eF-site ID 1twh-ABCEFHIJKL PDB Code 1twh Chain A, B, C, E, F, H, I, J, K, L Title RNA polymerase II complexed with 2'dATP Classification TRANSCRIPTION Compound DNA-directed RNA polymerase II largest subunit Source ORGANISM_COMMON: baker's yeast; ORGANISM_SCIENTIFIC: Saccharomyces cerevisiae; Sequence A:  GQQYSSAPLRTVKEVQFGLFSPEEVRAISVAKIRFPETMD ETQTRAKIGGLNDPRLGSIDRNLKCQTCQEGMNECPGHFG HIDLAKPVFHVGFIAKIKKVCECVCMHCGKLLLDEHNELM RQALAIKDSKKRFAAIWTLCKTKMVCETDVPSEDDPTQLV SRGGCGNTQPTIRKDGLKLVGSWKKDRATGDADEPELRVL STEEILNIFKHISVKDFTSLGFNEVFSRPEWMILTCLPVP PPPVRPDLTFKLADILKANISLETLEHNGAPHHAIEEAES LLQFHVATYMDSIRADFSARTVISGDPNLELDQVGVPKSI AKTLTYPEVVTPYNIDRLTQLVRNGPNEHPGAKYVIRDSG DRIDLRYSKRAGDIQLQYGWKVERHIMDNDPVLFNRQPSL HKMSMMAHRVKVIPYSTFRLNLSVTSPYNADFDGDEMNLH VPQSEETRAELSQLCAVPLQIVSPQSNKPCMGIVQDTLCG IRKLTLRDTFIELDQVLNMLYWVPDWDGVIPTPAIIKPKP LWSGKQILSVAIPNGIHLQRFDEGTTLLSPKDNGMLIIDG QIIFGVVEKKTVGSSNGGLIHVVTREKGPQVCAKLFGNIQ KVVNFWLLHNGFSTGIGDTIADGPTMREITETIAEAKKKV LDVTKEAQANLLTAKHGMTLRESFEDNVVRFLNEARDKAG RLAEVNLKDLNNVKQMVMAGSKGSFINIAQMSACVGQQSV EGKRIAFGFVDRTLPHFSKDDYSPESKGFVENSYLRGLTP QEFFFHAMGGREGLIDTAVKTAETGYIQRRLVKALEDIMV HYDNTTRNSLGNVIQFIYGEDGMDAAHIEKQSLDTIGGSD AAFEKRYRVDLLNTDHTLDPSLLESGSEILGDLKLQVLLD EEYKQLVKDRKFLREVFVDGEANWPLPVNIRRIIQNAQQT FHIDHTKPSDLTIKDIVLGVKDLQENLLVLRGKNEIIQNA QRDAVTLFCCLLRSRLATRRVLQEYRLTKQAFDWVLSNIE AQFLRSVVHPGEMVGVLAAQSIGEPATQMTLKKVTSGVPR LKEILNVAKNMKTPSLTVYLEPGHAADQEQAKLIRSAIEH TTLKSVTIASEIYYDPDPRSTVIPEDEEIIQLHLQQSPWL LRLELDRAAMNDKDLTMGQVGERIKQTFKNDLFVIWSEDN DEKLIIRCRVVAEEDHMLKKIENTMLENITLRGVENIERV VMMKYDRKVPSPTGEYVKEPEWVLETDGVNLSEVMTVPGI DPTRIYTNSFIDIMEVLGIEAGRAALYKEVYNVIASDGSY VNYRHMALLVDVMTTQGGLTSVTTVEILFEAGASAELDDC RGVSENVILGQMAPIGTGAFDVMIDEESL B:  FEDESAPITAEDSWAVISAFFREKGLVSQQLDSFNQFVDY TLQDIICEDSTLIEISFGKIYVTKPMVNESDGVTHALYPQ EARLRNLTYSSGLFVDVKKRTYEKVFIGRLPIMLRSKNCY LSEATESDLYKLKECPFDMGGYFIINGSEKVLIAQERSAG NIVQVFKKAAPSPISHVAEIRSALEKGSRFISTLQVKLYG REGSSARTIKATLPYIKQDIPIVIIFRALGIIPDGEILEH ICYDVNDWQMLEMLKPCVEDGFVIQDRETALDFIGRRGTA LGIKKEKRIQYAKDILQKEFLPHITQLEGFESRKAFFLGY MINRLLLCALDRKDQDDRDHFGKKRLDLAGPLLAQLFKTL FKKLTKDIFRYMQRTVELAINAKTITSGLKYALATGNWGA GVSQVLNRYTYSSTLSHLRRTNTPIAKPRQLHNTHWGLVC PAETPEGQACGLVKNLSLMSCISVGTDPMPIITFLSEWGM EPLEDYVPHQSPDATRVFVNGVWHGVHRNPARLMETLRTL RRKGDINPEVSMIRDIREKELKIFTDAGRVYRPLFIVEDD ESLGHKELKVRKGHIAKLMATEYQDEYTWSSLLNEGLVEY IDAEEEESILIAMQPEDLEPDVDPAKRIRVSHHATTFTHC EIHPSMILGVAASIIPFPDHNQSPRNTYQSAMGKQAMGVF LTNYNVRMDTMANILYYPQKPLGTTRAMEYLKFRELPAGQ NAIVAIACYSGYNQEDSMIMNQSSIDRGLFRSLFFRSYMD QEKKYGMSITETFEKPQRTNTLRMKHGTYDKLDDDGLIAP GVRVSGEDVIIGKTTSKRDASTPLRSTENGIVDQVLVTTN QDGLKFVKVRVRTTKIPQIGDKFASRHGQKGTIGITYRRE DMPFTAEGIVPDLIINPHAIPSRMTVAHLIECLLSKVAAL SGNEGDASPFTDITVEGISKLLREHGYQSRGFEVMYNGHT GKKLMAQIFFGPTYYQRLRHMVDDKIHARARGPGLRFGEM ERDCMIAHGAASFLKERLMEASDAFRVHICGICGLMTVIA KLNHNQFECKGCDNKIDIYQIHIPYAAKLLFQELMAMNIT PRLYTDRSRDF C:  EEGPQVKIREASKDNVDFILSNVDLAMANSLRRVMIAEIP TLAIDSVEVETNTTVLADEFIAHRLGLIPLQSMDIEQLEY SRDCFCEDHCDKCSVVLTLQAFGESESTTNVYSKDLVIVS NLMGRNIGHPIIQDKEGNGVLICKLRKGQELKLTCVAKKG IAKEHAKWGPAAAIEFEYDPWNKLKHTDYWYEQDSAKEWP QSKNCEYEDPPNEGDPFDYKAQADTFYMNVESVGSIPVDQ VVVRGIDTLQKKVASILLALTQMDQD E:  MDQENERNISRLWRAFRTVKEMVKDRGYFITQEEVELPLE DFKAKYCDSMGRPQRKMMSFQANPTEESISKFPDMGSLWV EFCDEPSVGVKTMKTFVIHIQEKNFQTGIFVYQNNITPSA MKLVPSIPPATIETFNEAALVVNITHHELVPKHIRLSSDE KRELLKRYRLKESQLPRIQRADPVALYLGLKRGEVVKIIR KSETSGRYASYRICM F:  KAIPKDQRATTPYMTKYERARILGTRALQISMNAPVFVDL EGETDPLRIAMKELAEKKIPLVIRRYLPDGSFEDWSVEEL IVD H:  SNTLFDDIFQVSEVDPGRYNKVCRIEAASTTQDQCKLTLD INVELFPVAAQDSLTVTIASSLTRSWRPPQAGDRSLADDY DYVMYGTAYKFEEVSKDLIAVYYSFGGLLMRLEGNYRNLN NLKQENAYLLIRR I:  MTTFRFCRDCNNMLYPREDKENNRLLFECRTCSYVEEAGS PLVYRHELITNIGETAGVVQDIGSDPTLPRSDRECPKCHS RENVFFQSQQRRKDTSMVLFFVCLSCSHIFTSDQKNKRTQ F J:  MIVPVRCFSCGKVVGDKWESYLNLLQEDELDEGTALSRLG LKRYCCRRMILTHVDLIEKFLRYN K:  MNAPDRFELFLLGEGESKLKIDPDTKAPNAVVITFEKEDH TLGNLIRAELLNDRKVLFAAYKVEHPFFARFKLRIQTTEG YDPKDALKNACNSIINKLGALKTNFETEWNLQTL L:  ATLKYICAECSSKLSLSRTDAVRCKDCGHRILLKARTKRL VQFEAR Description Functional site 1) chain A residue 481 type sequence D description BINDING SITE FOR RESIDUE MN A 3009 source : AC1 2) chain A residue 483 type sequence D description BINDING SITE FOR RESIDUE MN A 3009 source : AC1 3) chain A residue 485 type sequence D description BINDING SITE FOR RESIDUE MN A 3009 source : AC1 4) chain A residue 481 type sequence D description BINDING SITE FOR RESIDUE MN A 3010 source : AC2 5) chain A residue 483 type sequence D description BINDING SITE FOR RESIDUE MN A 3010 source : AC2 6) chain B residue 837 type sequence D description BINDING SITE FOR RESIDUE MN A 3010 source : AC2 7) chain J residue 7 type sequence C description BINDING SITE FOR RESIDUE ZN J 3001 source : AC3 8) chain J residue 10 type sequence C description BINDING SITE FOR RESIDUE ZN J 3001 source : AC3 9) chain J residue 45 type sequence C description BINDING SITE FOR RESIDUE ZN J 3001 source : AC3 10) chain J residue 46 type sequence C description BINDING SITE FOR RESIDUE ZN J 3001 source : AC3 11) chain C residue 86 type sequence C description BINDING SITE FOR RESIDUE ZN C 3002 source : AC4 12) chain C residue 88 type sequence C description BINDING SITE FOR RESIDUE ZN C 3002 source : AC4 13) chain C residue 92 type sequence C description BINDING SITE FOR RESIDUE ZN C 3002 source : AC4 14) chain C residue 95 type sequence C description BINDING SITE FOR RESIDUE ZN C 3002 source : AC4 15) chain I residue 7 type sequence C description BINDING SITE FOR RESIDUE ZN I 3003 source : AC5 16) chain I residue 10 type sequence C description BINDING SITE FOR RESIDUE ZN I 3003 source : AC5 17) chain I residue 29 type sequence C description BINDING SITE FOR RESIDUE ZN I 3003 source : AC5 18) chain I residue 32 type sequence C description BINDING SITE FOR RESIDUE ZN I 3003 source : AC5 19) chain I residue 75 type sequence C description BINDING SITE FOR RESIDUE ZN I 3004 source : AC6 20) chain I residue 78 type sequence C description BINDING SITE FOR RESIDUE ZN I 3004 source : AC6 21) chain I residue 103 type sequence C description BINDING SITE FOR RESIDUE ZN I 3004 source : AC6 22) chain I residue 106 type sequence C description BINDING SITE FOR RESIDUE ZN I 3004 source : AC6 23) chain L residue 31 type sequence C description BINDING SITE FOR RESIDUE ZN L 3005 source : AC7 24) chain L residue 34 type sequence C description BINDING SITE FOR RESIDUE ZN L 3005 source : AC7 25) chain L residue 36 type sequence S description BINDING SITE FOR RESIDUE ZN L 3005 source : AC7 26) chain L residue 48 type sequence C description BINDING SITE FOR RESIDUE ZN L 3005 source : AC7 27) chain L residue 51 type sequence C description BINDING SITE FOR RESIDUE ZN L 3005 source : AC7 28) chain A residue 107 type sequence C description BINDING SITE FOR RESIDUE ZN A 3006 source : AC8 29) chain A residue 110 type sequence C description BINDING SITE FOR RESIDUE ZN A 3006 source : AC8 30) chain A residue 148 type sequence C description BINDING SITE FOR RESIDUE ZN A 3006 source : AC8 31) chain A residue 166 type sequence G description BINDING SITE FOR RESIDUE ZN A 3006 source : AC8 32) chain A residue 167 type sequence C description BINDING SITE FOR RESIDUE ZN A 3006 source : AC8 33) chain B residue 1163 type sequence C description BINDING SITE FOR RESIDUE ZN B 3007 source : AC9 34) chain B residue 1166 type sequence C description BINDING SITE FOR RESIDUE ZN B 3007 source : AC9 35) chain B residue 1182 type sequence C description BINDING SITE FOR RESIDUE ZN B 3007 source : AC9 36) chain B residue 1185 type sequence C description BINDING SITE FOR RESIDUE ZN B 3007 source : AC9 37) chain A residue 67 type sequence C description BINDING SITE FOR RESIDUE ZN A 3008 source : BC1 38) chain A residue 70 type sequence C description BINDING SITE FOR RESIDUE ZN A 3008 source : BC1 39) chain A residue 77 type sequence C description BINDING SITE FOR RESIDUE ZN A 3008 source : BC1 40) chain A residue 80 type sequence H description BINDING SITE FOR RESIDUE ZN A 3008 source : BC1 41) chain A residue 481 type sequence D description BINDING SITE FOR RESIDUE ATP A 3011 source : BC2 42) chain A residue 483 type sequence D description BINDING SITE FOR RESIDUE ATP A 3011 source : BC2 43) chain A residue 485 type sequence D description BINDING SITE FOR RESIDUE ATP A 3011 source : BC2 44) chain B residue 766 type sequence R description BINDING SITE FOR RESIDUE ATP A 3011 source : BC2 45) chain B residue 986 type sequence Q description BINDING SITE FOR RESIDUE ATP A 3011 source : BC2 46) chain B residue 987 type sequence K description BINDING SITE FOR RESIDUE ATP A 3011 source : BC2 47) chain B residue 1020 type sequence R description BINDING SITE FOR RESIDUE ATP A 3011 source : BC2 48) chain B residue 837 type catalytic sequence D description 788 source MCSA : MCSA1 49) chain A residue 483 type catalytic sequence D description 788 source MCSA : MCSA1 50) chain A residue 485 type catalytic sequence D description 788 source MCSA : MCSA1 51) chain I residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI5 52) 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 53) 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 54) chain I residue 75-110 type prosite sequence CPKCHSRENVFFQSQQRRKDTSMVLFFVCLSCSHIF description ZF_TFIIS_1 Zinc finger TFIIS-type signature. CpkChsrenvffqSQQRRkDTSmvlffvCls...CshiF source prosite : PS00466 55) 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 56) 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 57) 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 58) 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 59) chain B residue 977-989 type prosite sequence GDKFASRHGQKGT description RNA_POL_BETA RNA polymerases beta chain signature. GdKFASrHGQKGT source prosite : PS01166 60) chain L residue 31-51 type ZN_FING sequence CAECSSKLSLSRTDAVRCKDC description C4-type source Swiss-Prot : SWS_FT_FI1 61) chain A residue 483 type ZN_FING sequence D description C4-type source Swiss-Prot : SWS_FT_FI1 62) chain A residue 485 type ZN_FING sequence D description C4-type source Swiss-Prot : SWS_FT_FI1 63) chain J residue 10 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 64) chain J residue 45 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 65) chain J residue 46 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 66) chain A residue 107 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 67) chain A residue 110 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 68) chain A residue 148 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 69) chain A residue 167 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 70) chain A residue 481 type ZN_FING sequence D description C4-type source Swiss-Prot : SWS_FT_FI1 71) chain L residue 31 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI2 72) chain L residue 34 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI2 73) chain L residue 48 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI2 74) chain L residue 51 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI2 75) chain B residue 1185 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI2 76) 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 77) 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 78) 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 79) 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 80) 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 81) 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 82) 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 83) 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

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