Crystal structure of Exportin-5:RanGTP:pre-miRNA complex. Determined by X-ray diffraction at 2.92 Å resolution. Released 8 Dec 2009.
Explore 3A6P in 3D Show helices and sheets RCSB PDB PDBe
3A6P contains 155 α-helices and 20 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-21 | 16 | |
| α-helix | 27-43 | 17 | |
| α-helix | 47-54 | 8 | |
| α-helix | 61-77 | 17 | |
| α-helix | 79-81 | 3 | |
| α-helix | 84-100 | 17 | |
| α-helix | 110-127 | 18 | |
| α-helix | 135-144 | 10 | |
| α-helix | 147-161 | 15 | |
| α-helix | 162-166 | 5 | |
| α-helix | 172-184 | 13 | |
| α-helix | 186-207 | 22 | |
| α-helix | 214-232 | 19 | |
| α-helix | 240-244 | 5 | |
| α-helix | 249-256 | 8 | |
| α-helix | 257-259 | 3 | |
| α-helix | 264-275 | 12 | |
| α-helix | 281-284 | 4 | |
| α-helix | 285-291 | 7 | |
| α-helix | 293-304 | 12 | |
| α-helix | 313-338 | 26 | |
| α-helix | 349-360 | 12 | |
| α-helix | 365-379 | 15 | |
| α-helix | 388-405 | 18 | |
| α-helix | 418-425 | 8 | |
| α-helix | 429-453 | 25 | |
| α-helix | 455-470 | 16 | |
| α-helix | 498-520 | 23 | |
| α-helix | 528-540 | 13 | |
| α-helix | 546-559 | 14 | |
| α-helix | 560-564 | 5 | |
| α-helix | 567-569 | 3 | |
| α-helix | 570-582 | 13 | |
| α-helix | 595-614 | 20 | |
| α-helix | 616-619 | 4 | |
| α-helix | 620-622 | 3 | |
| α-helix | 623-635 | 13 | |
| α-helix | 642-656 | 15 | |
| α-helix | 657-659 | 3 | |
| α-helix | 662-680 | 19 | |
| α-helix | 683-690 | 8 | |
| α-helix | 692-699 | 8 | |
| α-helix | 713-734 | 22 | |
| α-helix | 741-746 | 6 | |
| β-strand | 750-753 | 4 | 1 |
| β-strand | 759-761 | 3 | 1 |
| α-helix | 766-785 | 20 | |
| α-helix | 789-792 | 4 | |
| α-helix | 797-799 | 3 | |
| α-helix | 805-806 | 2 | |
| α-helix | 807-813 | 7 | |
| α-helix | 832-858 | 27 | |
| α-helix | 868-875 | 8 | |
| α-helix | 885-891 | 7 | |
| α-helix | 892-896 | 5 | |
| α-helix | 897-901 | 5 | |
| α-helix | 905-907 | 3 | |
| α-helix | 908-912 | 5 | |
| α-helix | 913-935 | 23 | |
| α-helix | 953-977 | 25 | |
| β-strand | 978 | 1 | 2 |
| β-strand | 1011 | 1 | 2 |
| α-helix | 1013-1019 | 7 | |
| α-helix | 1022-1035 | 14 | |
| α-helix | 1041-1047 | 7 | |
| α-helix | 1048-1052 | 5 | |
| α-helix | 1053-1056 | 4 | |
| α-helix | 1066-1082 | 17 | |
| α-helix | 1087-1103 | 17 | |
| α-helix | 1111-1115 | 5 | |
| α-helix | 1123-1132 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1307-1315 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 11-17 | 7 | 3 |
| α-helix | 23-31 | 9 | |
| α-helix | 40-42 | 3 | |
| β-strand | 45-54 | 10 | 3 |
| β-strand | 57-66 | 10 | 3 |
| α-helix | 70-72 | 3 | |
| α-helix | 76-80 | 5 | |
| β-strand | 85-91 | 7 | 3 |
| α-helix | 95-99 | 5 | |
| α-helix | 101-111 | 11 | |
| β-strand | 117-122 | 6 | 3 |
| α-helix | 138-141 | 4 | |
| β-strand | 145-148 | 4 | 3 |
| α-helix | 159-168 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-21 | 16 | |
| α-helix | 27-42 | 16 | |
| α-helix | 47-54 | 8 | |
| α-helix | 61-73 | 13 | |
| α-helix | 74-78 | 5 | |
| α-helix | 84-96 | 13 | |
| α-helix | 97-101 | 5 | |
| α-helix | 110-127 | 18 | |
| α-helix | 135-144 | 10 | |
| α-helix | 147-161 | 15 | |
| α-helix | 162-166 | 5 | |
| α-helix | 172-184 | 13 | |
| α-helix | 186-207 | 22 | |
| α-helix | 214-232 | 19 | |
| α-helix | 240-242 | 3 | |
| α-helix | 249-256 | 8 | |
| α-helix | 257-259 | 3 | |
| α-helix | 264-275 | 12 | |
| α-helix | 281-283 | 3 | |
| α-helix | 285-291 | 7 | |
| α-helix | 293-304 | 12 | |
| α-helix | 313-337 | 25 | |
| α-helix | 344-346 | 3 | |
| α-helix | 349-360 | 12 | |
| α-helix | 365-379 | 15 | |
| α-helix | 388-391 | 4 | |
| α-helix | 394-405 | 12 | |
| α-helix | 418-425 | 8 | |
| α-helix | 429-453 | 25 | |
| α-helix | 455-469 | 15 | |
| α-helix | 498-520 | 23 | |
| α-helix | 528-539 | 12 | |
| α-helix | 546-559 | 14 | |
| α-helix | 560-564 | 5 | |
| α-helix | 567-569 | 3 | |
| α-helix | 570-582 | 13 | |
| α-helix | 595-614 | 20 | |
| α-helix | 616-619 | 4 | |
| α-helix | 623-635 | 13 | |
| α-helix | 642-656 | 15 | |
| α-helix | 657-659 | 3 | |
| α-helix | 662-672 | 11 | |
| α-helix | 674-680 | 7 | |
| α-helix | 683-690 | 8 | |
| α-helix | 692-699 | 8 | |
| α-helix | 713-734 | 22 | |
| α-helix | 741-747 | 7 | |
| β-strand | 750-753 | 4 | 4 |
| β-strand | 759-761 | 3 | 4 |
| α-helix | 766-785 | 20 | |
| α-helix | 791-793 | 3 | |
| α-helix | 797-799 | 3 | |
| α-helix | 807-814 | 8 | |
| α-helix | 829-831 | 3 | |
| α-helix | 832-858 | 27 | |
| α-helix | 860-863 | 4 | |
| α-helix | 868-873 | 6 | |
| α-helix | 880-882 | 3 | |
| α-helix | 885-891 | 7 | |
| α-helix | 892-896 | 5 | |
| α-helix | 897-901 | 5 | |
| α-helix | 905-907 | 3 | |
| α-helix | 908-912 | 5 | |
| α-helix | 913-935 | 23 | |
| α-helix | 953-977 | 25 | |
| β-strand | 978 | 1 | 5 |
| β-strand | 1011 | 1 | 5 |
| α-helix | 1013-1019 | 7 | |
| α-helix | 1022-1037 | 16 | |
| α-helix | 1041-1047 | 7 | |
| α-helix | 1048-1052 | 5 | |
| α-helix | 1053-1056 | 4 | |
| α-helix | 1066-1082 | 17 | |
| α-helix | 1087-1103 | 17 | |
| α-helix | 1111-1115 | 5 | |
| α-helix | 1123-1133 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 11-17 | 7 | 6 |
| α-helix | 23-32 | 10 | |
| β-strand | 45-54 | 10 | 6 |
| β-strand | 57-66 | 10 | 6 |
| α-helix | 76-79 | 4 | |
| β-strand | 85-91 | 7 | 6 |
| α-helix | 95-99 | 5 | |
| α-helix | 101-111 | 11 | |
| β-strand | 117-122 | 6 | 6 |
| α-helix | 138-141 | 4 | |
| β-strand | 145-148 | 4 | 6 |
| α-helix | 159-169 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Exportin-5 | A, F | protein | 1204 | Homo sapiens | Q9HAV4 (AlphaFold model) |
| 13-mer peptide | B, G | protein | 13 | Homo sapiens | |
| GTP-binding nuclear protein Ran | C, H | protein | 216 | Canis lupus familiaris | P62825 (AlphaFold model) |
| pre-microRNA | D, I | RNA | 24 | ||
| pre-microRNA | E, J | RNA | 24 |
>3A6P_1 Exportin-5 (chains A, F) MAMDQVNALCEQLVKAVTVMMDPNSTQRYRLEALKFCEEFKEKCPICVPCGLRLAEKTQV AIVRHFGLQILEHVVKFRWNGMSRLEKVYLKNSVMELIANGTLNILEEENHIKDALSRIV VEMIKREWPQHWPDMLIELDTLSKQGETQTELVMFILLRLAEDVVTFQTLPPQRRRDIQQ TLTQNMERIFSFLLNTLQENVNKYQQVKTDTSQESKAQANCRVGVAALNTLAGYIDWVSM SHITAENCKLLEILCLLLNEQELQLGAAECLLIAVSRKGKLEDRKPLMVLFGDVAMHYIL SAAQTADGGGLVEKHYVFLKRLCQVLCALGNQLCALLGADSDVETPSNFGKYLESFLAFT THPSQFLRSSTQMTWGALFRHEILSRDPLLLAIIPKYLRASMTNLVKMGFPSKTDSPSCE YSRFDFDSDEDFNAFFNSSRAQQGEVMRLACRLDPKTSFQMAGEWLKYQLSTFLDAGSVN SCSAVGTGEGSLCSVFSPSFVQWEAMTLFLESVITQMFRTLNREEIPVNDGIELLQMVLN FDTKDPLILSCVLTNVSALFPFVTYRPEFLPQVFSKLFSSVTFETVEESKAPRTRAVRNV RRHACSSIIKMCRDYPQLVLPNFDMLYNHVKQLLSNELLLTQMEKCALMEALVLISNQFK NYERQKVFLEELMAPVASIWLSQDMHRVLSDVDAFIAYVGTDQKSCDPGLEDPCGLNRAR MSFCVYSILGVVKRTCWPTDLEEAKAGGFVVGYTSSGNPIFRNPCTEQILKLLDNLLALI RTHNTLYAPEMLAKMAEPFTKALDMLDAEKSAILGLPQPLLELNDSPVFKTVLERMQRFF STLYENCFHILGKAGPSMQQDFYTVEDLATQLLSSAFVNLNNIPDYRLRPMLRVFVKPLV LFCPPEHYEALVSPILGPLFTYLHMRLSQKWQVINQRSLLCGEDEAADENPESQEMLEEQ LVRMLTREVMDLITVCCVSKKGADHSSAPPADGDDEEMMATEVTPSAMAELTDLGKCLMK HEDVCTALLITAFNSLAWKDTLSCQRTTSQLCWPLLKQVLSGTLLADAVTWLFTSVLKGL QMHGQHDGCMASLVHLAFQIYEALRPRYLEIRAVMEQIPEIQKDSLDQFDCKLLNPSLQK VADKRRKDQFKRLIAGCIGKPLGEQFRKEVHIKNLPSLFKKTKPMLETEVLDNDGGGLAT IFEP
>3A6P_2 13-mer peptide (chains B, G) XXXXXXXXXXXXX
>3A6P_3 GTP-binding nuclear protein Ran (chains C, H) MAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIK FNVWDTAGQEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLC GNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVAMP ALAPPEVVMDPALAAQYEHDLEVAQTTALPDEDDDL
>3A6P_4 pre-microRNA (chains D, I) GGUAAACAUCCUCGACUGGAAGCU
>3A6P_5 pre-microRNA (chains E, J) GGCUUUCAGUCGGAUGUUUGCCGC
A high-resolution structure of the pre-microRNA nuclear export machinery. Okada, C., Yamashita, E., Lee, S.J. et al. Science (2009) 326:1275-1279. DOI 10.1126/science.1178705 · PubMed
Other PDB entries of the same protein (UniProt Q9HAV4 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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