eF-site ID 2ja6-ABCDEFGHIJKL PDB Code 2ja6 Chain A, B, C, D, E, F, G, H, I, J, K, L click to enlarge Title CPD lesion containing RNA Polymerase II elongation complex B Classification TRANSFERASE Compound DNA-DIRECTED RNA POLYMERASE II LARGEST SUBUNIT Source ORGANISM_COMMON: BAKERS' YEAST; ORGANISM_SCIENTIFIC: Saccharomyces cerevisiae; Sequence A:  VGQQYSSAPLRTVKEVQFGLFSPEEVRAISVAKIRFPETM DETQTRAKIGGLNDPRLGSIDRNLKCQTCQEGMNECPGHF GHIDLAKPVFHVGFIAKIKKVCECVCMHCGKLLLDEHNEL MRQALAIKDSKKRFAAIWTLCKTKMVCETDVPSEDDPTQL VSRGGCGNTQPTIRKDGLKLVGSWKKDRDEPELRVLSTEE ILNIFKHISVKDFTSLGFNEVFSRPEWMILTCLPVPPPPV RPSISFNESQRGEDDLTFKLADILKANISLETLEHNGAPH HAIEEAESLLQFHVATYMDNDIAGQPQALQKSGRPVKSIR ARLKGKEGRIRGNLMGKRVDFSARTVISGDPNLELDQVGV PKSIAKTLTYPEVVTPYNIDRLTQLVRNGPNEHPGAKYVI RDSGDRIDLRYSKRAGDIQLQYGWKVERHIMDNDPVLFNR QPSLHKMSMMAHRVKVIPYSTFRLNLSVTSPYNADFDGDE MNLHVPQSEETRAELSQLCAVPLQIVSPQSNKPCMGIVQD TLCGIRKLTLRDTFIELDQVLNMLYWVPDWDGVIPTPAII KPKPLWSGKQILSVAIPNGIHLQRFDEGTTLLSPKDNGML IIDGQIIFGVVEKKTVGSSNGGLIHVVTREKGPQVCAKLF GNIQKVVNFWLLHNGFSTGIGDTIADGPTMREITETIAEA KKKVLDVTKEAQANLLTAKHGMTLRESFEDNVVRFLNEAR DKAGRLAEVNLKDLNNVKQMVMAGSKGSFINIAQMSACVG QQSVEGKRIAFGFVDRTLPHFSKDDYSPESKGFVENSYLR GLTPQEFFFHAMGGREGLIDTAVKTAETGYIQRRLVKALE DIMVHYDNTTRNSLGNVIQFIYGEDGMDAAHIEKQSLDTI GGSDAAFEKRYRVDLLNTDHTLDPSLLESGSEILGDLKLQ VLLDEEYKQLVKDRKFLREVFVDGEANWPLPVNIRRIIQN AQQTFHIDHTKPSDLTIKDIVLGVKDLQENLLVLRGKNEI IQNAQRDAVTLFCCLLRSRLATRRVLQEYRLTKQAFDWVL SNIEAQFLRSVVHPGEMVGVLAAQSIGEPATQMTLKKVTS GVPRLKEILNVAKNMKTPSLTVYLEPGHAADQEQAKLIRS AIEHTTLKSVTIASEIYYDPDPRSTVIPEDEEIIQLHFSL QQSPWLLRLELDRAAMNDKDLTMGQVGERIKQTFKNDLFV IWSEDNDEKLIIRCRVVRPAEEDHMLKKIENTMLENITLR GVENIERVVMMKYDRKVPSPTGEYVKEPEWVLETDGVNLS EVMTVPGIDPTRIYTNSFIDIMEVLGIEAGRAALYKEVYN VIASDGSYVNYRHMALLVDVMTTQGGLTSVTRHGFNRSNT GALMRCSFEETVEILFEAGASAELDDCRGVSENVILGQMA PIGTGAFDVMIDEESLVKYMP B:  FEDESAPITAEDSWAVISAFFREKGLVSQQLDSFNQFVDY TLQDIICEDSTLIISFGKIYVTKPMVNESDGVTHALYPQE ARLRNLTYSSGLFVDVKKVFIGRLPIMLRSKNCYLSEATE SDLYKLKECPFDMGGYFIINGSEKVLIAQERSAGNIVQVF KKAAPSPISHVAEIRSALEKGSRFISTLQVKLYGREGSSA RTIKATLPYIKQDIPIVIIFRALGIIPDGEILEHICYDVN DWQMLEMLKPCVEDGFVIQDRETALDFIGRRGTALGIKKE KRIQYAKDILQKEFLPHITQLEGFESRKAFFLGYMINRLL LCALDRKDQDDRDHFGKKRLDLAGPLLAQLFKTLFKKLTK DIFRYMQRTVELAINAKTITSGLKYALATGNWGEQKKAMS SRAGVSQVLNRYTYSSTLSHLRRTNTPIKPRQLHNTHWGL VCPAETPEGQACGLVKNLSLMSCISVGTDPMPIITFLSEW GMEPLEDYVPHQSPDATRVFVNGVWHGVHRNPARLMETLR TLRRKGDINPEVSMIRDIREKELKIFTDAGRVYRPLFIVE DDESLGHKELKVRKGHIAKLMATEYQDEYTWSSLLNEGLV EYIDAEEEESILIAMQPEDLEPAEADVDPAKRIRVSHHAT TFTHCEIHPSMILGVAASIIPFPDHNQSPRNTYQSAMGKQ AMGVFLTNYNVRMDTMANILYYPQKPLGTTRAMEYLKFRE LPAGQNAIVAIACYSGYNQEDSMIMNQSSIDRGLFRSLFF RSYMDQEKKYGMSITETFEKPQRTNTLRMKHGTYDKLDDD GLIAPGVRVSGEDVIIGKTTPISSKRDASTPLRSTENGIV DQVLVTTNQDGLKFVKVRVRTTKIPQIGDKFASRHGQKGT IGITYRREDMPFTAEGIVPDLIINPHAIPSRMTVAHLIEC LLSKVAALSGNEGDASPFTDITVEGISKLLREHGYQSRGF EVMYNGHTGKKLMAQIFFGPTYYQRLRHMVDDKIHARARG PMQVLTRQPVEGRSRDGGLRFGEMERDCMIAHGAASFLKE RLMEASDAFRVHICGICGLMTVIAKLNHNQFECKGCDNKI DIYQIHIPYAAKLLFQELMAMNITPRLYTDRSRDF C:  SEEGPQVKIREASKDNVDFILSNVDLAMANSLRRVMIAEI PTLAIDSVEVETNTTVLADEFIAHRLGLIPLQSMDIEQLE YSRDCFCEDHCDKCSVVLTLQAFGESESTTNVYSKDLVIV SNLMGRNIGHPIIQDKEGNGVLICKLRKGQELKLTCVAKK GIAKEHAKWGPAAAIEFEYDPWNKLKHTDYWYEQDSAKEW PQSKNCEYEDPPNEGDPFDYKAQADTFYMNVESVGSIPVD QVVVRGIDTLQKKVASILLALTQMDQD D:  STSTFQTRRRRLKKVEEEENAATLQLGQEFQLKQINHQGE EEELIALNLSEARLVIKEALVERRRAFKRSQKKTREKELE SIDVLLEQTTGGNNKDLKNTMQYLTNFSRFRDQETVGAVI QLLKSTGLHPFEVAQLGSLACDTADEAKTLIPSLNNKISD DELERILKELSNLETLY E:  DQENERNISRLWRAFRTVKEMVKDRGYFITQEEVELPLED FKAKYCDSMGRPQRKMMSFQANPTEESISKFPDMGSLWVE FCDEPSVGVKTMKTFVIHIQEKNFQTGIFVYQNNITPSAM KLVPSIPPATIETFNEAALVVNITHHELVPKHIRLSSDEK RELLKRYRLKESQLPRIQRADPVALYLGLKRGEVVKIIRK SETSGRYASYRICM F:  LKEKAIPKDQRATTPYMTKYERARILGTRALQISMNAPVF VDLEGETDPLRIAMKELAEKKIPLVIRRYLPDGSFEDWSV EELIVDL G:  MFFIKDLSLNITLHPSFFGPRMKQYLKTKLLEEVEGSCTG KFGYILCVLDYDNIDIQRGRILPTDGSAEFNVKYRAVVFK PFKGEVVDGTVVSCSQHGFEVQVGPMKVFVTKHLMPQDLT FNAGSNPPSYQSSEDVITIKSRIRVKIEGCISQVSSIHAI GSIKEDYLGAI H:  SNTLFDDIFQVSEVDPGRYNKVCRIEAASTTQDQCKLTLD INVELFPVAAQDSLTVTIASSLNLTRSWRPPQAGDRSLAD DYDYVMYGTAYKFEEVSKDLIAVYYSFGGLLMRLEGNYRN LNNLKQENAYLLIRR I:  TTFRFCRDCNNMLYPREDKENNRLLFECRTCSYVEEAGSP LVYRHELITNIGETAGVVQDIGSDPTLPRSDRECPKCHSR ENVFFQSQQRRKDTSMVLFFVCLSCSHIFTSDQKNK J:  MIVPVRCFSCGKVVGDKWESYLNLLQEDELDEGTALSRLG LKRYCCRRMILTHVDLIEKFLRYNP K:  MNAPDRFELFLLGEGESKLKIDPDTKAPNAVVITFEKEDH TLGNLIRAELLNDRKVLFAAYKVEHPFFARFKLRIQTTEG YDPKDALKNACNSIINKLGALKTNFETEWNLQTL L:  ATLKYICAECSSKLSLSRTDAVRCKDCGHRILLKARTKRL VQFEAR Description Functional site 1) chain A residue 481 type sequence D description BINDING SITE FOR RESIDUE MG A2457 source : AC1 2) chain A residue 483 type sequence D description BINDING SITE FOR RESIDUE MG A2457 source : AC1 3) chain A residue 485 type sequence D description BINDING SITE FOR RESIDUE MG A2457 source : AC1 4) chain J residue 7 type sequence C description BINDING SITE FOR RESIDUE ZN A2458 source : AC2 5) chain J residue 10 type sequence C description BINDING SITE FOR RESIDUE ZN A2458 source : AC2 6) chain J residue 45 type sequence C description BINDING SITE FOR RESIDUE ZN A2458 source : AC2 7) chain J residue 46 type sequence C description BINDING SITE FOR RESIDUE ZN A2458 source : AC2 8) chain L residue 31 type sequence C description BINDING SITE FOR RESIDUE ZN A2459 source : AC3 9) chain L residue 34 type sequence C description BINDING SITE FOR RESIDUE ZN A2459 source : AC3 10) chain L residue 48 type sequence C description BINDING SITE FOR RESIDUE ZN A2459 source : AC3 11) chain L residue 51 type sequence C description BINDING SITE FOR RESIDUE ZN A2459 source : AC3 12) chain I residue 7 type sequence C description BINDING SITE FOR RESIDUE ZN A2460 source : AC4 13) chain I residue 10 type sequence C description BINDING SITE FOR RESIDUE ZN A2460 source : AC4 14) chain I residue 29 type sequence C description BINDING SITE FOR RESIDUE ZN A2460 source : AC4 15) chain I residue 32 type sequence C description BINDING SITE FOR RESIDUE ZN A2460 source : AC4 16) chain I residue 75 type sequence C description BINDING SITE FOR RESIDUE ZN A2461 source : AC5 17) chain I residue 78 type sequence C description BINDING SITE FOR RESIDUE ZN A2461 source : AC5 18) chain I residue 106 type sequence C description BINDING SITE FOR RESIDUE ZN A2461 source : AC5 19) chain I residue 108 type sequence H description BINDING SITE FOR RESIDUE ZN A2461 source : AC5 20) chain C residue 86 type sequence C description BINDING SITE FOR RESIDUE ZN A2462 source : AC6 21) chain C residue 88 type sequence C description BINDING SITE FOR RESIDUE ZN A2462 source : AC6 22) chain C residue 92 type sequence C description BINDING SITE FOR RESIDUE ZN A2462 source : AC6 23) chain C residue 95 type sequence C description BINDING SITE FOR RESIDUE ZN A2462 source : AC6 24) chain B residue 1163 type sequence C description BINDING SITE FOR RESIDUE ZN A2463 source : AC7 25) chain B residue 1166 type sequence C description BINDING SITE FOR RESIDUE ZN A2463 source : AC7 26) chain B residue 1182 type sequence C description BINDING SITE FOR RESIDUE ZN A2463 source : AC7 27) chain B residue 1185 type sequence C description BINDING SITE FOR RESIDUE ZN A2463 source : AC7 28) chain A residue 108 type sequence M description BINDING SITE FOR RESIDUE ZN A2464 source : AC8 29) chain A residue 110 type sequence C description BINDING SITE FOR RESIDUE ZN A2464 source : AC8 30) chain A residue 148 type sequence C description BINDING SITE FOR RESIDUE ZN A2464 source : AC8 31) chain A residue 167 type sequence C description BINDING SITE FOR RESIDUE ZN A2464 source : AC8 32) chain A residue 67 type sequence C description BINDING SITE FOR RESIDUE ZN A2465 source : AC9 33) chain A residue 70 type sequence C description BINDING SITE FOR RESIDUE ZN A2465 source : AC9 34) chain A residue 77 type sequence C description BINDING SITE FOR RESIDUE ZN A2465 source : AC9 35) chain A residue 80 type sequence H description BINDING SITE FOR RESIDUE ZN A2465 source : AC9 36) 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 37) 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 38) 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 39) 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 40) 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 41) 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 42) 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 43) 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 44) chain I residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI5 45) chain B residue 977-989 type prosite sequence GDKFASRHGQKGT description RNA_POL_BETA RNA polymerases beta chain signature. GdKFASrHGQKGT source prosite : PS01166 46) 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 47) 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 48) 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 49) 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 50) 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 51) chain I residue 75-110 type prosite sequence CPKCHSRENVFFQSQQRRKDTSMVLFFVCLSCSHIF description ZF_TFIIS_1 Zinc finger TFIIS-type signature. CpkChsrenvffqSQQRRkDTSmvlffvCls...CshiF source prosite : PS00466 52) 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 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 J residue 10 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 57) chain L residue 31-51 type ZN_FING sequence CAECSSKLSLSRTDAVRCKDC description C4-type source Swiss-Prot : SWS_FT_FI1 58) chain J residue 46 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 59) chain A residue 483 type ZN_FING sequence D description C4-type source Swiss-Prot : SWS_FT_FI1 60) chain A residue 485 type ZN_FING sequence D description C4-type source Swiss-Prot : SWS_FT_FI1 61) chain A residue 107 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 62) chain A residue 110 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 63) chain A residue 148 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 64) chain A residue 167 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 65) chain A residue 481 type ZN_FING sequence D 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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