eF-site ID 2e2j-ABCEFHIJKLNRT PDB Code 2e2j Chain A, B, C, E, F, H, I, J, K, L, N, R, T Title RNA polymerase II elongation complex in 5 mM Mg+2 with GMPCPP Classification TRANSCRIPTION,TRANSFERASE/DNA-RNA HYBRID Compound 5'-R(P*AP*UP*CP*GP*AP*GP*AP*GP*G)-3' Source ORGANISM_COMMON: baker's yeast; ORGANISM_SCIENTIFIC: Saccharomyces cerevisiae; Sequence A:  GQQYSSAPLRTVKEVQFGLFSPEEVRAISVAKIRFPETMD ETQTRAKIGGLNDPRLGSIDRNLKCQTCQEGMNECPGHFG HIDLAKPVFHVGFIAKIKKVCECVCMHCGKLLLDEHNELM RQALAIKDSKKRFAAIWTLCKTKMVCETDVPSLVSRGGCG NTQPTIRKDGLKLVGSWKLRVLSTEEILNIFKHISVKDFT SLGFNEVFSRPEWMILTCLPVPPPPVRPSISFNESQRGED DLTFKLADILKANISLETLEHNGAPHHAIEEAESLLQFHV ATYMDNDIAGQPQALQKSGRPVKSIRARLKGKEGRIRGNL MGKRVDFSARTVISGDPNLELDQVGVPKSIAKTLTYPEVV TPYNIDRLTQLVRNGPNEHPGAKYVIRDSGDRIDLRYSKR AGDIQLQYGWKVERHIMDNDPVLFNRQPSLHKMSMMAHRV KVIPYSTFRLNLSVTSPYNADFDGDEMNLHVPQSEETRAE LSQLCAVPLQIVSPQSNKPCMGIVQDTLCGIRKLTLRDTF IELDQVLNMLYWVPDWDGVIPTPAIIKPKPLWSGKQILSV AIPNGIHLQRFDEGTTLLSPKDNGMLIIDGQIIFGVVEKK TVGSSNGGLIHVVTREKGPQVCAKLFGNIQKVVNFWLLHN GFSTGIGDTIADGPTMREITETIAEAKKKVLDVTKEAQAN LLTAKHGMTLRESFEDNVVRFLNEARDKAGRLAEVNLKDL NNVKQMVMAGSKGSFINIAQMSACVGQQSVEGKRIAFGFV DRTLPHFSKDDYSPESKGFVENSYLRGLTPQEFFFHAMGG REGLIDTAVKTAETGYIQRRLVKALEDIMVHYDNTTRNSL GNVIQFIYGEDGMDAAHIEKQSLDTIGGSDAAFEKRYRVD LLNTDHTLDPSLLESGSEILGDLKLQVLLDEEYKQLVKDR KFLREVFVDGEANWPLPVNIRRIIQNAQQTFHIDHTKPSD LTIKDIVLGVKDLQENLLVLRGKNEIIQNAQRDAVTLFCC LLRSRLATRRVLQEYRLTKQAFDWVLSNIEAQFLRSVVHP GEMVGVLAAQSIGEPATQMTLKKVTSGVPRLKEILNVAKN MKTPSLTVYLEPGHAADQEQAKLIRSAIEHTTLKSVTIAS EIYYDPDPRSTVIPEDEEIIQLHFSLQQSPWLLRLELDRA AMNDKDLTMGQVGERIKQTFKNDLFVIWSEDNDEKLIIRC RVVAEEDHMLKKIENTMLENITLRGVENIERVVMMKYDRK VPSPTGEYVKEPEWVLETDGVNLSEVMTVPGIDPTRIYTN SFIDIMEVLGIEAGRAALYKEVYNVIASDGSYVNYRHMAL LVDVMTTQGGLTSVTRHGFNRSNTGALMRCSFEETVEILF EAGASAELDDCRGVSENVILGQMAPIGTGAFDVMI B:  DESAPITAEDSWAVISAFFREKGLVSQQLDSFNQFVDYTL QDIICEDSTLIEISFGKIYVTKPMVNESDGVTHALYPQEA RLRNLTYSSGLFVDVKKKVFIGRLPIMLRSKNCYLSEATE SDLYKLKECPFDMGGYFIINGSEKVLIAQERSAGNIVQVF KKAAPSPISHVAEIRSALEKGSRFISTLQVKLYGREGSSA RTIKATLPYIKQDIPIVIIFRALGIIPDGEILEHICYDVN DWQMLEMLKPCVEDGFVIQDRETALDFIGKEKRIQYAKDI LQKEFLPHITQLEGFESRKAFFLGYMINRLLLCALDRKDQ DDRDHFGKKRLDLAGPLLAQLFKTLFKKLTKDIFRYMQRT VELAINAKTITSGLKYALATGNWGEQKKAMSSRAGVSQVL NRYTYSSTLSHLRRTNTPIAKPRQLHNTHWGLVCPAETPE GQACGLVKNLSLMSCISVGTDPMPIITFLSEWGMEPLEDY VPHQSPDATRVFVNGVWHGVHRNPARLMETLRTLRRKGDI NPEVSMIRDIREKELKIFTDAGRVYRPLFIVEDDESLGHK ELKVRKGHIAKLMATEYQDEYTWSSLLNEGLVEYIDAEEE ESILIAMQPEDLEPAEADVDPAKRIRVSHHATTFTHCEIH PSMILGVAASIIPFPDHNQSPRNTYQSAMGKQAMGVFLTN YNVRMDTMANILYYPQKPLGTTRAMEYLKFRELPAGQNAI VAIACYSGYNQEDSMIMNQSSIDRGLFRSLFFRSYMDQEK KYGMSITETFEKPQRTNTLRMKHGTYDKLDDDGLIAPGVR VSGEDVIIGKTTPISSKRDASTPLRSTENGIVDQVLVTTN QDGLKFVKVRVRTTKIPQIGDKFASRHGQKGTIGITYRRE DMPFTAEGIVPDLIINPHAIPSRMTVAHLIECLLSKVAAL SGNEGDASPFTDITVEGISKLLREHGYQSRGFEVMYNGHT GKKLMAQIFFGPTYYQRLRHMVDDKIHARARGPMQVLTRQ PVEGRSRDGGLRFGEMERDCMIAHGAASFLKERLMEASDA FRVHICGICGLMTVIAKLNHNQFECKGCDNKIDIYQIHIP YAAKLLFQELMAMNITPRLYTDRSR C:  SEEGPQVKIREASKDNVDFILSNVDLAMANSLRRVMIAEI PTLAIDSVEVETNTTVLADEFIAHRLGLIPLQSMDIEQLE YSRDCFCEDHCDKCSVVLTLQAFGESESTTNVYSKDLVIV SNLMGRNIGHPIIQDKEGNGVLICKLRKGQELKLTCVAKK GIAKEHAKWGPAAAIEFEYDPWNKLKHTDYWYEQDSAKEW PQSKNCEYEDPPNEGDPFDYKAQADTFYMNVESVGSIPVD QVVVRGIDTLQKKVASILLALTQMDQD E:  DQENERNISRLWRAFRTVKEMVKDRGYFITQEEVELPLED FKAKYCDSMGRPQRKMMSFQANPTEESISKFPDMGSLWVE FCDEPSVGVKTMKTFVIHIQEKNFQTGIFVYQNNITPSAM KLVPSIPPATIETFNEAALVVNITHHELVPKHIRLSSDEK RELLKRYRLKESQLPRIQRADPVALYLGLKRGEVVKIIRK SETSGRYASYRICM F:  LKEKAIPKDQRATTPYMTKYERARILGTRALQISMNAPVF VDLEGETDPLRIAMKELAEKKIPLVIRRYLPDGSFEDWSV EELIVD H:  SNTLFDDIFQVSEVDPGRYNKVCRIEAASTTQDQCKLTLD INVELFPVAAQDSLTVTIASSLTRSWRPPQAGDRSLADDY DYVMYGTAYKFEEVSKDLIAVYYSFGGLLMRLEGNYRNLN NLKQENAYLLIRR I:  TTFRFCRDCNNMLYPREDKENNRLLFECRTCSYVEEAGSP LVYRHELITNIGETAGVVQDIGSDPTLPRSDRECPKCHSR ENVFFQSQQRRKDTSMVLFFVCLSCSHIFTSDQKNKRTQ J:  MIVPVRCFSCGKVVGDKWESYLNLLQEDELDEGTALSRLG LKRYCCRRMILTHVDLIEKFLRYNP K:  MNAPDRFELFLLGEGESKLKIDPDTKAPNAVVITFEKEDH TLGNLIRAELLNDRKVLFAAYKVEHPFFARFKLRIQTTEG YDPKDALKNACNSIINKLGALKTNFETEWNLQTL L:  ATLKYICAECSSKLSLSRTDAVRCKDCGHRILLKARTKRL VQFEAR N:  CTGCTTATCGGTA R:  AUCGAGAGG T:  TACCGATAAGCAGACGACCCTCTCGAT Description Functional site 1) chain A residue 107 type sequence C description BINDING SITE FOR RESIDUE ZN A 1734 source : AC1 2) chain A residue 110 type sequence C description BINDING SITE FOR RESIDUE ZN A 1734 source : AC1 3) chain A residue 148 type sequence C description BINDING SITE FOR RESIDUE ZN A 1734 source : AC1 4) chain A residue 167 type sequence C description BINDING SITE FOR RESIDUE ZN A 1734 source : AC1 5) chain A residue 67 type sequence C description BINDING SITE FOR RESIDUE ZN A 1735 source : AC2 6) chain A residue 70 type sequence C description BINDING SITE FOR RESIDUE ZN A 1735 source : AC2 7) chain A residue 77 type sequence C description BINDING SITE FOR RESIDUE ZN A 1735 source : AC2 8) chain A residue 80 type sequence H description BINDING SITE FOR RESIDUE ZN A 1735 source : AC2 9) chain B residue 1163 type sequence C description BINDING SITE FOR RESIDUE ZN B 1307 source : AC3 10) chain B residue 1166 type sequence C description BINDING SITE FOR RESIDUE ZN B 1307 source : AC3 11) chain B residue 1182 type sequence C description BINDING SITE FOR RESIDUE ZN B 1307 source : AC3 12) chain B residue 1185 type sequence C description BINDING SITE FOR RESIDUE ZN B 1307 source : AC3 13) chain C residue 86 type sequence C description BINDING SITE FOR RESIDUE ZN C 319 source : AC4 14) chain C residue 88 type sequence C description BINDING SITE FOR RESIDUE ZN C 319 source : AC4 15) chain C residue 92 type sequence C description BINDING SITE FOR RESIDUE ZN C 319 source : AC4 16) chain C residue 95 type sequence C description BINDING SITE FOR RESIDUE ZN C 319 source : AC4 17) chain I residue 7 type sequence C description BINDING SITE FOR RESIDUE ZN I 203 source : AC5 18) chain I residue 10 type sequence C description BINDING SITE FOR RESIDUE ZN I 203 source : AC5 19) chain I residue 29 type sequence C description BINDING SITE FOR RESIDUE ZN I 203 source : AC5 20) chain I residue 31 type sequence T description BINDING SITE FOR RESIDUE ZN I 203 source : AC5 21) chain I residue 32 type sequence C description BINDING SITE FOR RESIDUE ZN I 203 source : AC5 22) chain I residue 75 type sequence C description BINDING SITE FOR RESIDUE ZN I 204 source : AC6 23) chain I residue 78 type sequence C description BINDING SITE FOR RESIDUE ZN I 204 source : AC6 24) chain I residue 103 type sequence C description BINDING SITE FOR RESIDUE ZN I 204 source : AC6 25) chain I residue 106 type sequence C description BINDING SITE FOR RESIDUE ZN I 204 source : AC6 26) chain J residue 7 type sequence C description BINDING SITE FOR RESIDUE ZN J 101 source : AC7 27) chain J residue 10 type sequence C description BINDING SITE FOR RESIDUE ZN J 101 source : AC7 28) chain J residue 45 type sequence C description BINDING SITE FOR RESIDUE ZN J 101 source : AC7 29) chain J residue 46 type sequence C description BINDING SITE FOR RESIDUE ZN J 101 source : AC7 30) chain L residue 31 type sequence C description BINDING SITE FOR RESIDUE ZN L 105 source : AC8 31) chain L residue 34 type sequence C description BINDING SITE FOR RESIDUE ZN L 105 source : AC8 32) chain L residue 48 type sequence C description BINDING SITE FOR RESIDUE ZN L 105 source : AC8 33) chain L residue 51 type sequence C description BINDING SITE FOR RESIDUE ZN L 105 source : AC8 34) chain A residue 481 type sequence D description BINDING SITE FOR RESIDUE MG A 2001 source : AC9 35) chain A residue 483 type sequence D description BINDING SITE FOR RESIDUE MG A 2001 source : AC9 36) chain A residue 485 type sequence D description BINDING SITE FOR RESIDUE MG A 2001 source : AC9 37) chain R residue 10 type sequence G description BINDING SITE FOR RESIDUE MG A 2001 source : AC9 38) chain A residue 481 type sequence D description BINDING SITE FOR RESIDUE MG A 2002 source : BC1 39) chain A residue 483 type sequence D description BINDING SITE FOR RESIDUE MG A 2002 source : BC1 40) chain B residue 837 type sequence D description BINDING SITE FOR RESIDUE MG A 2002 source : BC1 41) chain A residue 446 type sequence R description BINDING SITE FOR RESIDUE G2P T 3000 source : BC2 42) chain A residue 448 type sequence P description BINDING SITE FOR RESIDUE G2P T 3000 source : BC2 43) chain A residue 479 type sequence N description BINDING SITE FOR RESIDUE G2P T 3000 source : BC2 44) chain B residue 766 type sequence R description BINDING SITE FOR RESIDUE G2P T 3000 source : BC2 45) chain B residue 1020 type sequence R description BINDING SITE FOR RESIDUE G2P T 3000 source : BC2 46) chain R residue 10 type sequence G description BINDING SITE FOR RESIDUE G2P T 3000 source : BC2 47) chain T residue 18 type sequence C description BINDING SITE FOR RESIDUE G2P T 3000 source : BC2 48) chain T residue 19 type sequence C description BINDING SITE FOR RESIDUE G2P T 3000 source : BC2 49) chain B residue 837 type catalytic sequence D description 788 source MCSA : MCSA1 50) chain A residue 483 type catalytic sequence D description 788 source MCSA : MCSA1 51) chain A residue 485 type catalytic sequence D description 788 source MCSA : MCSA1 52) chain I residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI5 53) chain J residue 2-11 type prosite sequence IVPVRCFSCG description RNA_POL_N_8KD RNA polymerases N / 8 Kd subunits signature. IVPVrCFSCG source prosite : PS01112 54) chain F residue 86-100 type prosite sequence TKYERARILGTRALQ description RNA_POL_K_14KD RNA polymerases K / 14 to 18 Kd subunits signature. TkYErARiLGtRAlQ source prosite : PS01111 55) chain I residue 75-110 type prosite sequence CPKCHSRENVFFQSQQRRKDTSMVLFFVCLSCSHIF description ZF_TFIIS_1 Zinc finger TFIIS-type signature. CpkChsrenvffqSQQRRkDTSmvlffvCls...CshiF source prosite : PS00466 56) chain I residue 6-32 type prosite sequence FCRDCNNMLYPREDKENNRLLFECRTC description RNA_POL_M_15KD RNA polymerases M / 15 Kd subunits signature. FCrDCNNMLypredkennrllfeCrtC source prosite : PS01030 57) chain C residue 31-71 type prosite sequence NSLRRVMIAEIPTLAIDSVEVETNTTVLADEFIAHRLGLI P description RNA_POL_D_30KD RNA polymerases D / 30 to 40 Kd subunits signature. NSLRRvmiaeiptlAidsVevetNtTvlaDEfIAhRLGLIP source prosite : PS00446 58) chain E residue 147-160 type prosite sequence HELVPKHIRLSSDE description RNA_POL_H_23KD RNA polymerases H / 23 Kd subunits signature. HELVPKHirLssDE source prosite : PS01110 59) chain K residue 35-66 type prosite sequence FEKEDHTLGNLIRAELLNDRKVLFAAYKVEHP description RNA_POL_L_13KD RNA polymerases L / 13 to 16 Kd subunits signature. FekEdHTLgNlIraeLlndrkVlfaaYkveHP source prosite : PS01154 60) chain B residue 977-989 type prosite sequence GDKFASRHGQKGT description RNA_POL_BETA RNA polymerases beta chain signature. GdKFASrHGQKGT source prosite : PS01166 61) chain C residue 2 type MOD_RES sequence S description N-acetylserine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI2 62) chain B residue 1163 type MOD_RES sequence C description N-acetylserine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI2 63) chain B residue 1166 type MOD_RES sequence C description N-acetylserine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI2 64) chain B residue 1182 type MOD_RES sequence C description N-acetylserine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI2 65) chain B residue 1185 type MOD_RES sequence C description N-acetylserine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI2 66) chain C residue 86 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 67) chain A residue 483 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI1 68) chain A residue 485 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI1 69) chain C residue 88 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 70) chain C residue 92 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 71) chain C residue 95 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 72) chain A residue 107 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 73) chain A residue 110 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 74) chain A residue 148 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 75) chain A residue 167 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI1 76) chain A residue 481 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI1 77) chain I residue 78 type CROSSLNK sequence C description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:32142654, ECO:0007744|PubMed:22106047 source Swiss-Prot : SWS_FT_FI4 78) chain I residue 103 type CROSSLNK sequence C description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:32142654, ECO:0007744|PubMed:22106047 source Swiss-Prot : SWS_FT_FI4 79) chain I residue 106 type CROSSLNK sequence C description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:32142654, ECO:0007744|PubMed:22106047 source Swiss-Prot : SWS_FT_FI4 80) chain B residue 919 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI3 81) chain I residue 10 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI3 82) chain A residue 1350 type MOD_RES sequence K description Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI3 83) chain I residue 32 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI3

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