eF-site ID 6rip-D PDB Code 6rip Chain D click to enlarge Title Cryo-EM structure of E. coli RNA polymerase backtracked elongation complex in swiveled state Classification TRANSCRIPTION Compound Non-template DNA Source (6RIP) Sequence D:  EFDAIKIALASPDMIRSWSFGEVKKPETINYRTFKPERDG LFCARIFGPVKDYECLCGKYKRLKHRGVICEKCGVEVTQT KVRRERMGHIELASPTAHIWFLKSLPSRIGLLLDMPLRDI ERVLYFESYVVIEGGMTNLERQQILTEEQYLDALEEFGDE FDAKMGAEAIQALLKSMDLEQECEQLREELNETNSETKRK KLTKRIKLLEAFVQSGNKPEWMILTVLPVLPPDLRPLVPL DGGRFATSDLNDLYRRVINRNNRLKRLLDLAAPDIIVRNE KRMLQEAVDALLDNGRRGRAITGSNKRPLKSLADMIKGKQ GRFRQNLLGKRVDYSGRSVITVGPYLRLHQCGLPKKMALE LFKPFIYGKLELRGLATTIKAAKKMVEREEAVVWDILDEV IREHPVLLNRAPTLHRLGIQAFEPVLIEGKAIQLHPLVCA AYNADFDGDQMAVHVPLTLEAQLEARALMMSTNNILSPAN GEPIIVPSQDVVLGLYYMTRDCVNAKGEGMVLTGPKEAER LYRSGLASLHARVKVRITEYEKDANGELVAKTSLKDTTVG RAILWMIVPKGLPYSIVNQALGKKAISKMLNTCYRILGLK PTVIFADQIMYTGFAYAARSGASVGIDDMVIPEKKHEIIS EAEAEVAEIQEQFQSGLVTAGERYNKVIDIWAAANDRVSK AMMDNLQTETVINRDGQEEKQVSFNSIYMMADSGARGSAA QIRQLAGMRGLMAKPDGSIIETPITANFREGLNVLQYFIS THGARKGLADTALKTANSGYLTRRLVDVAQDLVVTEDDCG THEGIMMTPVIEGGDVKEPLRDRVLGRVTAEDVLKPGTAD ILVPRNTLLHEQWCDLLEENSVDAVKVRSVVSCDTDFGVC AHCYGRDLARGHIINKGEAIGVIAAQSIGEPGTQLTMRTF SSIQVKNKGSIKLSNVKSVVNSSGKLVITSRNTELKLIDE FGRTKESYKVPYGAVLAKGDGEQVAGGETVANWDPHTMPV ITEVSGFVRFTDMIDGQTITRQTDELTGLSSLVVLDSAER TAGGKDLRPALKIVDAQGNDVLIPGTDMPAQYFLPGKAIV QLEDGVQISSGDTLARITGGLPRVADLFEARRPKEPAILA EISGIVSFGKETKGKRRLVITPVDGSDPYEEMIPKWRQLN VFEGERVERGDVISDGPEAPHDILRLRGVHAVTRYIVNEV QDVYRLQGVKINDKHIEVIVRQMLRKATIVNAGSSDFLEG EQVEYSRVKIANRELEANGKVGATYSRDLLGITKASLATE SFISAASFQETTRVLTEAAVAGKRDELRGLKENVIVGRLI PAGTGYAYHQDRMRRR Description (1)  DNA-directed RNA polymerase subunit alpha, DNA-directed RNA polymerase subunit beta, DNA-directed RNA polymerase subunit beta', DNA-directed RNA polymerase subunit omega/DNA Complex Functional site 1) chain D residue 70 type sequence C description binding site for residue ZN D 1501 source : AC1 2) chain D residue 71 type sequence L description binding site for residue ZN D 1501 source : AC1 3) chain D residue 72 type sequence C description binding site for residue ZN D 1501 source : AC1 4) chain D residue 85 type sequence C description binding site for residue ZN D 1501 source : AC1 5) chain D residue 88 type sequence C description binding site for residue ZN D 1501 source : AC1 6) chain D residue 814 type sequence C description binding site for residue ZN D 1502 source : AC2 7) chain D residue 883 type sequence R description binding site for residue ZN D 1502 source : AC2 8) chain D residue 888 type sequence C description binding site for residue ZN D 1502 source : AC2 9) chain D residue 895 type sequence C description binding site for residue ZN D 1502 source : AC2 10) chain D residue 898 type sequence C description binding site for residue ZN D 1502 source : AC2 11) chain D residue 460 type sequence D description binding site for residue MG D 1503 source : AC3 12) chain D residue 462 type sequence D description binding site for residue MG D 1503 source : AC3 13) chain D residue 464 type sequence D description binding site for residue MG D 1503 source : AC3 14) chain D residue 895 type BINDING sequence C description BINDING => ECO:0000269|PubMed:32871103, ECO:0007744|PDB:4MEX, ECO:0007744|PDB:4MEY source Swiss-Prot : SWS_FT_FI1 15) chain D residue 898 type BINDING sequence C description BINDING => ECO:0000269|PubMed:32871103, ECO:0007744|PDB:4MEX, ECO:0007744|PDB:4MEY source Swiss-Prot : SWS_FT_FI1 16) chain D residue 460 type BINDING sequence D description BINDING => ECO:0000269|PubMed:32871103, ECO:0007744|PDB:4MEX, ECO:0007744|PDB:4MEY source Swiss-Prot : SWS_FT_FI1 17) chain D residue 462 type BINDING sequence D description BINDING => ECO:0000269|PubMed:32871103, ECO:0007744|PDB:4MEX, ECO:0007744|PDB:4MEY source Swiss-Prot : SWS_FT_FI1 18) chain D residue 464 type BINDING sequence D description BINDING => ECO:0000269|PubMed:32871103, ECO:0007744|PDB:4MEX, ECO:0007744|PDB:4MEY source Swiss-Prot : SWS_FT_FI1 19) chain D residue 814 type BINDING sequence C description BINDING => ECO:0000269|PubMed:32871103, ECO:0007744|PDB:4MEX, ECO:0007744|PDB:4MEY source Swiss-Prot : SWS_FT_FI1 20) chain D residue 888 type BINDING sequence C description BINDING => ECO:0000269|PubMed:32871103, ECO:0007744|PDB:4MEX, ECO:0007744|PDB:4MEY source Swiss-Prot : SWS_FT_FI1 21) chain D residue 70 type BINDING sequence C description BINDING => ECO:0000269|PubMed:32871103, ECO:0007744|PDB:4MEX, ECO:0007744|PDB:4MEY source Swiss-Prot : SWS_FT_FI1 22) chain D residue 72 type BINDING sequence C description BINDING => ECO:0000269|PubMed:32871103, ECO:0007744|PDB:4MEX, ECO:0007744|PDB:4MEY source Swiss-Prot : SWS_FT_FI1 23) chain D residue 85 type BINDING sequence C description BINDING => ECO:0000269|PubMed:32871103, ECO:0007744|PDB:4MEX, ECO:0007744|PDB:4MEY source Swiss-Prot : SWS_FT_FI1 24) chain D residue 88 type BINDING sequence C description BINDING => ECO:0000269|PubMed:32871103, ECO:0007744|PDB:4MEX, ECO:0007744|PDB:4MEY source Swiss-Prot : SWS_FT_FI1 25) chain D residue 983 type MOD_RES sequence K description N6-acetyllysine => ECO:0000255|HAMAP-Rule:MF_01322, ECO:0000269|PubMed:18723842 source Swiss-Prot : SWS_FT_FI2

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