eF-site ID 4a3f-ABCDEFGHIJKLNPT PDB Code 4a3f Chain A, B, C, D, E, F, G, H, I, J, K, L, N, P, T Title RNA Polymerase II initial transcribing complex with a 6nt DNA-RNA hybrid and soaked with AMPCPP Classification TRANSCRIPTION Compound DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB1 Source ORGANISM_COMMON: BAKER'S YEAST; ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE; Sequence A:  GQQYSSAPLRTVKEVQFGLFSPEEVRAISVAKIRFPETMD ETQTRAKIGGLNDPRLGSIDRNLKCQTCQEGMNECPGHFG HIDLAKPVFHVGFIAKIKKVCECVCMHCGKLLLDEHNELM RQALAIKDSKKRFAAIWTLCKTKMVCETDVPSEDDPTQLV SRGGCGNTQPTIRKDGLKLVGSWKKDRATGDADEPELRVL STEEILNIFKHISVKDFTSLGFNEVFSRPEWMILTCLPVP PPPVRPSISFNESQRGEDDLTFKLADILKANISLETLEHN GAPHHAIEEAESLLQFHVATYMDNDIAGQPQALQKSGRPV KSIRARLKGKEGRIRGNLMGKRVDFSARTVISGDPNLELD QVGVPKSIAKTLTYPEVVTPYNIDRLTQLVRNGPNEHPGA KYVIRDSGDRIDLRYSKRAGDIQLQYGWKVERHIMDNDPV LFNRQPSLHKMSMMAHRVKVIPYSTFRLNLSVTSPYNADF DGDEMNLHVPQSEETRAELSQLCAVPLQIVSPQSNKPCMG IVQDTLCGIRKLTLRDTFIELDQVLNMLYWVPDWDGVIPT PAIIKPKPLWSGKQILSVAIPNGIHLQRFDEGTTLLSPKD NGMLIIDGQIIFGVVEKKTVGSSNGGLIHVVTREKGPQVC AKLFGNIQKVVNFWLLHNGFSTGIGDTIADGPTMREITET IAEAKKKVLDVTKEAQANLLTAKHGMTLRESFEDNVVRFL NEARDKAGRLAEVNLKDLNNVKQMVMAGSKGSFINIAQMS ACVGQQSVEGKRIAFGFVDRTLPHFSKDDYSPESKGFVEN SYLRGLTPQEFFFHAMGGREGLIDTAVKTAETGYIQRRLV KALEDIMVHYDNTTRNSLGNVIQFIYGEDGMDAAHIEKQS LDTIGGSDAAFEKRYRVDLLNTDHTLDPSLLESGSEILGD LKLQVLLDEEYKQLVKDRKFLREVFVDGEANWPLPVNIRR IIQNAQQTFHIDHTKPSDLTIKDIVLGVKDLQENLLVLRG KNEIIQNAQRDAVTLFCCLLRSRLATRRVLQEYRLTKQAF DWVLSNIEAQFLRSVVHPGEMVGVLAAQSIGEPATQMTLN TKKVTSGVPRLKEILNVAKNMKTPSLTVYLEPGHAADQEQ AKLIRSAIEHTTLKSVTIASEIYYDPDPRSTVIPEDEEII QLHFSLQQSPWLLRLELDRAAMNDKDLTMGQVGERIKQTF KNDLFVIWSEDNDEKLIIRCRVVAEEDHMLKKIENTMLEN ITLRGVENIERVVMMKYDRKVPSPTGEYVKEPEWVLETDG VNLSEVMTVPGIDPTRIYTNSFIDIMEVLGIEAGRAALYK EVYNVIASDGSYVNYRHMALLVDVMTTQGGLTSVTRHGFN RSNTGALMRCSFEETVEILFEAGASAELDDCRGVSENVIL GQMAPIGTGAFDVMIDEESLVKYMP B:  DESAPITAEDSWAVISAFFREKGLVSQQLDSFNQFVDYTL QDIICEDSTLIISFGKIYVTKPMVNESDGVTHALYPQEAR LRNLTYSSGLFVDVKKKVFIGRLPIMLRSKNCYLSEATES DLYKLKECPFDMGGYFIINGSEKVLIAQERSAGNIVQVFK KAAPSPISHVAEIRSALEKGSRFISTLQVKLYGREGSSAR TIKATLPYIKQDIPIVIIFRALGIIPDGEILEHICYDVND WQMLEMLKPCVEDGFVIQDRETALDFIGRRGTALGIKKEK RIQYAKDILQKEFLPHITQLEGFESRKAFFLGYMINRLLL CALDRKDQDDRDHFGKKRLDLAGPLLAQLFKTLFKKLTKD IFRYMQRTVELAINAKTITSGLKYALATGNWGEQKKAMSS RAGVSQVLNRYTYSSTLSHLRRTNTPIAKPRQLHNTHWGL VCPAETPEGQACGLVKNLSLMSCISVGTDPMPIITFLSEW GMEPLEDYVPHQSPDATRVFVNGVWHGVHRNPARLMETLR TLRRKGDINPEVSMIRDIREKELKIFTDAGRVYRPLFIVE DDESLGHKELKVRKGHIAKLMATEYQDEYTWSSLLNEGLV EYIDAEEEESILIAMQPEDLEPAEADVDPAKRIRVSHHAT TFTHCEIHPSMILGVAASIIPFPDHNQSPRNTYQSAMGKQ AMGVFLTNYNVRMDTMANILYYPQKPLGTTRAMEYLKFRE LPAGQNAIVAIACYSGYNQEDSMIMNQSSIDRGLFRSLFF RSYMDQEKKYGMSITETFEKPQRTNTLRMKHGTYDKLDDD GLIAPGVRVSGEDVIIGKTTPISSKRDASTPLRSTENGIV DQVLVTTNQDGLKFVKVRVRTTKIPQIGDKFASRHGQKGT IGITYRREDMPFTAEGIVPDLIINPHAIPSRMTVAHLIEC LLSKVAALSGNEGDASPFTDITVEGISKLLREHGYQSRGF EVMYNGHTGKKLMAQIFFGPTYYQRLRHMVDDKIHARARG PMQVLTRQPVEGRSRDGGLRFGEMERDCMIAHGAASFLKE RLMEASDAFRVHICGICGLMTVIAKLNHNQFECKGCDNKI DIYQIHIPYAAKLLFQELMAMNITPRLYTDRSRDF C:  EEGPQVKIREASKDNVDFILSNVDLAMANSLRRVMIAEIP TLAIDSVEVETNTTVLADEFIAHRLGLIPLQSMDIEQLEY SRDCFCEDHCDKCSVVLTLQAFGESESTTNVYSKDLVIVS NLMGRNIGHPIIQDKEGNGVLICKLRKGQELKLTCVAKKG IAKEHAKWGPAAAIEFEYDPWNKLKHTDYWYEQDSAKEWP QSKNCEYEDPPNEGDPFDYKAQADTFYMNVESVGSIPVDQ VVVRGIDTLQKKVASILLALTQMDQD D:  VSTSTFQTRRRRLKKVEEEENAATLQLGQEFQLKQINHQG EEEELIALNLSEARLVIKEALVERRRAFKRSQKKTREKEL ESIDVLLEQTTGGNNKDLKNTMQYLTNFSRFRDQETVGAV IQLLKSTGLHPFEVAQLGSLACDTADEAKTLIPSLNNKIS DDELERILKELSNLETLY E:  DQENERNISRLWRAFRTVKEMVKDRGYFITQEEVELPLED FKAKYCDSMGRPQRKMMSFQANPTEESISKFPDMGSLWVE FCDEPSVGVKTMKTFVIHIQEKNFQTGIFVYQNNITPSAM KLVPSIPPATIETFNEAALVVNITHHELVPKHIRLSSDEK RELLKRYRLKESQLPRIQRADPVALYLGLKRGEVVKIIRK SETSGRYASYRICM F:  KAIPKDQRATTPYMTKYERARILGTRALQISMNAPVFVDL EGETDPLRIAMKELAEKKIPLVIRRYLPDGSFEDWSVEEL IVDL G:  MFFIKDLSLNITLHPSFFGPRMKQYLKTKLLEEVEGSCTG KFGYILCVLDYDNIDIQRGRILPTDGSAEFNVKYRAVVFK PFKGEVVDGTVVSCSQHGFEVQVGPMKVFVTKHLMPQDLT FNAGSNPPSYQSSEDVITIKSRIRVKIEGCISQVSSIHAI GSIKEDYLGAI H:  SNTLFDDIFQVSEVDPGRYNKVCRIEAASTTQDQCKLTLD INVELFPVAAQDSLTVTIASSLTRSWRPPQAGDRSLADDY DYVMYGTAYKFEEVSKDLIAVYYSFGGLLMRLEGNYRNLN NLKQENAYLLIRR I:  TTFRFCRDCNNMLYPREDKENNRLLFECRTCSYVEEAGSP LVYRHELITNIGETAGVVQDIGSDPTLPRSDRECPKCHSR ENVFFQSQQRRKDTSMVLFFVCLSCSHIFTSDQKNKRTQ J:  MIVPVRCFSCGKVVGDKWESYLNLLQEDELDEGTALSRLG LKRYCCRRMILTHVDLIEKFLRYNP K:  MNAPDRFELFLLGEGESKLKIDPDTKAPNAVVITFEKEDH TLGNLIRAELLNDRKVLFAAYKVEHPFFARFKLRIQTTEG YDPKDALKNACNSIINKLGALKTNFETEWNLQTLA L:  ATLKYICAECSSKLSLSRTDAVRCKDCGHRILLKARTKRL VQFEAR N:  AAGTACTTGAG P:  CCAGGA T:  CTCAAGTACTTTTTCCXGGT Description (1)  DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB1 (E.C.2.7.7.6), DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB2 (E.C.2.7.7.6), DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB3, DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB4, DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC 1, DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC 2, RPB7, DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB7, DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC 3, DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB9, DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC 5, DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB11, DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC 4 Functional site 1) chain A residue 446 type sequence R description BINDING SITE FOR RESIDUE APC A 2455 source : AC1 2) chain A residue 448 type sequence P description BINDING SITE FOR RESIDUE APC A 2455 source : AC1 3) chain A residue 479 type sequence N description BINDING SITE FOR RESIDUE APC A 2455 source : AC1 4) chain A residue 483 type sequence D description BINDING SITE FOR RESIDUE APC A 2455 source : AC1 5) chain A residue 1078 type sequence Q description BINDING SITE FOR RESIDUE APC A 2455 source : AC1 6) chain A residue 1082 type sequence N description BINDING SITE FOR RESIDUE APC A 2455 source : AC1 7) chain B residue 529 type sequence E description BINDING SITE FOR RESIDUE APC A 2455 source : AC1 8) chain B residue 766 type sequence R description BINDING SITE FOR RESIDUE APC A 2455 source : AC1 9) chain B residue 1020 type sequence R description BINDING SITE FOR RESIDUE APC A 2455 source : AC1 10) chain P residue 10 type sequence A description BINDING SITE FOR RESIDUE APC A 2455 source : AC1 11) chain T residue 18 type sequence T description BINDING SITE FOR RESIDUE APC A 2455 source : AC1 12) chain T residue 19 type sequence T description BINDING SITE FOR RESIDUE APC A 2455 source : AC1 13) chain A residue 107 type sequence C description BINDING SITE FOR RESIDUE ZN A 2456 source : AC2 14) chain A residue 110 type sequence C description BINDING SITE FOR RESIDUE ZN A 2456 source : AC2 15) chain A residue 148 type sequence C description BINDING SITE FOR RESIDUE ZN A 2456 source : AC2 16) chain A residue 167 type sequence C description BINDING SITE FOR RESIDUE ZN A 2456 source : AC2 17) chain A residue 67 type sequence C description BINDING SITE FOR RESIDUE ZN A 2457 source : AC3 18) chain A residue 70 type sequence C description BINDING SITE FOR RESIDUE ZN A 2457 source : AC3 19) chain A residue 77 type sequence C description BINDING SITE FOR RESIDUE ZN A 2457 source : AC3 20) chain A residue 80 type sequence H description BINDING SITE FOR RESIDUE ZN A 2457 source : AC3 21) chain A residue 481 type sequence D description BINDING SITE FOR RESIDUE MG A 2458 source : AC4 22) chain A residue 483 type sequence D description BINDING SITE FOR RESIDUE MG A 2458 source : AC4 23) chain A residue 485 type sequence D description BINDING SITE FOR RESIDUE MG A 2458 source : AC4 24) chain P residue 10 type sequence A description BINDING SITE FOR RESIDUE MG A 2458 source : AC4 25) chain B residue 1163 type sequence C description BINDING SITE FOR RESIDUE ZN B 2225 source : AC5 26) chain B residue 1166 type sequence C description BINDING SITE FOR RESIDUE ZN B 2225 source : AC5 27) chain B residue 1182 type sequence C description BINDING SITE FOR RESIDUE ZN B 2225 source : AC5 28) chain B residue 1185 type sequence C description BINDING SITE FOR RESIDUE ZN B 2225 source : AC5 29) chain C residue 86 type sequence C description BINDING SITE FOR RESIDUE ZN C 1269 source : AC6 30) chain C residue 88 type sequence C description BINDING SITE FOR RESIDUE ZN C 1269 source : AC6 31) chain C residue 92 type sequence C description BINDING SITE FOR RESIDUE ZN C 1269 source : AC6 32) chain C residue 95 type sequence C description BINDING SITE FOR RESIDUE ZN C 1269 source : AC6 33) chain I residue 7 type sequence C description BINDING SITE FOR RESIDUE ZN I 1121 source : AC7 34) chain I residue 10 type sequence C description BINDING SITE FOR RESIDUE ZN I 1121 source : AC7 35) chain I residue 29 type sequence C description BINDING SITE FOR RESIDUE ZN I 1121 source : AC7 36) chain I residue 32 type sequence C description BINDING SITE FOR RESIDUE ZN I 1121 source : AC7 37) chain I residue 75 type sequence C description BINDING SITE FOR RESIDUE ZN I 1122 source : AC8 38) chain I residue 78 type sequence C description BINDING SITE FOR RESIDUE ZN I 1122 source : AC8 39) chain I residue 103 type sequence C description BINDING SITE FOR RESIDUE ZN I 1122 source : AC8 40) chain I residue 106 type sequence C description BINDING SITE FOR RESIDUE ZN I 1122 source : AC8 41) chain J residue 7 type sequence C description BINDING SITE FOR RESIDUE ZN J 1066 source : AC9 42) chain J residue 10 type sequence C description BINDING SITE FOR RESIDUE ZN J 1066 source : AC9 43) chain J residue 45 type sequence C description BINDING SITE FOR RESIDUE ZN J 1066 source : AC9 44) chain J residue 46 type sequence C description BINDING SITE FOR RESIDUE ZN J 1066 source : AC9 45) chain L residue 31 type sequence C description BINDING SITE FOR RESIDUE ZN L 1071 source : BC1 46) chain L residue 34 type sequence C description BINDING SITE FOR RESIDUE ZN L 1071 source : BC1 47) chain L residue 48 type sequence C description BINDING SITE FOR RESIDUE ZN L 1071 source : BC1 48) chain L residue 51 type sequence C description BINDING SITE FOR RESIDUE ZN L 1071 source : BC1 49) 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 50) 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 51) 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 52) 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 53) 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 54) 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 55) 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 56) 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 57) chain I residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI5 58) chain B residue 977-989 type prosite sequence GDKFASRHGQKGT description RNA_POL_BETA RNA polymerases beta chain signature. GdKFASrHGQKGT source prosite : PS01166 59) 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 60) 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 61) 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 62) 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 63) 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 64) chain I residue 75-110 type prosite sequence CPKCHSRENVFFQSQQRRKDTSMVLFFVCLSCSHIF description ZF_TFIIS_1 Zinc finger TFIIS-type signature. CpkChsrenvffqSQQRRkDTSmvlffvCls...CshiF source prosite : PS00466 65) 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 66) chain B residue 837 type catalytic sequence D description 788 source MCSA : MCSA1 67) chain A residue 483 type catalytic sequence D description 788 source MCSA : MCSA1 68) chain A residue 485 type catalytic sequence D description 788 source MCSA : MCSA1 69) chain A residue 483 type ZN_FING sequence D description C4-type source Swiss-Prot : SWS_FT_FI1 70) chain A residue 485 type ZN_FING sequence D 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 31-51 type ZN_FING sequence CAECSSKLSLSRTDAVRCKDC description C4-type source Swiss-Prot : SWS_FT_FI1 77) chain J residue 10 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 78) chain J residue 45 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 79) chain J residue 46 type ZN_FING sequence C description C4-type source Swiss-Prot : SWS_FT_FI1 80) chain B residue 1185 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI2 81) chain L residue 31 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI2 82) chain L residue 34 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI2 83) chain L residue 48 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI2 84) chain L residue 51 type BINDING sequence C description source Swiss-Prot : SWS_FT_FI2

Display surface Download Links