eF-site ID 1zyr-ABCDEF PDB Code 1zyr Chain A, B, C, D, E, F click to enlarge Title Structure of Thermus thermophilus RNA polymerase holoenzyme in complex with the antibiotic streptolydigin Classification TRANSCRIPTION,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 422 type sequence R description BINDING SITE FOR RESIDUE STD D 1525 source : AC1 2) chain C residue 423 type sequence A description BINDING SITE FOR RESIDUE STD D 1525 source : AC1 3) chain C residue 425 type sequence F description BINDING SITE FOR RESIDUE STD D 1525 source : AC1 4) chain C residue 428 type sequence R description BINDING SITE FOR RESIDUE STD D 1525 source : AC1 5) chain D residue 1082 type sequence A description BINDING SITE FOR RESIDUE STD D 1525 source : AC1 6) chain D residue 1085 type sequence A description BINDING SITE FOR RESIDUE STD D 1525 source : AC1 7) chain D residue 1086 type sequence L description BINDING SITE FOR RESIDUE STD D 1525 source : AC1 8) chain D residue 1090 type sequence D description BINDING SITE FOR RESIDUE STD D 1525 source : AC1 9) chain D residue 1257 type sequence P description BINDING SITE FOR RESIDUE STD D 1525 source : AC1 10) chain D residue 58 type sequence C description BINDING SITE FOR RESIDUE ZN D 9001 source : AC3 11) chain D residue 60 type sequence C description BINDING SITE FOR RESIDUE ZN D 9001 source : AC3 12) chain D residue 73 type sequence C description BINDING SITE FOR RESIDUE ZN D 9001 source : AC3 13) chain D residue 76 type sequence C description BINDING SITE FOR RESIDUE ZN D 9001 source : AC3 14) chain D residue 1112 type sequence C description BINDING SITE FOR RESIDUE ZN D 9002 source : AC4 15) chain D residue 1194 type sequence C description BINDING SITE FOR RESIDUE ZN D 9002 source : AC4 16) chain D residue 1195 type sequence Q description BINDING SITE FOR RESIDUE ZN D 9002 source : AC4 17) chain D residue 1196 type sequence T description BINDING SITE FOR RESIDUE ZN D 9002 source : AC4 18) chain D residue 1201 type sequence C description BINDING SITE FOR RESIDUE ZN D 9002 source : AC4 19) chain D residue 1204 type sequence C description BINDING SITE FOR RESIDUE ZN D 9002 source : AC4 20) chain D residue 739 type sequence D description BINDING SITE FOR RESIDUE MG D 9901 source : AC7 21) chain D residue 741 type sequence D description BINDING SITE FOR RESIDUE MG D 9901 source : AC7 22) chain D residue 743 type sequence D description BINDING SITE FOR RESIDUE MG D 9901 source : AC7 23) chain C residue 836-848 type prosite sequence GDKLANRHGNKGV description RNA_POL_BETA RNA polymerases beta chain signature. GdKLANrHGNKGV source prosite : PS01166 24) chain F residue 187-194 type prosite sequence LIEANLRL description CPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. LIEANLRL source prosite : PS00867 25) chain D residue 58 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_01322 source Swiss-Prot : SWS_FT_FI1 26) chain D residue 1201 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_01322 source Swiss-Prot : SWS_FT_FI1 27) chain D residue 1204 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_01322 source Swiss-Prot : SWS_FT_FI1 28) chain D residue 60 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_01322 source Swiss-Prot : SWS_FT_FI1 29) chain D residue 73 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_01322 source Swiss-Prot : SWS_FT_FI1 30) chain D residue 76 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_01322 source Swiss-Prot : SWS_FT_FI1 31) chain D residue 739 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_01322 source Swiss-Prot : SWS_FT_FI1 32) chain D residue 741 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_01322 source Swiss-Prot : SWS_FT_FI1 33) chain D residue 743 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_01322 source Swiss-Prot : SWS_FT_FI1 34) chain D residue 1112 type BINDING sequence C description BINDING => ECO:0000255|HAMAP-Rule:MF_01322 source Swiss-Prot : SWS_FT_FI1 35) 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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