eF-site ID 2be5-ABCDEF PDB Code 2be5 Chain A, B, C, D, E, F click to enlarge Title Crystal structure of the T. Thermophilus RNA polymerase holoenzyme in complex with inhibitor tagetitoxin Classification TRANSFERASE Compound DNA-directed RNA polymerase alpha chain Source ORGANISM_SCIENTIFIC: Thermus thermophilus; Sequence A:  MLDSKLKAPVFTVRTQGREYGEFVLEPLERGFGVTLGNPL RRILLSSIPGTAVTSVYIEDVLHEFSTIPGVKEDVVEIIL NLKELVVRFLNPSLQTVTLLLKAEGPKEVKARDFLPVADV EIMNPDLHIATLEEGGRLNMEVRVDRGVGYVPAEKHGIKD RINAIPVDAVFSPVRRVAFQVEDTRLGQRTDLDKLTLRIW TDGSVTPLEALNQAVEILREHLTYFSNPQ B:  MLDSKLKAPVFTVRTQGREYGEFVLEPLERGFGVTLGNPL RRILLSSIPGTAVTSVYIEDVLHEFSTIPGVKEDVVEIIL NLKELVVRFLNPSLQTVTLLLKAEGPKEVKARDFLPVADV EIMNPDLHIATLEEGGRLNMEVRVDRGVGYVPAEKHGIKD RINAIPVDAVFSPVRRVAFQVEDTRLGQRTDLDKLTLRIW TDGSVTPLEALNQAVEILREHLTYFSNPQ C:  MEIKRFGRIREVIPLPPLTEIQVESYRRALQADVPPEKRE NVGIQAAFRETFPIEEEDKGKGGLVLDFLEYRLGEPPFPQ DECREKDLTYQAPLYARLQLIHKDTGLIKEDEVFLGHIPL MTEDGSFIINGADRVIVSQIHRSPGVYFTPDPARPGRYIA SIIPLPKRGPWIDLEVEPNGVVSMKVNKRKFPLVLLLRVL GYDQETLARELGAYGELVQGLMDESVFAMRPEEALIRLFT LLRPGDPPKRDKAVAYVYGLIADPRRYDLGEAGRYKAEEK LGIRLSGRTLARFEDGEFKDEVFLPTLRYLFALTAGVPGH EVDDIDHLGNRRIRTVGELMTDQFRVGLARLARGVRERML MGSEDSLTPAKLVNSRPLEAAIREFFSRSQLSQFKDETNP LSSLRHKRRISALGPGGLTRERAGFDVRDVHRTHYGRICP VETPEGANIGLITSLAAYARVDELGFIRTPYRRVVGGVVT DEVVYMTATEEDRYTIAQANTPLEGNRIAAERVVARRKGE PVIVSPEEVEFMDVSPKQVFSVNTNLIPFLEHDDANRALM GSNMQTQAVPLIRAQAPVVMTGLEERVVRDSLAALYAEED GEVAKVDGNRIVVRYEDGRLVEYPLRRFYRSNQGTALDQR PRVVVGQRVRKGDLLADGPASENGFLALGQNVLVAIMPFD GYNFEDAIVISEELLKRDFYTSIHIERYEIEARDTKLGPE RITRDIPHLSEAALRDLDEEGVVRIGAEVKPGDILVGRTS FKGESEPTPEERLLRSIFGEKARDVKDTSLRVPPGEGGIV VRTVRLRRGDPGVELKPGVREVVRVYVAQKRKLQVGDKLA NRHGNKGVVAKILPVEDMPHLPDGTPVDVILNPLGVPSRM NLGQILETHLGLAGYFLGQRYISPIFDGAKEPEIKELLAQ AFEVYFGKRKGEGFGVDKREVEVLRRAEKLGLVTPGKTPE EQLKELFLQGKVVLYDGRTGEPIEGPIVVGQMFIMKLYHM VEDKMHARSTGPYSLITQQPLGGKAQFGGQRFGEMEVWAL EAYGAAHTLQEMLTLKSDDIEGRNAAYEAIIKGEDVPEPS VPESFRVLVKELQALALDVQTLDEKDNPVDIFEGLASKR D:  KKEVRKVRIALASPEKIRSWSYGEVEKPETINYRTLKPER DGLFDERIFGPIKDYECACGKYKRQRFEGKVCERCGVEVT KSIVRRYRMGHIELATPAAHIWFVKDVPSKIGTLLDLSAT ELEQVLYFSKYIVLDPKGAILNGVPVEKRQLLTDEEYREL RYGKQETYPLPPGVDALVKDGEEVVKGQELAPGVVSRLDG VALYRFPRRVRVEYVKKERAGLRLPLAAWVEKEAYKPGEI LAELPEPYLFGDKIVAAIDPEEEVIAEAEGVVHLHEPASI LVVKARVYPFEDDVEVSTGDRVAPGDVLADGGKVKSDVYG RVEVDLVRNVVRVVESYDIDARMGAEAIQQLLKELDLEAL EKELLEEMKHPSRARRAKARKRLEVVRAFLDSGNRPEWMI LEAVPVLPPDLRPMVQVDGGRFATSDLNDLYRRLINRNNR LKKLLAQGAPEIIIRNEKRMLQEAVDALLDNGRRGAPVTN PGSDRPLRSLTDILSGKQGRFRQNLLGKRVDYSGRSVIVV GPQLKLHQCGLPKRMALELFKPFLLKKMEEKGIAPNVKAA RRMLERQRDIKDEVWDALEEVIHGKVVLLNRAPTLHRLGI QAFQPVLVEGQSIQLHPLVCEAFNADFDGDQMAVHVPLSS FAQAEARIQMLSAHNLLSPASGEPLAKPSRDIILGLYYIT QVRKEKKGAGLEFATPEEALAAHERGEVALNAPIKVAGRE TSVGRLKYVFANPDEALLAVAHGIVDLQDVVTVRYMGKRL ETSPGRILFARIVAEAVEDEKVAWELIQLDVPQEKNSLKD LVYQAFLRLGMEKTARLLDALKYYGFTFSTTSGITIGIDD AVIPEEKKQYLEEADRKLLQIEQAYEMGFLTDRERYDQIL QLWTETTEKVTQAVFKNFEENYPFNPLYVMAQSGARGNPQ QIRQLCGLRGLMQKPSGETFEVPVRSSFREGLTVLEYFIS SHGARKGGADTALRTADSGYLTRKLVDVTHEIVVREADCG TTNYISVPLFQPDEVTRSLRLRKRADIEAGLYGRVLAREV EVLGVRLEEGRYLSMDDVHLLIKAAEAGEIQEVPVRSPLT CQTRYGVCQKCYGYDLSMARPVSIGEAVGIVAAQSIGEPG TQLTMRTFHTGGVAGAADITQGLPRVIELFEARRPKAKAV ISEIDGVVRIEETEEKLSVFVESEGFSKEYKLPKEARLLV KDGDYVEAGQPLTRGAIDPHQLLEAKGPEAVERYLVEEIQ KVYRAQGVKLHDKHIEIVVRQMMKYVEVTDPGDSRLLEGQ VLEKWDVEALNERLIAEGKTPVAWKPLLMGVTKSALSTKS WLSAASFQNTTHVLTEAAIAGKKDELIGLKENVILGRLIP AGTGSDFVRFTQVVDQKTLKAIEEARKEAVEA E:  AEPGIDKLFGMVDSKYRLTVVVAKRAQQLLRHGFKNTVLE PEERPKMQTLEGLFDDPNAETWAMKELLTGRLVFGENLVP EDRLQKEMERIYPGE F:  KISTSDPVRQYLHEIGQVPLLTLEEEVELARKVEEGMEAI KKLSEITGLDPDLIREVVRAKILGSARVRHIPGLKETLDP KTVEEIDQKLKSLPKEHKRYLHIAREGEAARQHLIEANLR LVVSIAKKYTGRGLSFLDLIQEGNQGLIRAVEKFEYKRRF KFSTYATWWIRQAINRAIADQARTIRIPVHMVETINKLSR TARQLQQELGREPTYEEIAEAMGPGWDAKRVEETLKIAQE PVSLETPIGDEKDSFYGDFIPDEHLPSPVDAATQSLLSEE LEKALSKLSEREAMVLKLRKGLIDGEEVGAFFGVTRERIR QIENKALRKLKYHESRTRKLRDFLD Description Functional site 1) chain C residue 685 type sequence E description BINDING SITE FOR RESIDUE MG C 9004 source : AC1 2) chain C residue 879 type sequence R description BINDING SITE FOR RESIDUE MG C 9004 source : AC1 3) chain D residue 739 type sequence D description BINDING SITE FOR RESIDUE MG C 9004 source : AC1 4) chain D residue 1029 type sequence R description BINDING SITE FOR RESIDUE MG C 9004 source : AC1 5) chain D residue 58 type sequence C description BINDING SITE FOR RESIDUE ZN D 9058 source : AC2 6) chain D residue 60 type sequence C description BINDING SITE FOR RESIDUE ZN D 9058 source : AC2 7) chain D residue 73 type sequence C description BINDING SITE FOR RESIDUE ZN D 9058 source : AC2 8) chain D residue 76 type sequence C description BINDING SITE FOR RESIDUE ZN D 9058 source : AC2 9) chain D residue 1112 type sequence C description BINDING SITE FOR RESIDUE ZN D 9112 source : AC3 10) chain D residue 1194 type sequence C description BINDING SITE FOR RESIDUE ZN D 9112 source : AC3 11) chain D residue 1201 type sequence C description BINDING SITE FOR RESIDUE ZN D 9112 source : AC3 12) chain D residue 1204 type sequence C description BINDING SITE FOR RESIDUE ZN D 9112 source : AC3 13) chain D residue 739 type sequence D description BINDING SITE FOR RESIDUE MG D 9003 source : AC4 14) chain D residue 741 type sequence D description BINDING SITE FOR RESIDUE MG D 9003 source : AC4 15) chain D residue 743 type sequence D description BINDING SITE FOR RESIDUE MG D 9003 source : AC4 16) chain C residue 557 type sequence R description BINDING SITE FOR RESIDUE TGT D 9001 source : AC5 17) chain C residue 878 type sequence S description BINDING SITE FOR RESIDUE TGT D 9001 source : AC5 18) chain C residue 879 type sequence R description BINDING SITE FOR RESIDUE TGT D 9001 source : AC5 19) chain D residue 737 type sequence N description BINDING SITE FOR RESIDUE TGT D 9001 source : AC5 20) chain D residue 739 type sequence D description BINDING SITE FOR RESIDUE TGT D 9001 source : AC5 21) chain D residue 783 type sequence R description BINDING SITE FOR RESIDUE TGT D 9001 source : AC5 22) chain D residue 1029 type sequence R description BINDING SITE FOR RESIDUE TGT D 9001 source : AC5 23) chain D residue 1031 type sequence N description BINDING SITE FOR RESIDUE TGT D 9001 source : AC5 24) chain D residue 1034 type sequence Q description BINDING SITE FOR RESIDUE TGT D 9001 source : AC5 25) chain F residue 187-194 type prosite sequence LIEANLRL description CPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. LIEANLRL source prosite : PS00867 26) chain C residue 836-848 type prosite sequence GDKLANRHGNKGV description RNA_POL_BETA RNA polymerases beta chain signature. GdKLANrHGNKGV source prosite : PS01166 27) chain D residue 58 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_01322 source Swiss-Prot : SWS_FT_FI1 28) chain D residue 1201 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_01322 source Swiss-Prot : SWS_FT_FI1 29) chain D residue 1204 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_01322 source Swiss-Prot : SWS_FT_FI1 30) chain D residue 60 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_01322 source Swiss-Prot : SWS_FT_FI1 31) chain D residue 73 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_01322 source Swiss-Prot : SWS_FT_FI1 32) chain D residue 76 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_01322 source Swiss-Prot : SWS_FT_FI1 33) chain D residue 739 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_01322 source Swiss-Prot : SWS_FT_FI1 34) chain D residue 741 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_01322 source Swiss-Prot : SWS_FT_FI1 35) chain D residue 743 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_01322 source Swiss-Prot : SWS_FT_FI1 36) chain D residue 1112 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_01322 source Swiss-Prot : SWS_FT_FI1 37) chain D residue 1194 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_01322 source Swiss-Prot : SWS_FT_FI1

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