eF-site ID 1twg-ABCEFHIJKL
PDB Code 1twg
Chain A, B, C, E, F, H, I, J, K, L
Title RNA polymerase II complexed with CTP
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 167
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 3006
source : AC8

32) chain B
residue 1163
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 3007
source : AC9

33) chain B
residue 1166
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 3007
source : AC9

34) chain B
residue 1182
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 3007
source : AC9

35) chain B
residue 1185
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 3007
source : AC9

36) chain A
residue 67
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 3008
source : BC1

37) chain A
residue 70
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 3008
source : BC1

38) chain A
residue 77
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 3008
source : BC1

39) chain A
residue 80
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 3008
source : BC1

40) chain A
residue 481
type
sequence D
description BINDING SITE FOR RESIDUE CTP B 3008
source : BC2

41) chain A
residue 483
type
sequence D
description BINDING SITE FOR RESIDUE CTP B 3008
source : BC2

42) chain A
residue 485
type
sequence D
description BINDING SITE FOR RESIDUE CTP B 3008
source : BC2

43) chain B
residue 766
type
sequence R
description BINDING SITE FOR RESIDUE CTP B 3008
source : BC2

44) chain B
residue 986
type
sequence Q
description BINDING SITE FOR RESIDUE CTP B 3008
source : BC2

45) chain B
residue 987
type
sequence K
description BINDING SITE FOR RESIDUE CTP B 3008
source : BC2

46) chain B
residue 837
type catalytic
sequence D
description 788
source MCSA : MCSA1

47) chain A
residue 483
type catalytic
sequence D
description 788
source MCSA : MCSA1

48) chain A
residue 485
type catalytic
sequence D
description 788
source MCSA : MCSA1

49) 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

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 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

54) 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

55) 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

56) chain B
residue 977-989
type prosite
sequence GDKFASRHGQKGT
description RNA_POL_BETA RNA polymerases beta chain signature. GdKFASrHGQKGT
source prosite : PS01166

57) 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

58) 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

59) 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

60) 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

61) chain I
residue 40
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:18407956
source Swiss-Prot : SWS_FT_FI5

62) chain L
residue 31-51
type ZN_FING
sequence CAECSSKLSLSRTDAVRCKDC
description C4-type
source Swiss-Prot : SWS_FT_FI1

63) chain A
residue 483
type ZN_FING
sequence D
description C4-type
source Swiss-Prot : SWS_FT_FI1

64) chain A
residue 485
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 J
residue 46
type ZN_FING
sequence C
description C4-type
source Swiss-Prot : SWS_FT_FI1

68) chain A
residue 107
type ZN_FING
sequence C
description C4-type
source Swiss-Prot : SWS_FT_FI1

69) chain A
residue 110
type ZN_FING
sequence C
description C4-type
source Swiss-Prot : SWS_FT_FI1

70) chain A
residue 148
type ZN_FING
sequence C
description C4-type
source Swiss-Prot : SWS_FT_FI1

71) chain A
residue 167
type ZN_FING
sequence C
description C4-type
source Swiss-Prot : SWS_FT_FI1

72) chain A
residue 481
type ZN_FING
sequence D
description C4-type
source Swiss-Prot : SWS_FT_FI1

73) chain L
residue 31
type BINDING
sequence C
description
source Swiss-Prot : SWS_FT_FI2

74) chain L
residue 34
type BINDING
sequence C
description
source Swiss-Prot : SWS_FT_FI2

75) chain L
residue 48
type BINDING
sequence C
description
source Swiss-Prot : SWS_FT_FI2

76) chain L
residue 51
type BINDING
sequence C
description
source Swiss-Prot : SWS_FT_FI2

77) chain B
residue 1185
type BINDING
sequence C
description
source Swiss-Prot : SWS_FT_FI2

78) 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

79) 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

80) 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

81) 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


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