eF-site ID 4nca-AB PDB Code 4nca Chain A, B click to enlarge Title Structure of Thermus thermophilus Argonaute bound to guide DNA 19-mer and target DNA in the presence of Mg2+ Classification NUCLEAR PROTEIN/DNA Compound Argonaute Source Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039) (4NCA) Sequence A:  HLGKTEVFLNRFALRPLNPEELRPWRLEVVLDPPPGREEV YPLLAQVARRAGGVTVRMGDGLASWSPPEVLVLEGTLARM GQTYAYRLYPKGRRPLDPKDPGERSVLSALARRLLQERLR RLEGVWVEGLAVYRREHARGPGWRVLGGAVLDLWVSDSGA FLLEVDPAYRILCEMSLEAWLAQGHPLPKRVRNAYDRRTW ELLRLGEEDPKELPLPGGLSLLDYHASKGRLQGREGGRVA WVADPKDPRKPIPHLTGLLVPVLTLEDLHEEEGSLALSLP WEERRRRTREIASWIGRRLGLGTPEAVRAQAYRLSIPKLM GRRAVSKPADALRVGFYRAQETALALLRLDGAQGWPEFLR RALLRAFGASGASLRLHTLHAHPSQGLAFREALRKAKEEG VQAVLVLTPPMAWEDRNRLKALLLREGLPSQILNVPLREE ERHRWENALLGLLAKAGLQVVALSGAYPAELAVGFDAGGR ESFRFGGAACAVGGDGGHLLWTLPEAQAGERIPQEVVWDL LEETLWAFRRKAGRLPSRVLLLRDGRVPQDEFALALEALA REGIAYDLVSVRKSGGGRVYPVQGRLADGLYVPLEDKTFL LLTVHRDFRGTPRPLKLVHEAGDTPLEALAHQIFHLTRLY PASGFAFPRLPAPLHLADRLVKEVGRLGIRHLKEVDREKL FFV B:  LGKTEVFLNRFALRPLNPEELRPWRLEVVLDPPPGREEVY PLLAQVARRAGGVTVRMGDGLASWSPPEVLVLEGTLARMG QTYAYRLYPKGRRPLDPKDPGERSVLSALARRLLQERLRR LEGVWVEGLAVYRREHARGPGWRVLGGAVLDLWVSDSGAF LLEVDPAYRILCEMSLEAWLAQGHPLPKRVRNAYDRRTWE LLRLGEEDPKELPLPGGLSLLDYHASKGRLQGREGGRVAW VADPKKPIPHLTGLLVPVLTLEDLHEEGSLALSLPWEERR RRTREIASWIGRRLGLGTPEAVRAQAYRLSIPKLMGRRAV SKPADALRVGFYRAQETALALLRLDGAQGWPEFLRRALLR AFGASGASLRLHTLHAHPSQGLAFREALRKAKEEGVQAVL VLTPPMAWEDRNRLKALLLREGLPSQILNVPLREEERHRW ENALLGLLAKAGLQVVALSGAYPAELAVGFDAGGRESFRF GGAACAVGGDGGHLLWTLPEAQAGERIPQEVVWDLLEETL WAFRRKAGRLPSRVLLLRDGRVPQDEFALALEALAREGIA YDLVSVRKSGGGRVYPVQGRLADGLYVPLEDKTFLLLTVH RDFRGTPRPLKLVHEAGDTPLEALAHQIFHLTRLYPASGF AFPRLPAPLHLADRLVKEVGRLGIRHLKEVDREKLFFV Description Functional site 1) chain A residue 195 type sequence N description BINDING SITE FOR RESIDUE DT A 701 source : AC1 2) chain A residue 197 type sequence Y description BINDING SITE FOR RESIDUE DT A 701 source : AC1 3) chain A residue 200 type sequence R description BINDING SITE FOR RESIDUE DT A 701 source : AC1 4) chain A residue 217 type sequence L description BINDING SITE FOR RESIDUE DT A 701 source : AC1 5) chain A residue 218 type sequence P description BINDING SITE FOR RESIDUE DT A 701 source : AC1 6) chain A residue 223 type sequence L description BINDING SITE FOR RESIDUE DT A 701 source : AC1 7) chain A residue 226 type sequence Y description BINDING SITE FOR RESIDUE DT A 701 source : AC1 8) chain A residue 227 type sequence H description BINDING SITE FOR RESIDUE DT A 701 source : AC1 9) chain A residue 232 type sequence R description BINDING SITE FOR RESIDUE DT A 701 source : AC1 10) chain A residue 254 type sequence I description BINDING SITE FOR RESIDUE DT A 701 source : AC1 11) chain A residue 255 type sequence P description BINDING SITE FOR RESIDUE DT A 701 source : AC1 12) chain A residue 256 type sequence H description BINDING SITE FOR RESIDUE DT A 701 source : AC1 13) chain B residue 37 type sequence P description BINDING SITE FOR RESIDUE DT A 701 source : AC1 14) chain B residue 38 type sequence G description BINDING SITE FOR RESIDUE DT A 701 source : AC1 15) chain B residue 39 type sequence R description BINDING SITE FOR RESIDUE DT A 701 source : AC1 16) chain A residue 478 type sequence D description BINDING SITE FOR RESIDUE MG A 702 source : AC2 17) chain A residue 479 type sequence A description BINDING SITE FOR RESIDUE MG A 702 source : AC2 18) chain A residue 546 type sequence D description BINDING SITE FOR RESIDUE MG A 702 source : AC2 19) chain A residue 37 type sequence P description BINDING SITE FOR RESIDUE DT B 701 source : AC3 20) chain A residue 38 type sequence G description BINDING SITE FOR RESIDUE DT B 701 source : AC3 21) chain A residue 39 type sequence R description BINDING SITE FOR RESIDUE DT B 701 source : AC3 22) chain B residue 195 type sequence N description BINDING SITE FOR RESIDUE DT B 701 source : AC3 23) chain B residue 197 type sequence Y description BINDING SITE FOR RESIDUE DT B 701 source : AC3 24) chain B residue 200 type sequence R description BINDING SITE FOR RESIDUE DT B 701 source : AC3 25) chain B residue 217 type sequence L description BINDING SITE FOR RESIDUE DT B 701 source : AC3 26) chain B residue 218 type sequence P description BINDING SITE FOR RESIDUE DT B 701 source : AC3 27) chain B residue 223 type sequence L description BINDING SITE FOR RESIDUE DT B 701 source : AC3 28) chain B residue 226 type sequence Y description BINDING SITE FOR RESIDUE DT B 701 source : AC3 29) chain B residue 227 type sequence H description BINDING SITE FOR RESIDUE DT B 701 source : AC3 30) chain B residue 232 type sequence R description BINDING SITE FOR RESIDUE DT B 701 source : AC3 31) chain B residue 254 type sequence I description BINDING SITE FOR RESIDUE DT B 701 source : AC3 32) chain B residue 255 type sequence P description BINDING SITE FOR RESIDUE DT B 701 source : AC3 33) chain B residue 256 type sequence H description BINDING SITE FOR RESIDUE DT B 701 source : AC3 34) chain B residue 478 type sequence D description BINDING SITE FOR RESIDUE MG B 702 source : AC4 35) chain B residue 660 type sequence D description BINDING SITE FOR RESIDUE MG B 702 source : AC4 36) chain B residue 478 type sequence D description BINDING SITE FOR RESIDUE MG B 703 source : AC5 37) chain B residue 479 type sequence A description BINDING SITE FOR RESIDUE MG B 703 source : AC5 38) chain B residue 546 type sequence D description BINDING SITE FOR RESIDUE MG B 703 source : AC5 39) chain A residue 685 type sequence V description BINDING SITE FOR RESIDUE MG C 101 source : AC6 40) chain A residue 478 type sequence D description BINDING SITE FOR RESIDUE MG D 101 source : AC7 41) chain A residue 660 type sequence D description BINDING SITE FOR RESIDUE MG D 101 source : AC7 42) chain B residue 685 type sequence V description BINDING SITE FOR RESIDUE MG E 101 source : AC8 43) chain A residue 478 type ACT_SITE sequence D description ACT_SITE => ECO:0000305|PubMed:18754009, ECO:0000305|PubMed:19092929, ECO:0000305|PubMed:24374628, ECO:0000305|PubMed:28911094 source Swiss-Prot : SWS_FT_FI1 44) chain A residue 546 type ACT_SITE sequence D description ACT_SITE => ECO:0000305|PubMed:18754009, ECO:0000305|PubMed:19092929, ECO:0000305|PubMed:24374628, ECO:0000305|PubMed:28911094 source Swiss-Prot : SWS_FT_FI1 45) chain A residue 660 type ACT_SITE sequence D description ACT_SITE => ECO:0000305|PubMed:18754009, ECO:0000305|PubMed:19092929, ECO:0000305|PubMed:24374628, ECO:0000305|PubMed:28911094 source Swiss-Prot : SWS_FT_FI1 46) chain B residue 478 type ACT_SITE sequence D description ACT_SITE => ECO:0000305|PubMed:18754009, ECO:0000305|PubMed:19092929, ECO:0000305|PubMed:24374628, ECO:0000305|PubMed:28911094 source Swiss-Prot : SWS_FT_FI1 47) chain B residue 546 type ACT_SITE sequence D description ACT_SITE => ECO:0000305|PubMed:18754009, ECO:0000305|PubMed:19092929, ECO:0000305|PubMed:24374628, ECO:0000305|PubMed:28911094 source Swiss-Prot : SWS_FT_FI1 48) chain B residue 660 type ACT_SITE sequence D description ACT_SITE => ECO:0000305|PubMed:18754009, ECO:0000305|PubMed:19092929, ECO:0000305|PubMed:24374628, ECO:0000305|PubMed:28911094 source Swiss-Prot : SWS_FT_FI1 49) chain A residue 512 type ACT_SITE sequence E description ACT_SITE => ECO:0000305|PubMed:24374628, ECO:0000305|PubMed:28911094 source Swiss-Prot : SWS_FT_FI2 50) chain B residue 512 type ACT_SITE sequence E description ACT_SITE => ECO:0000305|PubMed:24374628, ECO:0000305|PubMed:28911094 source Swiss-Prot : SWS_FT_FI2 51) chain A residue 478 type BINDING sequence D description BINDING => ECO:0000269|PubMed:24374628, ECO:0000305|PubMed:19812667, ECO:0000305|PubMed:28911094, ECO:0007744|PDB:4KPY, ECO:0007744|PDB:4N76 source Swiss-Prot : SWS_FT_FI3 52) chain B residue 478 type BINDING sequence D description BINDING => ECO:0000269|PubMed:24374628, ECO:0000305|PubMed:19812667, ECO:0000305|PubMed:28911094, ECO:0007744|PDB:4KPY, ECO:0007744|PDB:4N76 source Swiss-Prot : SWS_FT_FI3 53) chain A residue 546 type BINDING sequence D description BINDING => ECO:0000269|PubMed:24374628, ECO:0000305|PubMed:19092929, ECO:0000305|PubMed:19812667, ECO:0000305|PubMed:28911094, ECO:0007744|PDB:4KPY, ECO:0007744|PDB:4N76 source Swiss-Prot : SWS_FT_FI4 54) chain A residue 660 type BINDING sequence D description BINDING => ECO:0000269|PubMed:24374628, ECO:0000305|PubMed:19092929, ECO:0000305|PubMed:19812667, ECO:0000305|PubMed:28911094, ECO:0007744|PDB:4KPY, ECO:0007744|PDB:4N76 source Swiss-Prot : SWS_FT_FI4 55) chain B residue 546 type BINDING sequence D description BINDING => ECO:0000269|PubMed:24374628, ECO:0000305|PubMed:19092929, ECO:0000305|PubMed:19812667, ECO:0000305|PubMed:28911094, ECO:0007744|PDB:4KPY, ECO:0007744|PDB:4N76 source Swiss-Prot : SWS_FT_FI4 56) chain B residue 660 type BINDING sequence D description BINDING => ECO:0000269|PubMed:24374628, ECO:0000305|PubMed:19092929, ECO:0000305|PubMed:19812667, ECO:0000305|PubMed:28911094, ECO:0007744|PDB:4KPY, ECO:0007744|PDB:4N76 source Swiss-Prot : SWS_FT_FI4 57) chain A residue 685 type BINDING sequence V description BINDING => ECO:0000269|PubMed:24374628, ECO:0000305|PubMed:18754009, ECO:0000305|PubMed:19092929, ECO:0000305|PubMed:19812667, ECO:0000305|PubMed:28911094, ECO:0007744|PDB:4KPY, ECO:0007744|PDB:4N76 source Swiss-Prot : SWS_FT_FI5 58) chain B residue 685 type BINDING sequence V description BINDING => ECO:0000269|PubMed:24374628, ECO:0000305|PubMed:18754009, ECO:0000305|PubMed:19092929, ECO:0000305|PubMed:19812667, ECO:0000305|PubMed:28911094, ECO:0007744|PDB:4KPY, ECO:0007744|PDB:4N76 source Swiss-Prot : SWS_FT_FI5

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