eF-site ID 3eql-ABCDEF PDB Code 3eql Chain A, B, C, D, E, F click to enlarge Title Crystal structure of the T. Thermophilus RNA polymerase holoenzyme in complex with antibiotic myxopyronin Classification TRANSFERASE Compound DNA-directed RNA polymerase subunit alpha 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 VALYRFASILVVKARVYPFEDDVEVSTGDRVAPGDVLADG GKVKSDVYGRVEVDLVRNVVRVVESYDIDARMGAEAIQQL LKELDLEALEKELLEEMKHPSRARRAKARKRLEVVRAFLD SGNRPEWMILEAVPVLPPDLRPMVQVDGGRFATSDLNDLY RRLINRNNRLKKLLAQGAPEIIIRNEKRMLQEAVDALLDN GRRGAPVTNPGSDRPLRSLTDILSGKQGRFRQNLLGKRVD YSGRSVIVVGPQLKLHQCGLPKRMALELFKPFLLKKMEEK GIAPNVKAARRMLERQRDIKDEVWDALEEVIHGKVVLLNR APTLHRLGIQAFQPVLVEGQSIQLHPLVCEAFNADFDGDQ MAVHVPLSSFAQAEARIQMLSAHNLLSPASGEPLAKPSRD IILGLYYITQVRKEKKGAGLEFATPEEALAAHERGEVALN APIKVAGRETSVGRLKYVFANPDEALLAVAHGIVDLQDVV TVRYMGKRLETSPGRILFARIVAEAVEDEKVAWELIQLDV PQEKNSLKDLVYQAFLRLGMEKTARLLDALKYYGFTFSTT SGITIGIDDAVIPEEKKQYLEEADRKLLQIEQAYEMGFLT DRERYDQILQLWTETTEKVTQAVFKNFEENYPFNPLYVMA QSGARGNPQQIRQLCGLRGLMQKPSGETFEVPVRSSFREG LTVLEYFISSHGARKGGADTALRTADSGYLTRKLVDVTHE IVVREADCGTTNYISVPLFQPDEVTRSLRLRKRADIEAGL YGRVLAREVEVLGVRLEEGRYLSMDDVHLLIKAAEAGEIQ EVPVRSPLTCQTRYGVCQKCYGYDLSMARPVSIGEAVGIV AAQSIGEPGTQLTMRTFHTGGVAGAADITQGLPRVIELFE ARRPKAKAVISEIDGVVRIEETEEKLSVFVESEGFSKEYK LPKEARLLVKDGDYVEAGQPLTRGAIDPHQLLEAKGPEAV ERYLVEEIQKVYRAQGVKLHDKHIEIVVRQMMKYVEVTDP GDSRLLEGQVLEKWDVEALNERLIAEGKTPVAWKPLLMGV TKSALSTKSWLSAASFQNTTHVLTEAAIAGKKDELIGLKE NVILGRLIPAGTGSDFVRFTQVVDQKTLKAIEEARKEAVE A E:  AEPGIDKLFGMVDSKYRLTVVVAKRAQQLLRHGFKNTVLE PEERPKMQTLEGLFDDPNAVTWAMKELLTGRLVFGENLVP EDRLQKEMERLYPVE F:  KISTSDPVRQYLHEIGQVPLLTLEEEVELARKVEEGMEAI KKLSEITGLDPDLIREVVRAKILGSARVRHIPGLKETLDP KTVEEIDQKLKSLPKEHKRYLHIAREGEAARQHLIEANLR LVVSIAKKYTGRGLSFLDLIQEGNQGLIRAVEKFEYKRRF KFSTYATWWIRQAINRAIADQARTIRIPVHMVETINKLSR TARQLQQELGREPTYEEIAEAMGPGWDAKRVEETLKIAQE PVSLETPIGDEKDSFYGDFIPDEHLPSPVDAATQSLLSEE LEKALSKLSEREAMVLKLRKGLIDGEEVGAFFGVTRERIR QIENKALRKLKYHESRTRKLRDFLD Description Functional site 1) chain D residue 58 type sequence C description BINDING SITE FOR RESIDUE ZN D1525 source : AC1 2) chain D residue 60 type sequence C description BINDING SITE FOR RESIDUE ZN D1525 source : AC1 3) chain D residue 73 type sequence C description BINDING SITE FOR RESIDUE ZN D1525 source : AC1 4) chain D residue 76 type sequence C description BINDING SITE FOR RESIDUE ZN D1525 source : AC1 5) chain D residue 1112 type sequence C description BINDING SITE FOR RESIDUE ZN D1526 source : AC2 6) chain D residue 1194 type sequence C description BINDING SITE FOR RESIDUE ZN D1526 source : AC2 7) chain D residue 1201 type sequence C description BINDING SITE FOR RESIDUE ZN D1526 source : AC2 8) chain D residue 1204 type sequence C description BINDING SITE FOR RESIDUE ZN D1526 source : AC2 9) chain C residue 1034 type sequence E description BINDING SITE FOR RESIDUE MXP D1527 source : AC3 10) chain C residue 1038 type sequence W description BINDING SITE FOR RESIDUE MXP D1527 source : AC3 11) chain C residue 1041 type sequence E description BINDING SITE FOR RESIDUE MXP D1527 source : AC3 12) chain C residue 1084 type sequence S description BINDING SITE FOR RESIDUE MXP D1527 source : AC3 13) chain C residue 1088 type sequence L description BINDING SITE FOR RESIDUE MXP D1527 source : AC3 14) chain D residue 610 type sequence K description BINDING SITE FOR RESIDUE MXP D1527 source : AC3 15) chain D residue 611 type sequence Q description BINDING SITE FOR RESIDUE MXP D1527 source : AC3 16) chain D residue 619 type sequence L description BINDING SITE FOR RESIDUE MXP D1527 source : AC3 17) chain D residue 620 type sequence G description BINDING SITE FOR RESIDUE MXP D1527 source : AC3 18) chain D residue 1463 type sequence K description BINDING SITE FOR RESIDUE MXP D1527 source : AC3 19) chain D residue 1466 type sequence V description BINDING SITE FOR RESIDUE MXP D1527 source : AC3 20) chain D residue 1467 type sequence I description BINDING SITE FOR RESIDUE MXP D1527 source : AC3 21) chain D residue 739 type sequence D description BINDING SITE FOR RESIDUE MG D1528 source : AC4 22) chain D residue 741 type sequence D description BINDING SITE FOR RESIDUE MG D1528 source : AC4 23) chain D residue 743 type sequence D description BINDING SITE FOR RESIDUE MG D1528 source : AC4 24) chain D residue 1201 type DNA_BIND sequence C description H-T-H motif => ECO:0000255|HAMAP-Rule:MF_00963 source Swiss-Prot : SWS_FT_FI1 25) chain D residue 1204 type DNA_BIND sequence C description H-T-H motif => ECO:0000255|HAMAP-Rule:MF_00963 source Swiss-Prot : SWS_FT_FI1 26) chain D residue 73 type DNA_BIND sequence C description H-T-H motif => ECO:0000255|HAMAP-Rule:MF_00963 source Swiss-Prot : SWS_FT_FI1 27) chain D residue 76 type DNA_BIND sequence C description H-T-H motif => ECO:0000255|HAMAP-Rule:MF_00963 source Swiss-Prot : SWS_FT_FI1 28) chain D residue 739 type DNA_BIND sequence D description H-T-H motif => ECO:0000255|HAMAP-Rule:MF_00963 source Swiss-Prot : SWS_FT_FI1 29) chain D residue 741 type DNA_BIND sequence D description H-T-H motif => ECO:0000255|HAMAP-Rule:MF_00963 source Swiss-Prot : SWS_FT_FI1 30) chain D residue 743 type DNA_BIND sequence D description H-T-H motif => ECO:0000255|HAMAP-Rule:MF_00963 source Swiss-Prot : SWS_FT_FI1 31) chain D residue 1112 type DNA_BIND sequence C description H-T-H motif => ECO:0000255|HAMAP-Rule:MF_00963 source Swiss-Prot : SWS_FT_FI1 32) chain D residue 1194 type DNA_BIND sequence C description H-T-H motif => ECO:0000255|HAMAP-Rule:MF_00963 source Swiss-Prot : SWS_FT_FI1 33) chain C residue 836-848 type prosite sequence GDKLANRHGNKGV description RNA_POL_BETA RNA polymerases beta chain signature. GdKLANrHGNKGV source prosite : PS01166 34) chain F residue 187-194 type prosite sequence LIEANLRL description CPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. LIEANLRL source prosite : PS00867

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