eF-site ID 1i50-ABCEFHIJKL PDB Code 1i50 Chain A, B, C, E, F, H, I, J, K, L Title RNA POLYMERASE II CRYSTAL FORM II AT 2.8 A RESOLUTION Classification TRANSCRIPTION Compound DNA-DIRECTED RNA POLYMERASE II LARGEST SUBUNIT Source ORGANISM_COMMON: baker's yeast; ORGANISM_SCIENTIFIC: Saccharomyces cerevisiae; Sequence A:  VGQQYSSAPLRTVKEVQFGLFSPEEVRAISVAKIRFPETM DETQTRAKIGGLNDPRLGSIDRNLKCQTCQEGMNECPGHF GHIDLAKPVFHVGFIAKIKKVCECVCMHCGKLLLDEHNEL MRQALAIKDSKKRFAAIWTLCKTKMVCETDVPSEDDPTQL VSRGGCGNTQPTIRKDGLKLVGSWKKDRATGDADEPELRV LSTEEILNIFKHISVKDFTSLGFNEVFSRPEWMILTCLPV PPPPVRPSISFNESQRGEDDLTFKLADILKANISLETLEH NGAPHHAIEEAESLLQFHVATYMDNDIAGQPQALQKSGRP VKSIRARLKGKEGRIRGNLMGKRVDFSARTVISGDPNLEL DQVGVPKSIAKTLTYPEVVTPYNIDRLTQLVRNGPNEHPG AKYVIRDSGDRIDLRYSKRAGDIQLQYGWKVERHIMDNDP VLFNRQPSLHKMSMMAHRVKVIPYSTFRLNLSVTSPYNAD FDGDEMNLHVPQSEETRAELSQLCAVPLQIVSPQSNKPCM GIVQDTLCGIRKLTLRDTFIELDQVLNMLYWVPDWDGVIP TPAIIKPKPLWSGKQILSVAIPNGIHLQRFDEGTTLLSPK DNGMLIIDGQIIFGVVEKKTVGSSNGGLIHVVTREKGPQV CAKLFGNIQKVVNFWLLHNGFSTGIGDTIADGPTMREITE TIAEAKKKVLDVTKEAQANLLTAKHGMTLRESFEDNVVRF LNEARDKAGRLAEVNLKDLNNVKQMVMAGSKGSFINIAQM SACVGQQSVEGKRIAFGFVDRTLPHFSKDDYSPESKGFVE NSYLRGLTPQEFFFHAMGGREGLIDTAVKTAETGYIQRRL VKALEDIMVHYDNTTRNSLGNVIQFIYGEDGMDAAHIEKQ SLDTIGGSDAAFEKRYRVDLLNTDHTLDPSLLESGSEILG DLKLQVLLDEEYKQLVKDRKFLREVFVDGEANWPLPVNIR RIIQNAQQTFHIDHTKPSDLTIKDIVLGVKDLQENLLVLR GKNEIIQNAQRDAVTLFCCLLRSRLATRRVLQEYRLTKQA FDWVLSNIEAQFLRSVVHPGEMVGVLAAQSIGEPATQMTL KKVTSGVPRLKEILNVAKNMKTPSLTVYLEPGHAADQEQA KLIRSAIEHTTLKSVTIASEIYYDPDPRSTVIPEDEEIIQ LHFSLQQSPWLLRLELDRAAMNDKDLTMGQVGERIKQTFK NDLFVIWSEDNDEKLIIRCRVVAEEDHMLKKIENTMLENI TLRGVENIERVVMMKYDRKVPSPTGEYVKEPEWVLETDGV NLSEVMTVPGIDPTRIYTNSFIDIMEVLGIEAGRAALYKE VYNVIASDGSYVNYRHMALLVDVMTTQGGLTSVTRHGFNR SNTGALMRCSFEETVEILFEAGASAELDDCRGVSENVILG QMAPIGTGAFDVMIDEESL B:  FEDESAPITAEDSWAVISAFFREKGLVSQQLDSFNQFVDY TLQDIICEDSTLIEISFGKIYVTKPMVNESDGVTHALYPQ EARLRNLTYSSGLFVDVKKRTYEKVFIGRLPIMLRSKNCY LSEATESDLYKLKECPFDMGGYFIINGSEKVLIAQERSAG NIVQVFKKAAPSPISHVAEIRSALEKGSRFISTLQVKLYG REGSSARTIKATLPYIKQDIPIVIIFRALGIIPDGEILEH ICYDVNDWQMLEMLKPCVEDGFVIQDRETALDFIGRRGTA LGIKKEKRIQYAKDILQKEFLPHITQLEGFESRKAFFLGY MINRLLLCALDRKDQDDRDHFGKKRLDLAGPLLAQLFKTL FKKLTKDIFRYMQRTVELAINAKTITSGLKYALATGNWGA GVSQVLNRYTYSSTLSHLRRTNTPIAKPRQLHNTHWGLVC PAETPEGQACGLVKNLSLMSCISVGTDPMPIITFLSEWGM EPLEDYVPHQSPDATRVFVNGVWHGVHRNPARLMETLRTL RRKGDINPEVSMIRDIREKELKIFTDAGRVYRPLFIVEDD ESLGHKELKVRKGHIAKLMATEYQDEYTWSSLLNEGLVEY IDAEEEESILIAMQPEDLEPDVDPAKRIRVSHHATTFTHC EIHPSMILGVAASIIPFPDHNQSPRNTYQSAMGKQAMGVF LTNYNVRMDTMANILYYPQKPLGTTRAMEYLKFRELPAGQ NAIVAIACYSGYNQEDSMIMNQSSIDRGLFRSLFFRSYMD QEKKYGMSITETFEKPQRTNTLRMKHGTYDKLDDDGLIAP GVRVSGEDVIIGKTTPISSKRDASTPLRSTENGIVDQVLV TTNQDGLKFVKVRVRTTKIPQIGDKFASRHGQKGTIGITY RREDMPFTAEGIVPDLIINPHAIPSRMTVAHLIECLLSKV AALSGNEGDASPFTDITVEGISKLLREHGYQSRGFEVMYN GHTGKKLMAQIFFGPTYYQRLRHMVDDKIHARARGPGLRF GEMERDCMIAHGAASFLKERLMEASDAFRVHICGICGLMT VIAKLNHNQFECKGCDNKIDIYQIHIPYAAKLLFQELMAM NITPRLYTDRSRDF C:  EEGPQVKIREASKDNVDFILSNVDLAMANSLRRVMIAEIP TLAIDSVEVETNTTVLADEFIAHRLGLIPLQSMDIEQLEY SRDCFCEDHCDKCSVVLTLQAFGESESTTNVYSKDLVIVS NLMGRNIGHPIIQDKEGNGVLICKLRKGQELKLTCVAKKG IAKEHAKWGPAAAIEFEYDPWNKLKHTDYWYEQDSAKEWP QSKNCEYEDPPNEGDPFDYKAQADTFYMNVESVGSIPVDQ VVVRGIDTLQKKVASILLALTQMDQD E:  MDQENERNISRLWRAFRTVKEMVKDRGYFITQEEVELPLE DFKAKYCDSMGRPQRKMMSFQANPTEESISKFPDMGSLWV EFCDEPSVGVKTMKTFVIHIQEKNFQTGIFVYQNNITPSA MKLVPSIPPATIETFNEAALVVNITHHELVPKHIRLSSDE KRELLKRYRLKESQLPRIQRADPVALYLGLKRGEVVKIIR KSETSGRYASYRICM F:  KAIPKDQRATTPYMTKYERARILGTRALQISMNAPVFVDL EGETDPLRIAMKELAEKKIPLVIRRYLPDGSFEDWSVEEL IVDL H:  SNTLFDDIFQVSEVDPGRYNKVCRIEAASTTQDQCKLTLD INVELFPVAAQDSLTVTIASSLTRSWRPPQAGDRSLADDY DYVMYGTAYKFEEVSKDLIAVYYSFGGLLMRLEGNYRNLN NLKQENAYLLIRR I:  MTTFRFCRDCNNMLYPREDKENNRLLFECRTCSYVEEAGS PLVYRHELITNIGETAGVVQDIGSDPTLPRSDRECPKCHS RENVFFQSQQRRKDTSMVLFFVCLSCSHIFTSDQKNKRTQ FS J:  MIVPVRCFSCGKVVGDKWESYLNLLQEDELDEGTALSRLG LKRYCCRRMILTHVDLIEKFLRYNP K:  MNAPDRFELFLLGEGESKLKIDPDTKAPNAVVITFEKEDH TLGNLIRAELLNDRKVLFAAYKVEHPFFARFKLRIQTTEG YDPKDALKNACNSIINKLGALKTNFETEWNLQTL L:  ATLKYICAECSSKLSLSRTDAVRCKDCGHRILLKARTKRL VQFEAR Description Functional site 1) chain J residue 7 type sequence C description BINDING SITE FOR RESIDUE ZN J 3001 source : AC1 2) chain J residue 10 type sequence C description BINDING SITE FOR RESIDUE ZN J 3001 source : AC1 3) chain J residue 45 type sequence C description BINDING SITE FOR RESIDUE ZN J 3001 source : AC1 4) chain J residue 46 type sequence C description BINDING SITE FOR RESIDUE ZN J 3001 source : AC1 5) chain C residue 86 type sequence C description BINDING SITE FOR RESIDUE ZN C 3002 source : AC2 6) chain C residue 88 type sequence C description BINDING SITE FOR RESIDUE ZN C 3002 source : AC2 7) chain C residue 92 type sequence C description BINDING SITE FOR RESIDUE ZN C 3002 source : AC2 8) chain C residue 95 type sequence C description BINDING SITE FOR RESIDUE ZN C 3002 source : AC2 9) chain I residue 7 type sequence C description BINDING SITE FOR RESIDUE ZN I 3003 source : AC3 10) chain I residue 10 type sequence C description BINDING SITE FOR RESIDUE ZN I 3003 source : AC3 11) chain I residue 29 type sequence C description BINDING SITE FOR RESIDUE ZN I 3003 source : AC3 12) chain I residue 32 type sequence C description BINDING SITE FOR RESIDUE ZN I 3003 source : AC3 13) chain I residue 75 type sequence C description BINDING SITE FOR RESIDUE ZN I 3004 source : AC4 14) chain I residue 78 type sequence C description BINDING SITE FOR RESIDUE ZN I 3004 source : AC4 15) chain I residue 103 type sequence C description BINDING SITE FOR RESIDUE ZN I 3004 source : AC4 16) chain I residue 106 type sequence C description BINDING SITE FOR RESIDUE ZN I 3004 source : AC4 17) chain L residue 31 type sequence C description BINDING SITE FOR RESIDUE ZN L 3005 source : AC5 18) chain L residue 34 type sequence C description BINDING SITE FOR RESIDUE ZN L 3005 source : AC5 19) chain L residue 48 type sequence C description BINDING SITE FOR RESIDUE ZN L 3005 source : AC5 20) chain L residue 51 type sequence C description BINDING SITE FOR RESIDUE ZN L 3005 source : AC5 21) chain A residue 107 type sequence C description BINDING SITE FOR RESIDUE ZN A 3006 source : AC6 22) chain A residue 110 type sequence C description BINDING SITE FOR RESIDUE ZN A 3006 source : AC6 23) chain A residue 148 type sequence C description BINDING SITE FOR RESIDUE ZN A 3006 source : AC6 24) chain A residue 167 type sequence C description BINDING SITE FOR RESIDUE ZN A 3006 source : AC6 25) chain B residue 1163 type sequence C description BINDING SITE FOR RESIDUE ZN B 3007 source : AC7 26) chain B residue 1166 type sequence C description BINDING SITE FOR RESIDUE ZN B 3007 source : AC7 27) chain B residue 1182 type sequence C description BINDING SITE FOR RESIDUE ZN B 3007 source : AC7 28) chain B residue 1185 type sequence C description BINDING SITE FOR RESIDUE ZN B 3007 source : AC7 29) chain A residue 67 type sequence C description BINDING SITE FOR RESIDUE ZN A 3008 source : AC8 30) chain A residue 70 type sequence C description BINDING SITE FOR RESIDUE ZN A 3008 source : AC8 31) chain A residue 77 type sequence C description BINDING SITE FOR RESIDUE ZN A 3008 source : AC8 32) chain A residue 80 type sequence H description BINDING SITE FOR RESIDUE ZN A 3008 source : AC8 33) chain A residue 481 type sequence D description BINDING SITE FOR RESIDUE MN A 3009 source : AC9 34) chain A residue 483 type sequence D description BINDING SITE FOR RESIDUE MN A 3009 source : AC9 35) chain A residue 485 type sequence D description BINDING SITE FOR RESIDUE MN A 3009 source : AC9 36) 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 37) chain B residue 837 type catalytic sequence D description 788 source MCSA : MCSA1 38) chain A residue 483 type catalytic sequence D description 788 source MCSA : MCSA1 39) chain A residue 485 type catalytic sequence D description 788 source MCSA : MCSA1 40) 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 41) 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 42) 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 43) 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 44) 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 45) 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 46) 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 47) 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 48) chain I residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI5 49) chain B residue 977-989 type prosite sequence GDKFASRHGQKGT description RNA_POL_BETA RNA polymerases beta chain signature. GdKFASrHGQKGT source prosite : PS01166 50) 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 51) 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 52) 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 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 L residue 31-51 type ZN_FING sequence CAECSSKLSLSRTDAVRCKDC description C4-type source Swiss-Prot : SWS_FT_FI1 57) chain J residue 46 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 58) chain A residue 483 type ZN_FING sequence D description C4-type source Swiss-Prot : SWS_FT_FI1 59) chain A residue 485 type ZN_FING sequence D description C4-type source Swiss-Prot : SWS_FT_FI1 60) chain A residue 107 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 61) chain A residue 110 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 62) chain A residue 148 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 63) chain A residue 167 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 64) chain A residue 481 type ZN_FING sequence D description C4-type source Swiss-Prot : SWS_FT_FI1 65) chain J residue 10 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 66) chain J residue 45 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 67) chain L residue 34 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI2 68) chain L residue 48 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI2 69) chain L residue 51 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI2 70) chain B residue 1185 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI2 71) chain L residue 31 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI2

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