | 2 | 4 |
Chain D: 65 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 27-36 | 10 | |
| α-helix | 41-48 | 8 | |
| α-helix | 59-64 | 6 | |
| α-helix | 72-89 | 18 | |
| α-helix | 90-93 | 4 | |
| 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 | |
| α-helix | 182-185 | 4 | |
| β-strand | 186 | 1 | 11 |
| α-helix | 188-200 | 13 | |
| α-helix | 203-215 | 13 | |
| α-helix | 219-230 | 12 | |
| α-helix | 239-242 | 4 | |
| α-helix | 246-248 | 3 | |
| α-helix | 249-255 | 7 | |
| α-helix | 261-271 | 11 | |
| α-helix | 280-296 | 17 | |
| α-helix | 304-309 | 6 | |
| α-helix | 313-332 | 20 | |
| α-helix | 344-357 | 14 | |
| α-helix | 365-383 | 19 | |
| α-helix | 406-408 | 3 | |
| α-helix | 410-423 | 14 | |
| β-strand | 430-432 | 3 | 12 |
| β-strand | 442-444 | 3 | 12 |
| α-helix | 449-466 | 18 | |
| α-helix | 469-484 | 16 | |
| α-helix | 491-503 | 13 | |
| α-helix | 510-530 | 21 | |
| α-helix | 535-549 | 15 | |
| α-helix | 552-557 | 6 | |
| α-helix | 559-572 | 14 | |
| α-helix | 580-594 | 15 | |
| α-helix | 610-615 | 6 | |
| α-helix | 618-621 | 4 | |
| α-helix | 627-641 | 15 | |
| α-helix | 647-657 | 11 | |
| α-helix | 659-670 | 12 | |
| α-helix | 678-680 | 3 | |
| α-helix | 682-702 | 21 | |
| α-helix | 704-706 | 3 | |
| α-helix | 707-733 | 27 | |
| α-helix | 737-740 | 4 | |
| α-helix | 743-763 | 21 | |
| α-helix | 770-775 | 6 | |
| α-helix | 778-780 | 3 | |
| α-helix | 781-786 | 6 | |
| α-helix | 787-790 | 4 | |
| α-helix | 793-795 | 3 | |
| α-helix | 798-809 | 12 | |
| α-helix | 812-815 | 4 | |
| α-helix | 819-834 | 16 | |
| α-helix | 842-859 | 18 | |
| α-helix | 861-864 | 4 | |
| α-helix | 868-882 | 15 | |
| α-helix | 887-906 | 20 | |
| α-helix | 908-914 | 7 | |
| α-helix | 915-919 | 5 | |
| α-helix | 920-930 | 11 | |
| α-helix | 939-953 | 15 | |
| α-helix | 970-985 | 16 | |
| α-helix | 991-1003 | 13 | |
| α-helix | 1004-1006 | 3 | |
| α-helix | 1008-1023 | 16 | |
| α-helix | 1035-1052 | 18 | |
Chain E: 9 helices, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-8 | 7 | |
| α-helix | 23-24 | 2 | |
| α-helix | 40-49 | 10 | |
| α-helix | 57-66 | 10 | |
| β-strand | 102-106 | 5 | 7 |
| β-strand | 118-124 | 7 | 7 |
| β-strand | 127-134 | 8 | 8 |
| β-strand | 137-141 | 5 | 8 |
| β-strand | 147-151 | 5 | 8 |
| β-strand | 169-176 | 8 | 8 |
| α-helix | 177-179 | 3 | |
| β-strand | 181-190 | 10 | 8 |
| β-strand | 193-194 | 2 | 8 |
| α-helix | 200-208 | 9 | |
| β-strand | 227-230 | 4 | 8 |
| α-helix | 231-232 | 2 | |
| β-strand | 233-235 | 3 | 7 |
| α-helix | 238-244 | 7 | |
| β-strand | 253-260 | 8 | 7 |
| β-strand | 268-276 | 9 | 7 |
| α-helix | 280-283 | 4 | |
Chain F: 7 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 10-17 | 8 | 9 |
| α-helix | 23-32 | 10 | |
| β-strand | 47-54 | 8 | 9 |
| β-strand | 57-65 | 9 | 9 |
| α-helix | 77-80 | 4 | |
| β-strand | 85-91 | 7 | 9 |
| α-helix | 96-99 | 4 | |
| α-helix | 101-109 | 9 | |
| β-strand | 117-122 | 6 | 9 |
| α-helix | 133-135 | 3 | |
| α-helix | 138-142 | 5 | |
| β-strand | 145-148 | 4 | 9 |
| β-strand | 150 | 1 | 10 |
| β-strand | 155 | 1 | 10 |
| α-helix | 159-169 | 11 | |
| β-strand | 176-177 | 2 | 9 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Snurportin-1 | B, E | protein | 361 | Homo sapiens | O95149 (AlphaFold model) |
| GTP-binding nuclear protein Ran | C, F | protein | 176 | Homo sapiens | P62826 (AlphaFold model) |
| Exportin-1 | A, D | protein | 1073 | Mus musculus | Q6P5F9 (AlphaFold model) |
Sequence of entity 1 (B, E), FASTA
>3NBY_1 Snurportin-1 (chains B, E)
GSLNELALKLAGLDISQDLNSTAAPHPRLSQYKSKYSSLEQSERRRRLLELQKSKRLDYV
NHARRLAEDDWTGMESEEENKKDDEEMDIDTVKKLPKHYANQLMLSEWLIDVPSDLGQEW
IVVVCPVGKRALIVASRGSTSAYTKSGYCVNRFSSLLPGGNRRNSTAKDYTILDCIYNEV
NQTYYVLDVMCWRGHPFYDCQTDFRFYWMHSKLPEEEGLGEKTKLNPFKFVGLKNFPCTP
ESLCDVLSMDFPFEVDGLLFYHKQTHYSPGSTPLVGWLRPYMVSDVLGVAVPAGPLTTKP
DYAGHQLQQIMEHKKSQKEGMKEKLTHKASENGHYELEHLSTPKLKGSSHSPDHPGCLME
N
Sequence of entity 2 (C, F), FASTA
>3NBY_2 GTP-binding nuclear protein Ran (chains C, F)
GEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIKFNVW
DTAGLEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKV
DIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVAMP
Sequence of entity 3 (A, D), FASTA
>3NBY_3 Exportin-1 (chains A, D)
GSMPAIMTMLADHAARQLLDFSQKLDINLLDNVVNCLYHGEGAQQRMAQEVLTHLKEHPD
AWTRVDTILEFSQNMNTKYYGLQILENVIKTRWKILPRNQCEGIKKYVVGLIIKTSSDPT
CVEKEKVYIGKLNMILVQILKQEWPKHWPTFISDIVGASRTSESLCQNNMVILKLLSEEV
FDFSSGQITQVKAKHLKDSMCNEFSQIFQLCQFVMENSQNAPLVHATLETLLRFLNWIPL
GYIFETKLISTLIYKFLNVPMFRNVSLKCLTEIAGVSVSQYEEQFETLFTLTMMQLKQML
PLNTNIRLAYSNGKDDEQNFIQNLSLFLCTFLKEHGQLLEKRLNLREALMEALHYMLLVS
EVEETEIFKICLEYWNHLAAELYRESPFSTSASPLLSGSQHFDIPPRRQLYLTVLSKVRL
LMVSRMAKPEEVLVVENDQGEVVREFMKDTDSINLYKNMRETLVYLTHLDYVDTEIIMTK
KLQNQVNGTEWSWKNLNTLCWAIGSISGAMHEEDEKRFLVTVIKDLLGLCEQKRGKDNKA
IIASNIMYIVGQYPRFLRAHWKFLKTVVNKLFEFMHETHDGVQDMACDTFIKIAQKCRRH
FVQVQVGEVMPFIDEILNNINTIICDLQPQQVHTFYEAVGYMIGAQTDQTVQEHLIEKYM
LLPNQVWDSIIQQATKNVDILKDPETVKQLGSILKTNVRACKAVGHPFVIQLGRIYLDML
NVYKCLSENISAAIQANGEMVTKQPLIRSMRTVKRETLKLISGWVSRSNDPQMVAENFVP
PLLDAVLIDYQRNVPAAREPEVLSTMAIIVNKLGGHITAEIPQIFDAVFECTLNMINKDF
EEYPEHRTNFFLLLQAVNSHCFPAFLAIPPAQFKLVLDSIIWAFKHTMRNVADTGLQILF
TLLQNVAQEEAAAQSFYQTYFCDILQHIFSVVTDTSHTAGLTMHASILAYMFNLVEEGKI
STPLNPGNPVNNQMFIQDYVANLLKSAFPHLQDAQVKLFVTGLFSLNQDIPAFKEHLRDF
LVQIKEFAGEDTSDLFLEERETALRQAQEEKHKLQMSVPGILNPHEIPEEMCD
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| MG | Magnesium ion | Mg | 2 |
| GTP | Guanosine-5'-triphosphate | C10 H16 N5 O14 P3 | 2 |
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 O95149 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 2P8Q 2.35 Å, Crystal Structure of human Importin beta bound to the Snurportin1 IBB-domain
- 1XK5 2.4 Å, Crystal structure of the m3G-cap-binding domain of snurportin1 in complex with a…
- 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)
- 2QNA 2.84 Å, Crystal structure of human Importin-beta (127-876) in complex with the IBB-domain of…
- 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
- 3NC0 2.9 Å, Crystal structure of the HIV-1 Rev NES-CRM1-RanGTP nuclear export complex (crystal II)
- 3LWW 3.15 Å, Structure of an open and closed conformation of Human Importin Beta bound to the…
- 2Q5D 3.2 Å, Crystal Structure of Human Importin Beta bound to the Snurportin1 IBB-domain second…
Browse structure collections
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