eF-site ID 6n61-D PDB Code 6n61 Chain D click to enlarge Title Escherichia coli RNA polymerase sigma70-holoenzyme bound to upstream fork promoter DNA and Capistruin Classification TRANSFERASE/DNA Compound DNA-directed RNA polymerase subunit alpha Source (A0A096YQF1_BURTA) Sequence D:  FDAIKIALASPDMIRSWSFGEVKKPETINYRTFKPERDGL FCARIFGPVKDYECLCGKYKRLKHRGVICEKCGVEVTQTK VRRERMGHIELASPTAHIWFLKSLPSRIGLLLDMPLRDIE RVLYFESYVVIEGGMTNLERQQILTEEQYLDALEEFGDEF DAKMGAEAIQALLKSMDLEQECEQLREELNETNSETKRKK LTKRIKLLEAFVQSGNKPEWMILTVLPVLPPDLRPLVPLD GGRFATSDLNDLYRRVINRNNRLKRLLDLAAPDIIVRNEK RMLQEAVDALLDNGRRGRAITGSNKRPLKSLADMIKGKQG RFRQNLLGKRVDYSGRSVITVGPYLRLHQCGLPKKMALEL FKPFIYGKLELRGLATTIKAAKKMVEREEAVVWDILDEVI REHPVLLNRAPTLHRLGIQAFEPVLIEGKAIQLHPLVCAA YNADFDGDQMAVHVPLTLEAQLEARALMMSTNNILSPANG EPIIVPSQDVVLGLYYMTRDCVNAKGEGMVLTGPKEAERL YRSGLASLHARVKVRITEYEKDANGELVAKTSLKDTTVGR AILWMIVPKGLPYSIVNQALGKKAISKMLNTCYRILGLKP TVIFADQIMYTGFAYAARSGASVGIDDMVIPEKKHEIISE AEAEVAEIQEQFQSGLVTAGERYNKVIDIWAAANDRVSKA MMDNLQTETVINRDGQEEKQVSFNSIYMMADSGARGSAAQ IRQLAGMRGLMAKPDGSIIETPITANFREGLNVLQYFIST HGARKGLADTALKTANSGYLTRRLVDVAQDLVVTEDDCGT HEGIMMTPVIEGGDVKEPLRDRVLGRVTAEDVLKPGTADI LVPRNTLLHEQWCDLLEENSVDAVKVRSVVSCDTDFGVCA HCYGRDLARGHIINKGEAIGVIAAQSIGEPGTQLTMRTFH IGSSIQVKNKGSIKLSNVKSVVNSSGKLVITSRNTELKLI DEFGRTKESYKVPYGAVLAKGDGEQVAGGETVANWDPHTM ITGGLPRVADLFEARRPKEPAILAEISGIVSFGKETKGKR RLVITPVDGSDPYEEMIPKWRQLNVFEGERVERGDVISDG PEAPHDILRLRGVHAVTRYIVNEVQDVYRLQGVKINDKHI EVIVRQMLRKATIVNAGSSDGEQVEYSRVKIANRELEANG KVGATYSRDLLGITKASLATESFISAASFQETTRVLTEAA VAGKRDELRGLKENVIVGRLIPAGTGYAYHQDRMRRRAA Description Functional site 1) chain D residue 460 type sequence D description binding site for residue MG D 1501 source : AC2 2) chain D residue 462 type sequence D description binding site for residue MG D 1501 source : AC2 3) chain D residue 464 type sequence D description binding site for residue MG D 1501 source : AC2 4) chain D residue 70 type sequence C description binding site for residue ZN D 1502 source : AC3 5) chain D residue 72 type sequence C description binding site for residue ZN D 1502 source : AC3 6) chain D residue 85 type sequence C description binding site for residue ZN D 1502 source : AC3 7) chain D residue 87 type sequence K description binding site for residue ZN D 1502 source : AC3 8) chain D residue 88 type sequence C description binding site for residue ZN D 1502 source : AC3 9) chain D residue 814 type sequence C description binding site for residue ZN D 1503 source : AC4 10) chain D residue 888 type sequence C description binding site for residue ZN D 1503 source : AC4 11) chain D residue 895 type sequence C description binding site for residue ZN D 1503 source : AC4 12) chain D residue 898 type sequence C description binding site for residue ZN D 1503 source : AC4 13) chain D residue 511 type sequence Y description binding site for residue EPE D 1504 source : AC5 14) chain D residue 594 type sequence Q description binding site for residue EPE D 1504 source : AC5 15) chain D residue 595 type sequence A description binding site for residue EPE D 1504 source : AC5 16) chain D residue 596 type sequence L description binding site for residue EPE D 1504 source : AC5 17) chain D residue 597 type sequence G description binding site for residue EPE D 1504 source : AC5 18) chain D residue 600 type sequence A description binding site for residue EPE D 1504 source : AC5 19) chain D residue 727 type sequence D description binding site for residue EPE D 1504 source : AC5 20) 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 21) 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 22) 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 23) 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 24) 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 25) 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 26) 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 27) 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 28) 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 29) 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 30) 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 31) 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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