eF-site ID 4hau-ABC PDB Code 4hau Chain A, B, C click to enlarge Title Crystal structure of CRM1 inhibitor Ratjadone A in complex with CRM1-Ran-RanBP1 Classification PROTEIN TRANSPORT/ANTIBIOTIC Compound GTP-binding nuclear protein Ran Source Homo sapiens (Human) (XPO1_YEAST) Sequence A:  VQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVH PLVFHTNRGPIKFNVWDTAGQEKFGGLRDGYYIQAQCAII MFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKVDIKD RKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKL IGDPNLEFVAMPALAPPEQYEHDLEVAQTTALPDEDDDL B:  EEDEEVLYKVRAKLFRFDKDAKEWKERGTGDCKFLKNKKT NKVRILMRRDKTLKICANHIIAPEYTLKPNVGSDRSWVYA CTADIAEGEAEAFTFAIRFGSKENADKFKEEFEKAQEINK K C:  GAMEGILDFSNDLDIALLDQVVSTFYQGSGVQQKQAQEIL TKFQDNPDAWQKADQILQFSTNPQSKFIALSILDKLITRK WKLLPNDHRIGIRNFVVGMIISMCQDDEVFKTQKNLINKS DLTLVQILKQEWPQNWPEFIPELIGSSSSSVNVCENNMIV LKLLSEEVFDFSAEQMTQAKALHLKNSMSKEFEQIFKLCF QVLEQGSSSLIVATLESLLRYLHWIPYRYIYETNILELLS TKFMTSPDTRAITLKCLTEVSNLKIPQDNDLIKRQTVLFF QNTLQQIATSVMPVTADLKATYANANGNDQSFLQDLAMFL TTYLARNRALLESDESLRELLLNAHQYLIQLSKIEERELF KTTLDYWHNLVADLFYEPLKKHIYEEICSQLRLVIIENMV RPEEVLVVENDEGEIVREFVKESDTIQLYKSEREVLVYLT HLNVIDTEEIMISKLARQIDGSEWSWHNINTLSWAIGSIS GTMSEDTEKRFVVTVIKDLLDLCVKKRGKDNKAVVASDIM YVVGQYPRFLKAHWNFLRTVILKLFEFMHETHEGVQDMAC DTFIKIVQKCKYHFVIQQPRESEPFIQTIIRDIQKTTADL QPQQVHTFYKACGIIISEERSVAERNRLLSDLMQLPNMAW DTIVEQSTANPLLLDSETVKIIANIIKTNVAVCTSMGADF YPQLGHIYYNMLQLYRAVSSMISAQVAAEGLIATKTPKVR GLRTIKKEILKLVETYISKARNLDDVVKVLVEPLLNAVLE DYMNNVPDARDAEVLNCMTTVVEKVGHMIPQGVILILQSV FECTLDMINKDFTEYPEHRVEFYKLLKVINEKSFAAFLEL PPAAFKLFVDAICWAFKHNNRDVEVNGLQIALDLVKNIER MGNVPFANEFHKNYFFIFVSETFFVLTDSDHKSGFSKQAL LLMKLISLVYDNKISVPLYQAEVPQGTSNQVYLSQYLANM LSNAFPHLTSEQIASFLSALTKQCKDLVVFKGTLRDFLVQ IKEVGGDPTDYLFA Description (1)  GTP-binding nuclear protein Ran, Ran-specific GTPase-activating protein 1, Exportin-1 Functional site 1) chain A residue 18 type sequence D description BINDING SITE FOR RESIDUE GNP A 301 source : AC1 2) chain A residue 19 type sequence G description BINDING SITE FOR RESIDUE GNP A 301 source : AC1 3) chain A residue 20 type sequence G description BINDING SITE FOR RESIDUE GNP A 301 source : AC1 4) chain A residue 21 type sequence T description BINDING SITE FOR RESIDUE GNP A 301 source : AC1 5) chain A residue 22 type sequence G description BINDING SITE FOR RESIDUE GNP A 301 source : AC1 6) chain A residue 23 type sequence K description BINDING SITE FOR RESIDUE GNP A 301 source : AC1 7) chain A residue 24 type sequence T description BINDING SITE FOR RESIDUE GNP A 301 source : AC1 8) chain A residue 25 type sequence T description BINDING SITE FOR RESIDUE GNP A 301 source : AC1 9) chain A residue 35 type sequence F description BINDING SITE FOR RESIDUE GNP A 301 source : AC1 10) chain A residue 36 type sequence E description BINDING SITE FOR RESIDUE GNP A 301 source : AC1 11) chain A residue 37 type sequence K description BINDING SITE FOR RESIDUE GNP A 301 source : AC1 12) chain A residue 38 type sequence K description BINDING SITE FOR RESIDUE GNP A 301 source : AC1 13) chain A residue 39 type sequence Y description BINDING SITE FOR RESIDUE GNP A 301 source : AC1 14) chain A residue 42 type sequence T description BINDING SITE FOR RESIDUE GNP A 301 source : AC1 15) chain A residue 68 type sequence G description BINDING SITE FOR RESIDUE GNP A 301 source : AC1 16) chain A residue 69 type sequence Q description BINDING SITE FOR RESIDUE GNP A 301 source : AC1 17) chain A residue 122 type sequence N description BINDING SITE FOR RESIDUE GNP A 301 source : AC1 18) chain A residue 123 type sequence K description BINDING SITE FOR RESIDUE GNP A 301 source : AC1 19) chain A residue 125 type sequence D description BINDING SITE FOR RESIDUE GNP A 301 source : AC1 20) chain A residue 126 type sequence I description BINDING SITE FOR RESIDUE GNP A 301 source : AC1 21) chain A residue 150 type sequence S description BINDING SITE FOR RESIDUE GNP A 301 source : AC1 22) chain A residue 151 type sequence A description BINDING SITE FOR RESIDUE GNP A 301 source : AC1 23) chain A residue 152 type sequence K description BINDING SITE FOR RESIDUE GNP A 301 source : AC1 24) chain A residue 24 type sequence T description BINDING SITE FOR RESIDUE MG A 302 source : AC2 25) chain A residue 42 type sequence T description BINDING SITE FOR RESIDUE MG A 302 source : AC2 26) chain A residue 196 type sequence Q description BINDING SITE FOR RESIDUE EDO A 303 source : AC3 27) chain A residue 197 type sequence Y description BINDING SITE FOR RESIDUE EDO A 303 source : AC3 28) chain A residue 103 type sequence N description BINDING SITE FOR RESIDUE EDO A 304 source : AC4 29) chain A residue 107 type sequence D description BINDING SITE FOR RESIDUE EDO A 304 source : AC4 30) chain C residue 532 type sequence I description BINDING SITE FOR RESIDUE RJA C 1101 source : AC5 31) chain C residue 533 type sequence K description BINDING SITE FOR RESIDUE RJA C 1101 source : AC5 32) chain C residue 536 type sequence L description BINDING SITE FOR RESIDUE RJA C 1101 source : AC5 33) chain C residue 539 type sequence C description BINDING SITE FOR RESIDUE RJA C 1101 source : AC5 34) chain C residue 552 type sequence A description BINDING SITE FOR RESIDUE RJA C 1101 source : AC5 35) chain C residue 555 type sequence I description BINDING SITE FOR RESIDUE RJA C 1101 source : AC5 36) chain C residue 569 type sequence H description BINDING SITE FOR RESIDUE RJA C 1101 source : AC5 37) chain C residue 572 type sequence F description BINDING SITE FOR RESIDUE RJA C 1101 source : AC5 38) chain C residue 575 type sequence T description BINDING SITE FOR RESIDUE RJA C 1101 source : AC5 39) chain C residue 579 type sequence K description BINDING SITE FOR RESIDUE RJA C 1101 source : AC5 40) chain C residue 583 type sequence F description BINDING SITE FOR RESIDUE RJA C 1101 source : AC5 41) chain C residue 191 type sequence E description BINDING SITE FOR RESIDUE GOL C 1102 source : AC6 42) chain C residue 227 type sequence R description BINDING SITE FOR RESIDUE GOL C 1102 source : AC6 43) chain C residue 231 type sequence E description BINDING SITE FOR RESIDUE GOL C 1102 source : AC6 44) chain A residue 105 type sequence H description BINDING SITE FOR RESIDUE GOL C 1103 source : AC7 45) chain A residue 109 type sequence V description BINDING SITE FOR RESIDUE GOL C 1103 source : AC7 46) chain A residue 110 type sequence R description BINDING SITE FOR RESIDUE GOL C 1103 source : AC7 47) chain A residue 142 type sequence K description BINDING SITE FOR RESIDUE GOL C 1103 source : AC7 48) chain C residue 164 type sequence E description BINDING SITE FOR RESIDUE GOL C 1103 source : AC7 49) chain C residue 219 type sequence R description BINDING SITE FOR RESIDUE GOL C 1103 source : AC7 50) chain C residue 842 type sequence L description BINDING SITE FOR RESIDUE GOL C 1104 source : AC8 51) chain C residue 846 type sequence N description BINDING SITE FOR RESIDUE GOL C 1104 source : AC8 52) chain C residue 891 type sequence W description BINDING SITE FOR RESIDUE GOL C 1104 source : AC8 53) chain C residue 327 type sequence R description BINDING SITE FOR RESIDUE EDO C 1105 source : AC9 54) chain C residue 328 type sequence A description BINDING SITE FOR RESIDUE EDO C 1105 source : AC9 55) chain C residue 331 type sequence E description BINDING SITE FOR RESIDUE EDO C 1105 source : AC9 56) chain C residue 372 type sequence D description BINDING SITE FOR RESIDUE EDO C 1105 source : AC9 57) chain C residue 416 type sequence K description BINDING SITE FOR RESIDUE EDO C 1105 source : AC9 58) chain C residue 967 type sequence Y description BINDING SITE FOR RESIDUE EDO C 1106 source : BC1 59) chain C residue 988 type sequence Q description BINDING SITE FOR RESIDUE EDO C 1106 source : BC1 60) chain C residue 992 type sequence S description BINDING SITE FOR RESIDUE EDO C 1106 source : BC1 61) chain C residue 1019 type sequence T description BINDING SITE FOR RESIDUE EDO C 1106 source : BC1 62) chain C residue 1007 type sequence T description BINDING SITE FOR RESIDUE CL C 1107 source : BC2 63) chain C residue 1008 type sequence S description BINDING SITE FOR RESIDUE CL C 1107 source : BC2 64) chain C residue 1009 type sequence E description BINDING SITE FOR RESIDUE CL C 1107 source : BC2 65) chain C residue 605 type sequence K description BINDING SITE FOR RESIDUE CL C 1108 source : BC3 66) chain C residue 606 type sequence C description BINDING SITE FOR RESIDUE CL C 1108 source : BC3 67) chain C residue 607 type sequence K description BINDING SITE FOR RESIDUE CL C 1108 source : BC3 68) chain C residue 608 type sequence Y description BINDING SITE FOR RESIDUE CL C 1108 source : BC3 69) chain C residue 61 type sequence P description BINDING SITE FOR RESIDUE CL C 1109 source : BC4 70) chain C residue 62 type sequence Q description BINDING SITE FOR RESIDUE CL C 1109 source : BC4 71) chain A residue 18 type BINDING sequence D description BINDING => ECO:0000269|PubMed:10078529, ECO:0000269|PubMed:10353245, ECO:0000269|PubMed:10367892, ECO:0000269|PubMed:11832950, ECO:0000269|PubMed:18611384, ECO:0000269|PubMed:19389996, ECO:0000269|PubMed:19505478, ECO:0000269|PubMed:24449914, ECO:0000269|PubMed:24915079, ECO:0000269|PubMed:26272610, ECO:0000269|PubMed:26349033, ECO:0000269|PubMed:28282025, ECO:0000269|PubMed:7885480, ECO:0007744|PDB:1IBR, ECO:0007744|PDB:1K5G, ECO:0007744|PDB:1RRP, ECO:0007744|PDB:3CH5, ECO:0007744|PDB:3GJ0, ECO:0007744|PDB:3GJ3, ECO:0007744|PDB:3GJ4, ECO:0007744|PDB:3GJ5, ECO:0007744|PDB:3GJ6, ECO:0007744|PDB:3GJ7, ECO:0007744|PDB:3GJ8, ECO:0007744|PDB:3GJX, ECO:0007744|PDB:3NBY, ECO:0007744|PDB:3NBZ, ECO:0007744|PDB:3NC0, ECO:0007744|PDB:3NC1, ECO:0007744|PDB:3ZJY, ECO:0007744|PDB:4C0Q, ECO:0007744|PDB:4OL0, ECO:0007744|PDB:5CIQ, ECO:0007744|PDB:5CIT, ECO:0007744|PDB:5CIW, ECO:0007744|PDB:5CLQ, ECO:0007744|PDB:5DH9, ECO:0007744|PDB:5DHA, ECO:0007744|PDB:5DHF, ECO:0007744|PDB:5DI9, ECO:0007744|PDB:5DIF, ECO:0007744|PDB:5DIS, ECO:0007744|PDB:5DLQ, ECO:0007744|PDB:5UWH, ECO:0007744|PDB:5UWI, ECO:0007744|PDB:5UWJ, ECO:0007744|PDB:5UWO, ECO:0007744|PDB:5UWP, ECO:0007744|PDB:5UWQ, ECO:0007744|PDB:5UWR, ECO:0007744|PDB:5UWS, ECO:0007744|PDB:5UWT, ECO:0007744|PDB:5UWU, ECO:0007744|PDB:5UWW source Swiss-Prot : SWS_FT_FI1 72) chain A residue 60 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI10 73) chain A residue 99 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI10 74) chain A residue 71 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI11 75) chain A residue 134 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:29040603 source Swiss-Prot : SWS_FT_FI12 76) chain A residue 159 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62827 source Swiss-Prot : SWS_FT_FI13 77) chain A residue 71 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate source Swiss-Prot : SWS_FT_FI14 78) chain A residue 152 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI15 79) chain A residue 36 type BINDING sequence E description BINDING => ECO:0000269|PubMed:10078529, ECO:0000269|PubMed:10353245, ECO:0000269|PubMed:10367892, ECO:0000269|PubMed:11832950, ECO:0000269|PubMed:19389996, ECO:0000269|PubMed:24449914, ECO:0000269|PubMed:24915079, ECO:0000269|PubMed:26272610, ECO:0000269|PubMed:26349033, ECO:0000269|PubMed:28282025, ECO:0000269|PubMed:7885480, ECO:0007744|PDB:1IBR, ECO:0007744|PDB:1K5D, ECO:0007744|PDB:1QBK, ECO:0007744|PDB:1RRP, ECO:0007744|PDB:3GJX, ECO:0007744|PDB:3NBY, ECO:0007744|PDB:3NBZ, ECO:0007744|PDB:3NC0, ECO:0007744|PDB:3NC1, ECO:0007744|PDB:3ZJY, ECO:0007744|PDB:4C0Q, ECO:0007744|PDB:4OL0, ECO:0007744|PDB:5CLL, ECO:0007744|PDB:5CLQ, ECO:0007744|PDB:5DH9, ECO:0007744|PDB:5DHA, ECO:0007744|PDB:5DHF, ECO:0007744|PDB:5DI9, ECO:0007744|PDB:5DIF, ECO:0007744|PDB:5DIS, ECO:0007744|PDB:5DLQ, ECO:0007744|PDB:5JLJ, ECO:0007744|PDB:5UWH, ECO:0007744|PDB:5UWI, ECO:0007744|PDB:5UWJ, ECO:0007744|PDB:5UWO, ECO:0007744|PDB:5UWP, ECO:0007744|PDB:5UWQ, ECO:0007744|PDB:5UWR, ECO:0007744|PDB:5UWS, ECO:0007744|PDB:5UWT, ECO:0007744|PDB:5UWU, ECO:0007744|PDB:5UWW source Swiss-Prot : SWS_FT_FI2 80) chain A residue 68 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10078529, ECO:0000269|PubMed:10353245, ECO:0000269|PubMed:10367892, ECO:0000269|PubMed:11832950, ECO:0000269|PubMed:18611384, ECO:0000269|PubMed:19389996, ECO:0000269|PubMed:19505478, ECO:0000269|PubMed:24449914, ECO:0000269|PubMed:24915079, ECO:0000269|PubMed:26272610, ECO:0000269|PubMed:26349033, ECO:0000269|PubMed:28282025, ECO:0000269|PubMed:7885480, ECO:0007744|PDB:1IBR, ECO:0007744|PDB:1K5D, ECO:0007744|PDB:1QBK, ECO:0007744|PDB:1RRP, ECO:0007744|PDB:3GJX, ECO:0007744|PDB:3NBY, ECO:0007744|PDB:3NBZ, ECO:0007744|PDB:3NC0, ECO:0007744|PDB:3NC1, ECO:0007744|PDB:3ZJY, ECO:0007744|PDB:4C0Q, ECO:0007744|PDB:4OL0, ECO:0007744|PDB:5DH9, ECO:0007744|PDB:5DHA, ECO:0007744|PDB:5DHF, ECO:0007744|PDB:5DI9, ECO:0007744|PDB:5DIF, ECO:0007744|PDB:5DIS, ECO:0007744|PDB:5DLQ, ECO:0007744|PDB:5JLJ, ECO:0007744|PDB:5UWH, ECO:0007744|PDB:5UWI, ECO:0007744|PDB:5UWJ, ECO:0007744|PDB:5UWO, ECO:0007744|PDB:5UWP, ECO:0007744|PDB:5UWQ, ECO:0007744|PDB:5UWR, ECO:0007744|PDB:5UWS, ECO:0007744|PDB:5UWT, ECO:0007744|PDB:5UWU, ECO:0007744|PDB:5UWW source Swiss-Prot : SWS_FT_FI3 81) chain A residue 122 type BINDING sequence N description BINDING => ECO:0000269|PubMed:10078529, ECO:0000269|PubMed:10353245, ECO:0000269|PubMed:10367892, ECO:0000269|PubMed:11832950, ECO:0000269|PubMed:18611384, ECO:0000269|PubMed:19389996, ECO:0000269|PubMed:19505478, ECO:0000269|PubMed:24449914, ECO:0000269|PubMed:24915079, ECO:0000269|PubMed:26272610, ECO:0000269|PubMed:26349033, ECO:0000269|PubMed:28282025, ECO:0000269|PubMed:7885480, ECO:0007744|PDB:1IBR, ECO:0007744|PDB:1K5D, ECO:0007744|PDB:1QBK, ECO:0007744|PDB:1RRP, ECO:0007744|PDB:3CH5, ECO:0007744|PDB:3GJ0, ECO:0007744|PDB:3GJ3, ECO:0007744|PDB:3GJ4, ECO:0007744|PDB:3GJ5, ECO:0007744|PDB:3GJ6, ECO:0007744|PDB:3GJ7, ECO:0007744|PDB:3GJ8, ECO:0007744|PDB:3GJX, ECO:0007744|PDB:3NBY, ECO:0007744|PDB:3NBZ, ECO:0007744|PDB:3NC0, ECO:0007744|PDB:3NC1, ECO:0007744|PDB:3ZJY, ECO:0007744|PDB:4C0Q, ECO:0007744|PDB:4OL0, ECO:0007744|PDB:5CIQ, ECO:0007744|PDB:5CIT, ECO:0007744|PDB:5CIW, ECO:0007744|PDB:5CJ2, ECO:0007744|PDB:5CLL, ECO:0007744|PDB:5DH9, ECO:0007744|PDB:5DHA, ECO:0007744|PDB:5DHF, ECO:0007744|PDB:5DI9, ECO:0007744|PDB:5DIF, ECO:0007744|PDB:5DIS, ECO:0007744|PDB:5DLQ, ECO:0007744|PDB:5JLJ, ECO:0007744|PDB:5UWH, ECO:0007744|PDB:5UWI, ECO:0007744|PDB:5UWJ, ECO:0007744|PDB:5UWO, ECO:0007744|PDB:5UWP, ECO:0007744|PDB:5UWQ, ECO:0007744|PDB:5UWR, ECO:0007744|PDB:5UWS, ECO:0007744|PDB:5UWT, ECO:0007744|PDB:5UWU, ECO:0007744|PDB:5UWW source Swiss-Prot : SWS_FT_FI4 82) chain A residue 150 type BINDING sequence S description BINDING => ECO:0000269|PubMed:10078529, ECO:0000269|PubMed:10353245, ECO:0000269|PubMed:10367892, ECO:0000269|PubMed:11832950, ECO:0000269|PubMed:18611384, ECO:0000269|PubMed:19389996, ECO:0000269|PubMed:19505478, ECO:0000269|PubMed:24449914, ECO:0000269|PubMed:24915079, ECO:0000269|PubMed:26272610, ECO:0000269|PubMed:26349033, ECO:0000269|PubMed:28282025, ECO:0000269|PubMed:7885480, ECO:0007744|PDB:1K5G, ECO:0007744|PDB:3CH5, ECO:0007744|PDB:3GJ0, ECO:0007744|PDB:3GJ3, ECO:0007744|PDB:3GJ4, ECO:0007744|PDB:3GJ5, ECO:0007744|PDB:3GJ6, ECO:0007744|PDB:3GJ7, ECO:0007744|PDB:3GJ8, ECO:0007744|PDB:3GJX, ECO:0007744|PDB:3NBY, ECO:0007744|PDB:3NBZ, ECO:0007744|PDB:3NC0, ECO:0007744|PDB:3NC1, ECO:0007744|PDB:3ZJY, ECO:0007744|PDB:4C0Q, ECO:0007744|PDB:4OL0, ECO:0007744|PDB:5CIQ, ECO:0007744|PDB:5CIT, ECO:0007744|PDB:5CIW, ECO:0007744|PDB:5CJ2, ECO:0007744|PDB:5CLL, ECO:0007744|PDB:5CLQ, ECO:0007744|PDB:5DH9, ECO:0007744|PDB:5DHA, ECO:0007744|PDB:5DHF, ECO:0007744|PDB:5DI9, ECO:0007744|PDB:5DIF, ECO:0007744|PDB:5DIS, ECO:0007744|PDB:5DLQ, ECO:0007744|PDB:5JLJ, ECO:0007744|PDB:5UWH, ECO:0007744|PDB:5UWI, ECO:0007744|PDB:5UWJ, ECO:0007744|PDB:5UWO, ECO:0007744|PDB:5UWP, ECO:0007744|PDB:5UWQ, ECO:0007744|PDB:5UWR, ECO:0007744|PDB:5UWS, ECO:0007744|PDB:5UWT, ECO:0007744|PDB:5UWU, ECO:0007744|PDB:5UWW source Swiss-Prot : SWS_FT_FI5 83) chain A residue 69 type SITE sequence Q description Essential for GTP hydrolysis => ECO:0000269|PubMed:18591255, ECO:0000269|PubMed:26272610, ECO:0000269|PubMed:8636225 source Swiss-Prot : SWS_FT_FI6 84) chain A residue 24 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI8 85) chain A residue 37 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:31075303 source Swiss-Prot : SWS_FT_FI9

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