Cryo-EM structure of Importin-4 bound to RanGTP. Determined by electron microscopy at 7.1 Å resolution. Released 21 Sept 2022.
Explore 8DYO in 3D Show helices and sheets RCSB PDB PDBe
8DYO contains 72 α-helices and 11 β-strands across 2 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 | 6-14 | 9 | |
| α-helix | 20-25 | 6 | |
| α-helix | 27-30 | 4 | |
| α-helix | 45-47 | 3 | |
| α-helix | 51-68 | 18 | |
| α-helix | 78-89 | 12 | |
| α-helix | 94-107 | 14 | |
| α-helix | 117-128 | 12 | |
| α-helix | 132-148 | 17 | |
| α-helix | 154-167 | 14 | |
| α-helix | 174-187 | 14 | |
| α-helix | 188-190 | 3 | |
| α-helix | 202-213 | 12 | |
| α-helix | 218-231 | 14 | |
| α-helix | 244-254 | 11 | |
| α-helix | 262-277 | 16 | |
| α-helix | 281-284 | 4 | |
| α-helix | 288-299 | 12 | |
| α-helix | 307-309 | 3 | |
| α-helix | 329-343 | 15 | |
| α-helix | 349-360 | 12 | |
| α-helix | 366-379 | 14 | |
| α-helix | 385-389 | 5 | |
| α-helix | 398-401 | 4 | |
| α-helix | 409-422 | 14 | |
| α-helix | 427-429 | 3 | |
| α-helix | 436-445 | 10 | |
| α-helix | 452-461 | 10 | |
| α-helix | 466-468 | 3 | |
| α-helix | 471-476 | 6 | |
| α-helix | 477-484 | 8 | |
| α-helix | 494-511 | 18 | |
| α-helix | 519-530 | 12 | |
| α-helix | 538-554 | 17 | |
| α-helix | 557-559 | 3 | |
| α-helix | 560-563 | 4 | |
| α-helix | 569-572 | 4 | |
| α-helix | 586-597 | 12 | |
| α-helix | 606-616 | 11 | |
| α-helix | 671-682 | 12 | |
| α-helix | 692-704 | 13 | |
| α-helix | 711-721 | 11 | |
| α-helix | 724-733 | 10 | |
| α-helix | 738-756 | 19 | |
| α-helix | 766-780 | 15 | |
| α-helix | 784-787 | 4 | |
| α-helix | 795-803 | 9 | |
| α-helix | 828-834 | 7 | |
| α-helix | 835-837 | 3 | |
| α-helix | 843-845 | 3 | |
| α-helix | 852-854 | 3 | |
| α-helix | 855-866 | 12 | |
| α-helix | 872-888 | 17 | |
| α-helix | 891-907 | 17 | |
| α-helix | 917-927 | 11 | |
| α-helix | 932-936 | 5 | |
| α-helix | 938-941 | 4 | |
| α-helix | 946-951 | 6 | |
| α-helix | 955-970 | 16 | |
| α-helix | 981-987 | 7 | |
| α-helix | 998-1004 | 7 | |
| α-helix | 1020-1030 | 11 | |
| α-helix | 1038-1040 | 3 | |
| α-helix | 1046-1048 | 3 | |
| α-helix | 1060-1064 | 5 | |
| α-helix | 1070-1072 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 12-13 | 2 | 1 |
| β-strand | 16-18 | 3 | 2 |
| α-helix | 25-33 | 9 | |
| β-strand | 46 | 1 | 3 |
| β-strand | 52-56 | 5 | 1 |
| β-strand | 59-63 | 5 | 1 |
| β-strand | 69 | 1 | 3 |
| α-helix | 80-82 | 3 | |
| β-strand | 88-90 | 3 | 2 |
| β-strand | 93 | 1 | 4 |
| α-helix | 97-113 | 17 | |
| β-strand | 119-121 | 3 | 2 |
| β-strand | 124 | 1 | 4 |
| α-helix | 135-137 | 3 | |
| α-helix | 140-143 | 4 | |
| β-strand | 147-148 | 2 | 2 |
| α-helix | 161-171 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Importin-4 | A | protein | 1081 | Homo sapiens | Q8TEX9 (AlphaFold model) |
| GTP-binding nuclear protein GSP1/CNR1 | B | protein | 219 | Saccharomyces cerevisiae | P32835 (AlphaFold model) |
>8DYO_1 Importin-4 (chains A) MESAGLEQLLRELLLPDTERIRRATEQLQIVLRAPAALPALCDLLASAADPQIRQFAAVL TRRRLNTRWRRLAAEQRESLKSLILTALQRETEHCVSLSLAQLSATIFRKEGLEAWPQLL QLLQHSTHSPHSPEREMGLLLLSVVVTSRPEAFQPHHRELLRLLNETLGEVGSPGLLFYS LRTLTTMAPYLSTEDVPLARMLVPKLIMAMQTLIPIDEAKACEALEALDELLESEVPVIT PYLSEVLTFCLEVARNVALGNAIRIRILCCLTFLVKVKSKALLKNRLLPPLLHTLFPIVA AEPPPGQLDPEDQDSEEEELEIELMGETPKHFAVQVVDMLALHLPPEKLCPQLMPMLEEA LRSESPYQRKAGLLVLAVLSDGAGDHIRQRLLPPLLQIVCKGLEDPSQVVRNAALFALGQ FSENLQPHISSYSREVMPLLLAYLKSVPLGHTHHLAKACYALENFVENLGPKVQPYLPEL MECMLQLLRNPSSPRAKELAVSALGAIATAAQASLLPYFPAIMEHLREFLLTGREDLQPV QIQSLETLGVLARAVGEPMRPLAEECCQLGLGLCDQVDDPDLRRCTYSLFAALSGLMGEG LAPHLEQITTLMLLSLRSTEGIVPQYDGSSSFLLFDDESDGEEEEELMDEDVEEEDDSEI SGYSVENAFFDEKEDTCAAVGEISVNTSVAFLPYMESVFEEVFKLLECPHLNVRKAAHEA LGQFCCALHKACQSCPSEPNTAALQAALARVVPSYMQAVNRERERQVVMAVLEALTGVLR SCGTLTLKPPGRLAELCGVLKAVLQRKTACQDTDEEEEEEDDDQAEYDAMLLEHAGEAIP ALAAAAGGDSFAPFFAGFLPLLVCKTKQGCTVAEKSFAVGTLAETIQGLGAASAQFVSRL LPVLLSTAQEADPEVRSNAIFGMGVLAEHGGHPAQEHFPKLLGLLFPLLARERHDRVRDN ICGALARLLMASPTRKPEPQVLAALLHALPLKEDLEEWVTIGRLFSFLYQSSPDQVIDVA PELLRICSLILADNKIPPDTKAALLLLLTFLAKQHTDSFQAALGSLPVDKAQELQAVLGL S
>8DYO_2 GTP-binding nuclear protein GSP1/CNR1 (chains B) MSAPAANGEVPTFKLVLVGDGGTGKTTFVKRHLTGEFEKKYIATIGVEVHPLSFYTNFGE IKFDVWDTAGLEKFGGLRDGYYINAQCAIIMFDVTSRITYKNVPNWHRDLVRVCENIPIV LCGNKVDVKERKVKAKTITFHRKKNLQYYDISAKSNYNFEKPFLWLARKLAGNPQLEFVA SPALAPPEVQVDEQLMQQYQQEMEQATALPLPDEDDADL
Structure of IMPORTIN-4 bound to the H3-H4-ASF1 histone-histone chaperone complex. Bernardes, N.E., Fung, H.Y.J., Li, Y. et al. Proc Natl Acad Sci U S A (2022) 119:e2207177119-e2207177119. DOI 10.1073/pnas.2207177119 · PubMed
Other PDB entries of the same protein (UniProt Q8TEX9 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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