eF-site ID 2e2h-ABCEFHIJKL PDB Code 2e2h Chain A, B, C, E, F, H, I, J, K, L Title RNA polymerase II elongation complex at 5 mM Mg2+ with GTP Classification TRANSCRIPTION,TRANSFERASE/DNA-RNA HYBRID Compound 5'-R(*AP*UP*CP*GP*AP*GP*AP*GP*GP*A)-3' Source ORGANISM_COMMON: baker's yeast; ORGANISM_SCIENTIFIC: Saccharomyces cerevisiae; Sequence A:  VGQQYSSAPLRTVKEVQFGLFSPEEVRAISVAKIRFPETM DETQTRAKIGGLNDPRLGSIDRNLKCQTCQEGMNECPGHF GHIDLAKPVFHVGFIAKIKKVCECVCMHCGKLLLDEHNEL MRQALAIKDSKKRFAAIWTLCKTKMVCETDVPSELVSRGG CGNTQPTIRKDGLKLVGSWLRVLSTEEILNIFKHISVKDF TSLGFNEVFSRPEWMILTCLPVPPPPVRPSISFNESQRGE DDLTFKLADILKANISLETLEHNGAPHHAIEEAESLLQFH VATYMDNDIAGQPQAGRPVKSIRARLKGKEGRIRGNLMGK RVDFSARTVISGDPNLELDQVGVPKSIAKTLTYPEVVTPY NIDRLTQLVRNGPNEHPGAKYVIRDSGDRIDLRYSKRAGD IQLQYGWKVERHIMDNDPVLFNRQPSLHKMSMMAHRVKVI PYSTFRLNLSVTSPYNADFDGDEMNLHVPQSEETRAELSQ LCAVPLQIVSPQSNKPCMGIVQDTLCGIRKLTLRDTFIEL DQVLNMLYWVPDWDGVIPTPAIIKPKPLWSGKQILSVAIP NGIHLQRFDEGTTLLSPKDNGMLIIDGQIIFGVVEKKTVG SSNGGLIHVVTREKGPQVCAKLFGNIQKVVNFWLLHNGFS TGIGDTIADGPTMREITETIAEAKKKVLDVTKEAQANLLT AKHGMTLRESFEDNVVRFLNEARDKAGRLAEVNLKDLNNV KQMVMAGSKGSFINIAQMSACVGQQSVEGKRIAFGFVDRT LPHFSKDDYSPESKGFVENSYLRGLTPQEFFFHAMGGREG LIDTAVKTAETGYIQRRLVKALEDIMVHYDNTTRNSLGNV IQFIYGEDGMDAAHIEKQSLDTIGGSDAAFEKRYRVDLLN TDHTLDPSLLESGSEILGDLKLQVLLDEEYKQLVKDRKFL REVFVDGEANWPLPVNIRRIIQNAQQTFHIDHTKPSDLTI KDIVLGVKDLQENLLVLRGKNEIIQNAQRDAVTLFCCLLR SRLATRRVLQEYRLTKQAFDWVLSNIEAQFLRSVVHPGEM VGVLAAQSIGEPATQMTLNTFHFAGVASKKVTSGVPRLKE ILNVAKNMKTPSLTVYLEPGHAADQEQAKLIRSAIEHTTL KSVTIASEIYYDPDPRSTVIPEDEEIIQLHFSLQQSPWLL RLELDRAAMNDKDLTMGQVGERIKQTFKNDLFVIWSEDLI IRCRVVAEEDHMLKKIENTMLENITLRGVENIERVVMMKY DRKVPSPTGEYVKEPEWVLETDGVNLSEVMTVPGIDPTRI YTNSFIDIMEVLGIEAGRAALYKEVYNVIASDGSYVNYRH MALLVDVMTTQGGLTSVTRHGFNRSNTGALMRCSFEETVE ILFEAGASAELDDCRGVSENVILGQMAPIGTGAFDVMI B:  DESAPITAEDSWAVISAFFREKGLVSQQLDSFNQFVDYTL QDIICEDSTLIISFGKIYVTKPMVNESDGVTHALYPQEAR LRNLTYSSGLFVDVKVFIGRLPIMLRSKNCYLSEATESDL YKLKECPFDMGGYFIINGSEKVLIAQERSAGNIVQVFKKA APSPISHVAEIRSALEKGSISTLQVKLYGREGSSARTIKA TLPYIKQDIPIVIIFRALGIIPDGEILEHICYDVNDWQML EMLKPCVEDGFVIQDRETALDFIGKEKRIQYAKDILQKEF LPHITQLEGFESRKAFFLGYMINRLLLCALDRKDQDDRDH FGKKRLDLAGPLLAQLFKTLFKKLTKDIFRYMQRTVELAI NAKTITSGLKYALATGNWGEQKKAMSSRAGVSQVLNRYTY SSTLSHLRRTNTPIAKPRQLHNTHWGLVCPAETPEGQACG LVKNLSLMSCISVGTDPMPIITFLSEWGMEPLEDYVPHQS PDATRVFVNGVWHGVHRNPARLMETLRTLRRKGDINPEVS MIRDIREKELKIFTDAGRVYRPLFIVEDDESLGHKELKVR KGHIAKLMATEYQDEYTWSSLLNEGLVEYIDAEEEESILI AMQPEDLEPAEDVDPAKRIRVSATTFTHCEIHPSMILGVA ASIIPFPDHNQSPRNTYQSAMGKQAMGVFLTNYNVRMDTM ANILYYPQKPLGTTRAMEYLKFRELPAGQNAIVAIACYSG YNQEDSMIMNQSSIDRGLFRSLFFRSYMDQEKKYGMSITE TFEKPQRTNTLRMKHGTYDKLDDDGLIAPGVRVSGEDVII GKTTPISRDASTPLRSTENGIVDQVLVTTNQDGLKFVKVR VRTTKIPQIGDKFASRHGQKGTIGITYRREDMPFTAEGIV PDLIINPHAIPSRMTVAHLIECLLSKVAALSGNEGDASPF TDITVEGISKLLREHGYQSRGFEVMYNGHTGKKLMAQIFF GPTYYQRLRHMVDDKIHARARGPMQVLTRQPVEGRSRDGG LRFGEMERDCMIAHGAASFLKERLMEASDAFRVHICGICG LMTVIAKLNHNQFECKGCDNKIDIYQIHIPYAAKLLFQEL MAMNITPRLYTDRSRD C:  EEGPQVKIREASKDNVDFILSNVDLAMANSLRRVMIAEIP TLAIDSVEVETNTTVLADEFIAHRLGLIPLQSMDIEQLEY SRDCFCEDHCDKCSVVLTLQAFGESESTTNVYSKDLVIVS NLMGRNIGHPIIQDKEGNGVLICKLRKGQELKLTCVAKKG IAKEHAKWGPAAAIEFEYDPWNKLKHTDYWYEQDSAKEWP QSKNCEYEDPPNEGDPFDYKAQADTFYMNVESVGSIPVDQ VVVRGIDTLQKKVASILLALTQMDQD E:  QENERNISRLWRAFRTVKEMVKDRGYFITQEEVELPLEDF KAKYCDRPQRKMMSFQANPTEESISKFPDMGSLWVEFTFV IHIQEKNFQTGIFVTPSAMKLVPSIPPATIETFNEAALVV NITHHELVPKHIRLSSDEKRELLKRYRLKESQLPRIQRAD PVALYLGLKRGEVVKIIRKSETSGRYASYRICM F:  KAIPKDQRATTPYMTKYERARILGTRALQISMNAPVFVDL EGETDPLRIAMKELAEKKIPLVIRRYLPDGSFEDWSVEEL IVD H:  SNTLFDDIFQVSEVDPGRYNKVCRIEAASTTQDQCKLTLD INVELFPVAAQDSLTVTIASSLTRSWRPPQAGDRSLADDY DYVMYGTAYKFEEVSKDLIAVYYSFGGLLMRLEGNYRNLN NLKQENAYLLIRR I:  TTFRFCRDCNNMLYPREDKENNRLLFECRTCSYVEEAGSP LVYRHELITNIGETAGVVQDIGSDPTLPRSDRECPKCHSR ENVFFQSQQRRKDTSMVLFFVCLSCSHIFTSDQKNKRTQ J:  MIVPVRCFSCGKVVGDKWESYLNLLQEDELDEGTALSRLG LKRYCCRRMILTHVDLIEKFLRYNP K:  MNAPDRFELFLLGEGESKLKIDPDTKAPNAVVITFEKEDH TLGNLIRAELLNDRKVLFAAYKVEHPFFARFKLRIQTTEG YDPKDALKNACNSIINKLGALKTNFETEWNLQTL L:  ATLKYICAECSSKLSLSRTDAVRCKDCGHRILLKARTKRL VQFEAR Description Functional site 1) chain A residue 108 type sequence M 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 167 type sequence C description BINDING SITE FOR RESIDUE ZN A 1734 source : AC1 4) chain A residue 67 type sequence C description BINDING SITE FOR RESIDUE ZN A 1735 source : AC2 5) chain A residue 70 type sequence C description BINDING SITE FOR RESIDUE ZN A 1735 source : AC2 6) chain A residue 77 type sequence C description BINDING SITE FOR RESIDUE ZN A 1735 source : AC2 7) chain A residue 80 type sequence H description BINDING SITE FOR RESIDUE ZN A 1735 source : AC2 8) chain B residue 1163 type sequence C description BINDING SITE FOR RESIDUE ZN B 1307 source : AC3 9) chain B residue 1166 type sequence C description BINDING SITE FOR RESIDUE ZN B 1307 source : AC3 10) chain B residue 1182 type sequence C description BINDING SITE FOR RESIDUE ZN B 1307 source : AC3 11) chain B residue 1185 type sequence C description BINDING SITE FOR RESIDUE ZN B 1307 source : AC3 12) chain C residue 86 type sequence C description BINDING SITE FOR RESIDUE ZN C 319 source : AC4 13) chain C residue 88 type sequence C description BINDING SITE FOR RESIDUE ZN C 319 source : AC4 14) chain C residue 92 type sequence C description BINDING SITE FOR RESIDUE ZN C 319 source : AC4 15) chain C residue 95 type sequence C description BINDING SITE FOR RESIDUE ZN C 319 source : AC4 16) chain I residue 10 type sequence C description BINDING SITE FOR RESIDUE ZN I 203 source : AC5 17) chain I residue 29 type sequence C description BINDING SITE FOR RESIDUE ZN I 203 source : AC5 18) chain I residue 30 type sequence R description BINDING SITE FOR RESIDUE ZN I 203 source : AC5 19) chain I residue 32 type sequence C description BINDING SITE FOR RESIDUE ZN I 203 source : AC5 20) chain I residue 75 type sequence C description BINDING SITE FOR RESIDUE ZN I 204 source : AC6 21) chain I residue 78 type sequence C description BINDING SITE FOR RESIDUE ZN I 204 source : AC6 22) chain I residue 80 type sequence S description BINDING SITE FOR RESIDUE ZN I 204 source : AC6 23) chain I residue 103 type sequence C description BINDING SITE FOR RESIDUE ZN I 204 source : AC6 24) chain I residue 106 type sequence C description BINDING SITE FOR RESIDUE ZN I 204 source : AC6 25) chain I residue 108 type sequence H 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 9 type sequence S description BINDING SITE FOR RESIDUE ZN J 101 source : AC7 28) chain J residue 10 type sequence C description BINDING SITE FOR RESIDUE ZN J 101 source : AC7 29) chain J residue 45 type sequence C description BINDING SITE FOR RESIDUE ZN J 101 source : AC7 30) chain J residue 46 type sequence C description BINDING SITE FOR RESIDUE ZN J 101 source : AC7 31) chain L residue 31 type sequence C description BINDING SITE FOR RESIDUE ZN L 105 source : AC8 32) chain L residue 33 type sequence E description BINDING SITE FOR RESIDUE ZN L 105 source : AC8 33) chain L residue 34 type sequence C description BINDING SITE FOR RESIDUE ZN L 105 source : AC8 34) chain L residue 48 type sequence C description BINDING SITE FOR RESIDUE ZN L 105 source : AC8 35) chain L residue 51 type sequence C description BINDING SITE FOR RESIDUE ZN L 105 source : AC8 36) chain A residue 481 type sequence D description BINDING SITE FOR RESIDUE MG A 2001 source : AC9 37) chain A residue 483 type sequence D description BINDING SITE FOR RESIDUE MG A 2001 source : AC9 38) chain A residue 485 type sequence D description BINDING SITE FOR RESIDUE MG A 2001 source : AC9 39) chain A residue 481 type sequence D description BINDING SITE FOR RESIDUE MG A 2002 source : BC1 40) chain A residue 483 type sequence D description BINDING SITE FOR RESIDUE MG A 2002 source : BC1 41) chain B residue 837 type sequence D description BINDING SITE FOR RESIDUE MG A 2002 source : BC1 42) chain B residue 1020 type sequence R description BINDING SITE FOR RESIDUE MG A 2002 source : BC1 43) chain A residue 448 type sequence P description BINDING SITE FOR RESIDUE GTP T 3000 source : BC2 44) chain A residue 481 type sequence D description BINDING SITE FOR RESIDUE GTP T 3000 source : BC2 45) chain A residue 483 type sequence D description BINDING SITE FOR RESIDUE GTP T 3000 source : BC2 46) chain A residue 485 type sequence D description BINDING SITE FOR RESIDUE GTP T 3000 source : BC2 47) chain A residue 827 type sequence T description BINDING SITE FOR RESIDUE GTP T 3000 source : BC2 48) chain A residue 1081 type sequence L description BINDING SITE FOR RESIDUE GTP T 3000 source : BC2 49) chain A residue 1085 type sequence H description BINDING SITE FOR RESIDUE GTP T 3000 source : BC2 50) chain B residue 766 type sequence R description BINDING SITE FOR RESIDUE GTP T 3000 source : BC2 51) chain B residue 987 type sequence K description BINDING SITE FOR RESIDUE GTP T 3000 source : BC2 52) chain B residue 1020 type sequence R description BINDING SITE FOR RESIDUE GTP T 3000 source : BC2 53) chain B residue 837 type catalytic sequence D description 788 source MCSA : MCSA1 54) chain A residue 483 type catalytic sequence D description 788 source MCSA : MCSA1 55) chain A residue 485 type catalytic sequence D description 788 source MCSA : MCSA1 56) chain A residue 1085 type catalytic sequence H description 788 source MCSA : MCSA1 57) chain I residue 7 type BINDING sequence C description BINDING => ECO:0000269|PubMed:11313498, ECO:0000269|PubMed:11805306, ECO:0000269|PubMed:15537538, ECO:0000305|PubMed:11313499 source Swiss-Prot : SWS_FT_FI3 58) chain I residue 10 type BINDING sequence C description BINDING => ECO:0000269|PubMed:11313498, ECO:0000269|PubMed:11805306, ECO:0000269|PubMed:15537538, ECO:0000305|PubMed:11313499 source Swiss-Prot : SWS_FT_FI3 59) chain I residue 29 type BINDING sequence C description BINDING => ECO:0000269|PubMed:11313498, ECO:0000269|PubMed:11805306, ECO:0000269|PubMed:15537538, ECO:0000305|PubMed:11313499 source Swiss-Prot : SWS_FT_FI3 60) chain I residue 32 type BINDING sequence C description BINDING => ECO:0000269|PubMed:11313498, ECO:0000269|PubMed:11805306, ECO:0000269|PubMed:15537538, ECO:0000305|PubMed:11313499 source Swiss-Prot : SWS_FT_FI3 61) chain I residue 75 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00472, ECO:0000269|PubMed:11313498, ECO:0000269|PubMed:11805306, ECO:0000269|PubMed:15537538, ECO:0000305|PubMed:11313499 source Swiss-Prot : SWS_FT_FI4 62) chain I residue 78 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00472, ECO:0000269|PubMed:11313498, ECO:0000269|PubMed:11805306, ECO:0000269|PubMed:15537538, ECO:0000305|PubMed:11313499 source Swiss-Prot : SWS_FT_FI4 63) chain I residue 103 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00472, ECO:0000269|PubMed:11313498, ECO:0000269|PubMed:11805306, ECO:0000269|PubMed:15537538, ECO:0000305|PubMed:11313499 source Swiss-Prot : SWS_FT_FI4 64) chain I residue 106 type BINDING sequence C description BINDING => ECO:0000255|PROSITE-ProRule:PRU00472, ECO:0000269|PubMed:11313498, ECO:0000269|PubMed:11805306, ECO:0000269|PubMed:15537538, ECO:0000305|PubMed:11313499 source Swiss-Prot : SWS_FT_FI4 65) chain L residue 31-51 type ZN_FING sequence CAECSSKLSLSRTDAVRCKDC description C4-type source Swiss-Prot : SWS_FT_FI1 66) chain A residue 483 type ZN_FING sequence D description C4-type source Swiss-Prot : SWS_FT_FI1 67) chain A residue 485 type ZN_FING sequence D description C4-type source Swiss-Prot : SWS_FT_FI1 68) chain J residue 10 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 69) chain J residue 45 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 70) chain J residue 46 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 71) chain A residue 107 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 72) chain A residue 110 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 73) chain A residue 148 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 74) chain A residue 167 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 75) chain A residue 481 type ZN_FING sequence D description C4-type source Swiss-Prot : SWS_FT_FI1 76) chain L residue 31 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI2 77) chain L residue 34 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI2 78) chain L residue 48 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI2 79) chain L residue 51 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI2 80) chain B residue 1185 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI2 81) chain I residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI5 82) 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 83) 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 84) chain I residue 75-110 type prosite sequence CPKCHSRENVFFQSQQRRKDTSMVLFFVCLSCSHIF description ZF_TFIIS_1 Zinc finger TFIIS-type signature. CpkChsrenvffqSQQRRkDTSmvlffvCls...CshiF source prosite : PS00466 85) 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 86) 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 87) 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 88) 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 89) chain B residue 977-989 type prosite sequence GDKFASRHGQKGT description RNA_POL_BETA RNA polymerases beta chain signature. GdKFASrHGQKGT source prosite : PS01166

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