Crystal structure of Importin13 - RanGTP complex. Determined by X-ray diffraction at 2.8 Å resolution. Released 16 Feb 2010.
Explore 2X19 in 3D Show helices and sheets RCSB PDB PDBe
2X19 contains 71 α-helices and 10 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 |
|---|---|---|---|
| β-strand | 12-19 | 8 | 1 |
| α-helix | 25-34 | 10 | |
| α-helix | 36-38 | 3 | |
| β-strand | 47-55 | 9 | 1 |
| β-strand | 56 | 1 | 2 |
| β-strand | 60-68 | 9 | 1 |
| α-helix | 72-74 | 3 | |
| α-helix | 78-81 | 4 | |
| β-strand | 87-93 | 7 | 1 |
| α-helix | 97-101 | 5 | |
| α-helix | 103-113 | 11 | |
| β-strand | 119-124 | 6 | 1 |
| α-helix | 135-137 | 3 | |
| α-helix | 140-142 | 3 | |
| β-strand | 146-150 | 5 | 1 |
| β-strand | 152 | 1 | 3 |
| β-strand | 157 | 1 | 3 |
| α-helix | 161-170 | 10 | |
| β-strand | 178 | 1 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 23-35 | 13 | |
| α-helix | 39-54 | 16 | |
| α-helix | 58-65 | 8 | |
| α-helix | 72-88 | 17 | |
| α-helix | 90-92 | 3 | |
| α-helix | 95-97 | 3 | |
| α-helix | 98-111 | 14 | |
| α-helix | 117-134 | 18 | |
| α-helix | 142-150 | 9 | |
| α-helix | 160-177 | 18 | |
| α-helix | 195-197 | 3 | |
| α-helix | 198-209 | 12 | |
| α-helix | 216-230 | 15 | |
| α-helix | 236-238 | 3 | |
| α-helix | 240-249 | 10 | |
| α-helix | 256-267 | 12 | |
| α-helix | 272-274 | 3 | |
| α-helix | 276-287 | 12 | |
| α-helix | 290-298 | 9 | |
| α-helix | 302-325 | 24 | |
| α-helix | 327-329 | 3 | |
| α-helix | 330-344 | 15 | |
| α-helix | 355-360 | 6 | |
| α-helix | 361-371 | 11 | |
| α-helix | 376-401 | 26 | |
| α-helix | 406-410 | 5 | |
| α-helix | 414-438 | 25 | |
| α-helix | 440-451 | 12 | |
| α-helix | 452-456 | 5 | |
| α-helix | 463-476 | 14 | |
| α-helix | 487-494 | 8 | |
| α-helix | 495-497 | 3 | |
| α-helix | 503-515 | 13 | |
| α-helix | 517-522 | 6 | |
| α-helix | 524-527 | 4 | |
| α-helix | 531-537 | 7 | |
| α-helix | 541-543 | 3 | |
| α-helix | 544-557 | 14 | |
| α-helix | 559-561 | 3 | |
| α-helix | 566-578 | 13 | |
| α-helix | 584-598 | 15 | |
| α-helix | 603-625 | 23 | |
| α-helix | 631-650 | 20 | |
| α-helix | 676-695 | 20 | |
| α-helix | 699-715 | 17 | |
| α-helix | 721-723 | 3 | |
| α-helix | 724-737 | 14 | |
| α-helix | 741-754 | 14 | |
| α-helix | 762-781 | 20 | |
| α-helix | 787-803 | 17 | |
| α-helix | 805-809 | 5 | |
| α-helix | 815-825 | 11 | |
| α-helix | 831-844 | 14 | |
| α-helix | 845-847 | 3 | |
| α-helix | 853-857 | 5 | |
| α-helix | 862-871 | 10 | |
| α-helix | 872-876 | 5 | |
| α-helix | 879-881 | 3 | |
| α-helix | 882-895 | 14 | |
| α-helix | 897-907 | 11 | |
| α-helix | 920-930 | 11 | |
| α-helix | 937-952 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| GTP-binding nuclear protein GSP1/CNR1 | A | protein | 172 | SACCHAROMYCES CEREVISIAE | P32835 (AlphaFold model) |
| Importin-13 | B | protein | 963 | HOMO SAPIENS | O94829 (AlphaFold model) |
>2X19_1 GTP-BINDING NUCLEAR PROTEIN GSP1/CNR1 (chains A) GEVPTFKLVLVGDGGTGKTTFVKRHLTGEFEKKYIATIGVEVHPLSFYTNFGEIKFDVWD TAGLEKFGGLRDGYYINAQCAIIMFDVTSRITYKNVPNWHRDLVRVCENIPIVLCGNKVD VKERKVKAKTITFHRKKNLQYYDISAKSNYNFEKPFLWLARKLAGNPQLEFV
>2X19_2 IMPORTIN-13 (chains B) MERREEQPGAAGAGAAPALDFTVENVEKALHQLYYDPNIENKNLAQKWLMQAQVSPQAWH FSWQLLQPDKVPEIQYFGASALHIKISRYWSDIPTDQYESLKAQLFTQITRFASGSKIVL TRLCVALASLALSMMPDAWPCAVADMVRLFQAEDSPVDGQGRCLALLELLTVLPEEFQTS RLPQYRKGLVRTSLAVECGAVFPLLEQLLQQPSSPSCVRQKVLKCFSSWVQLEVPLQDCE ALIQAAFAALQDSELFDSSVEAIVNAISQPDAQRYVNTLLKLIPLVLGLQEQLRQAVQNG DMETSHGICRIAVALGENHSRALLDQVEHWQSFLALVNMIMFCTGIPGHYPVNETTSSLT LTFWYTLQDDILSFEAEKQAVYQQVYRPVYFQLVDVLLHKAQFPSDEEYGFWSSDEKEQF RIYRVDISDTLMYVYEMLGAELLSNLYDKLGRLLTSSEEPYSWQHTEALLYGFQSIAETI DVNYSDVVPGLIGLIPRISISNVQLADTVMFTIGALSEWLADHPVMINSVLPLVLHALGN PELSVSSVSTLKKICRECKYDLPPYAANIVAVSQDVLMKQIHKTSQCMWLMQALGFLLSA LQVEEILKNLHSLISPYIQQLEKLAEEIPNPSNKLAIVHILGLLSNLFTTLDISHHEDDH EGPELRKLPVPQGPNPVVVVLQQVFQLIQKVLSKWLNDAQVVEAVCAIFEKSVKTLLDDF APMVPQLCEMLGRMYSTIPQASALDLTRQLVHIFAHEPAHFPPIEALFLLVTSVTLTLFQ QGPRDHPDIVDSFMQLLAQALKRKPDLFLCERLDVKAVFQCAVLALKFPEAPTVKASCGF FTELLPRCGEVESVGKVVQEDGRMLLIAVLEAIGGQASRSLMDCFADILFALNKHCFSLL SMWIKEALQPPGFPSARLSPEQKDTFSQQILRERVNKRRVKEMVKEFTLLCRGLHGTDYT ADY
Nuclear Import Mechanism of the Ejc Component Mago- Y14 Revealed by Structural Studies of Importin 13. Bono, F., Cook, A.G., Grunwald, M. et al. Mol Cell (2010) 37:211. DOI 10.1016/J.MOLCEL.2010.01.007 · PubMed
Other PDB entries of the same protein (UniProt P32835 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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