eF-site ID 2e2h-ABCEFHIJKLNRT
PDB Code 2e2h
Chain A, B, C, E, F, H, I, J, K, L, N, R, T
Title RNA polymerase II elongation complex at 5 mM Mg2+ with GTP
Classification TRANSCRIPTION,TRANSFERASE/DNA-RNA HYBRID
Compound 5'-R(*AP*UP*CP*GP*AP*GP*AP*GP*GP*A)-3'
Source ORGANISM_COMMON: baker's yeast; ORGANISM_SCIENTIFIC: Saccharomyces cerevisiae;
Sequence A:  VGQQYSSAPLRTVKEVQFGLFSPEEVRAISVAKIRFPETM
DETQTRAKIGGLNDPRLGSIDRNLKCQTCQEGMNECPGHF
GHIDLAKPVFHVGFIAKIKKVCECVCMHCGKLLLDEHNEL
MRQALAIKDSKKRFAAIWTLCKTKMVCETDVPSELVSRGG
CGNTQPTIRKDGLKLVGSWLRVLSTEEILNIFKHISVKDF
TSLGFNEVFSRPEWMILTCLPVPPPPVRPSISFNESQRGE
DDLTFKLADILKANISLETLEHNGAPHHAIEEAESLLQFH
VATYMDNDIAGQPQAGRPVKSIRARLKGKEGRIRGNLMGK
RVDFSARTVISGDPNLELDQVGVPKSIAKTLTYPEVVTPY
NIDRLTQLVRNGPNEHPGAKYVIRDSGDRIDLRYSKRAGD
IQLQYGWKVERHIMDNDPVLFNRQPSLHKMSMMAHRVKVI
PYSTFRLNLSVTSPYNADFDGDEMNLHVPQSEETRAELSQ
LCAVPLQIVSPQSNKPCMGIVQDTLCGIRKLTLRDTFIEL
DQVLNMLYWVPDWDGVIPTPAIIKPKPLWSGKQILSVAIP
NGIHLQRFDEGTTLLSPKDNGMLIIDGQIIFGVVEKKTVG
SSNGGLIHVVTREKGPQVCAKLFGNIQKVVNFWLLHNGFS
TGIGDTIADGPTMREITETIAEAKKKVLDVTKEAQANLLT
AKHGMTLRESFEDNVVRFLNEARDKAGRLAEVNLKDLNNV
KQMVMAGSKGSFINIAQMSACVGQQSVEGKRIAFGFVDRT
LPHFSKDDYSPESKGFVENSYLRGLTPQEFFFHAMGGREG
LIDTAVKTAETGYIQRRLVKALEDIMVHYDNTTRNSLGNV
IQFIYGEDGMDAAHIEKQSLDTIGGSDAAFEKRYRVDLLN
TDHTLDPSLLESGSEILGDLKLQVLLDEEYKQLVKDRKFL
REVFVDGEANWPLPVNIRRIIQNAQQTFHIDHTKPSDLTI
KDIVLGVKDLQENLLVLRGKNEIIQNAQRDAVTLFCCLLR
SRLATRRVLQEYRLTKQAFDWVLSNIEAQFLRSVVHPGEM
VGVLAAQSIGEPATQMTLNTFHFAGVASKKVTSGVPRLKE
ILNVAKNMKTPSLTVYLEPGHAADQEQAKLIRSAIEHTTL
KSVTIASEIYYDPDPRSTVIPEDEEIIQLHFSLQQSPWLL
RLELDRAAMNDKDLTMGQVGERIKQTFKNDLFVIWSEDLI
IRCRVVAEEDHMLKKIENTMLENITLRGVENIERVVMMKY
DRKVPSPTGEYVKEPEWVLETDGVNLSEVMTVPGIDPTRI
YTNSFIDIMEVLGIEAGRAALYKEVYNVIASDGSYVNYRH
MALLVDVMTTQGGLTSVTRHGFNRSNTGALMRCSFEETVE
ILFEAGASAELDDCRGVSENVILGQMAPIGTGAFDVMI
B:  DESAPITAEDSWAVISAFFREKGLVSQQLDSFNQFVDYTL
QDIICEDSTLIISFGKIYVTKPMVNESDGVTHALYPQEAR
LRNLTYSSGLFVDVKVFIGRLPIMLRSKNCYLSEATESDL
YKLKECPFDMGGYFIINGSEKVLIAQERSAGNIVQVFKKA
APSPISHVAEIRSALEKGSISTLQVKLYGREGSSARTIKA
TLPYIKQDIPIVIIFRALGIIPDGEILEHICYDVNDWQML
EMLKPCVEDGFVIQDRETALDFIGKEKRIQYAKDILQKEF
LPHITQLEGFESRKAFFLGYMINRLLLCALDRKDQDDRDH
FGKKRLDLAGPLLAQLFKTLFKKLTKDIFRYMQRTVELAI
NAKTITSGLKYALATGNWGEQKKAMSSRAGVSQVLNRYTY
SSTLSHLRRTNTPIAKPRQLHNTHWGLVCPAETPEGQACG
LVKNLSLMSCISVGTDPMPIITFLSEWGMEPLEDYVPHQS
PDATRVFVNGVWHGVHRNPARLMETLRTLRRKGDINPEVS
MIRDIREKELKIFTDAGRVYRPLFIVEDDESLGHKELKVR
KGHIAKLMATEYQDEYTWSSLLNEGLVEYIDAEEEESILI
AMQPEDLEPAEDVDPAKRIRVSATTFTHCEIHPSMILGVA
ASIIPFPDHNQSPRNTYQSAMGKQAMGVFLTNYNVRMDTM
ANILYYPQKPLGTTRAMEYLKFRELPAGQNAIVAIACYSG
YNQEDSMIMNQSSIDRGLFRSLFFRSYMDQEKKYGMSITE
TFEKPQRTNTLRMKHGTYDKLDDDGLIAPGVRVSGEDVII
GKTTPISRDASTPLRSTENGIVDQVLVTTNQDGLKFVKVR
VRTTKIPQIGDKFASRHGQKGTIGITYRREDMPFTAEGIV
PDLIINPHAIPSRMTVAHLIECLLSKVAALSGNEGDASPF
TDITVEGISKLLREHGYQSRGFEVMYNGHTGKKLMAQIFF
GPTYYQRLRHMVDDKIHARARGPMQVLTRQPVEGRSRDGG
LRFGEMERDCMIAHGAASFLKERLMEASDAFRVHICGICG
LMTVIAKLNHNQFECKGCDNKIDIYQIHIPYAAKLLFQEL
MAMNITPRLYTDRSRD
C:  EEGPQVKIREASKDNVDFILSNVDLAMANSLRRVMIAEIP
TLAIDSVEVETNTTVLADEFIAHRLGLIPLQSMDIEQLEY
SRDCFCEDHCDKCSVVLTLQAFGESESTTNVYSKDLVIVS
NLMGRNIGHPIIQDKEGNGVLICKLRKGQELKLTCVAKKG
IAKEHAKWGPAAAIEFEYDPWNKLKHTDYWYEQDSAKEWP
QSKNCEYEDPPNEGDPFDYKAQADTFYMNVESVGSIPVDQ
VVVRGIDTLQKKVASILLALTQMDQD
E:  QENERNISRLWRAFRTVKEMVKDRGYFITQEEVELPLEDF
KAKYCDRPQRKMMSFQANPTEESISKFPDMGSLWVEFTFV
IHIQEKNFQTGIFVTPSAMKLVPSIPPATIETFNEAALVV
NITHHELVPKHIRLSSDEKRELLKRYRLKESQLPRIQRAD
PVALYLGLKRGEVVKIIRKSETSGRYASYRICM
F:  KAIPKDQRATTPYMTKYERARILGTRALQISMNAPVFVDL
EGETDPLRIAMKELAEKKIPLVIRRYLPDGSFEDWSVEEL
IVD
H:  SNTLFDDIFQVSEVDPGRYNKVCRIEAASTTQDQCKLTLD
INVELFPVAAQDSLTVTIASSLTRSWRPPQAGDRSLADDY
DYVMYGTAYKFEEVSKDLIAVYYSFGGLLMRLEGNYRNLN
NLKQENAYLLIRR
I:  TTFRFCRDCNNMLYPREDKENNRLLFECRTCSYVEEAGSP
LVYRHELITNIGETAGVVQDIGSDPTLPRSDRECPKCHSR
ENVFFQSQQRRKDTSMVLFFVCLSCSHIFTSDQKNKRTQ
J:  MIVPVRCFSCGKVVGDKWESYLNLLQEDELDEGTALSRLG
LKRYCCRRMILTHVDLIEKFLRYNP
K:  MNAPDRFELFLLGEGESKLKIDPDTKAPNAVVITFEKEDH
TLGNLIRAELLNDRKVLFAAYKVEHPFFARFKLRIQTTEG
YDPKDALKNACNSIINKLGALKTNFETEWNLQTL
L:  ATLKYICAECSSKLSLSRTDAVRCKDCGHRILLKARTKRL
VQFEAR
N:  CTGCTTATCGGTAG
R:  AUCGAGAGGA
T:  CTACCGATAAGCAGACGCTCCTCTCGAT
Description


Functional site

1) chain A
residue 108
type
sequence M
description BINDING SITE FOR RESIDUE ZN A 1734
source : AC1

2) chain A
residue 110
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1734
source : AC1

3) chain A
residue 167
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1734
source : AC1

4) chain A
residue 67
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1735
source : AC2

5) chain A
residue 70
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1735
source : AC2

6) chain A
residue 77
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1735
source : AC2

7) chain A
residue 80
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 1735
source : AC2

8) chain B
residue 1163
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 1307
source : AC3

9) chain B
residue 1166
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 1307
source : AC3

10) chain B
residue 1182
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 1307
source : AC3

11) chain B
residue 1185
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 1307
source : AC3

12) chain C
residue 86
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 319
source : AC4

13) chain C
residue 88
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 319
source : AC4

14) chain C
residue 92
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 319
source : AC4

15) chain C
residue 95
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 319
source : AC4

16) chain I
residue 10
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 203
source : AC5

17) chain I
residue 29
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 203
source : AC5

18) chain I
residue 30
type
sequence R
description BINDING SITE FOR RESIDUE ZN I 203
source : AC5

19) chain I
residue 32
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 203
source : AC5

20) chain I
residue 75
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 204
source : AC6

21) chain I
residue 78
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 204
source : AC6

22) chain I
residue 80
type
sequence S
description BINDING SITE FOR RESIDUE ZN I 204
source : AC6

23) chain I
residue 103
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 204
source : AC6

24) chain I
residue 106
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 204
source : AC6

25) chain I
residue 108
type
sequence H
description BINDING SITE FOR RESIDUE ZN I 204
source : AC6

26) chain J
residue 7
type
sequence C
description BINDING SITE FOR RESIDUE ZN J 101
source : AC7

27) chain J
residue 9
type
sequence S
description BINDING SITE FOR RESIDUE ZN J 101
source : AC7

28) chain J
residue 10
type
sequence C
description BINDING SITE FOR RESIDUE ZN J 101
source : AC7

29) chain J
residue 45
type
sequence C
description BINDING SITE FOR RESIDUE ZN J 101
source : AC7

30) chain J
residue 46
type
sequence C
description BINDING SITE FOR RESIDUE ZN J 101
source : AC7

31) chain L
residue 31
type
sequence C
description BINDING SITE FOR RESIDUE ZN L 105
source : AC8

32) chain L
residue 33
type
sequence E
description BINDING SITE FOR RESIDUE ZN L 105
source : AC8

33) chain L
residue 34
type
sequence C
description BINDING SITE FOR RESIDUE ZN L 105
source : AC8

34) chain L
residue 48
type
sequence C
description BINDING SITE FOR RESIDUE ZN L 105
source : AC8

35) chain L
residue 51
type
sequence C
description BINDING SITE FOR RESIDUE ZN L 105
source : AC8

36) chain A
residue 481
type
sequence D
description BINDING SITE FOR RESIDUE MG A 2001
source : AC9

37) chain A
residue 483
type
sequence D
description BINDING SITE FOR RESIDUE MG A 2001
source : AC9

38) chain A
residue 485
type
sequence D
description BINDING SITE FOR RESIDUE MG A 2001
source : AC9

39) chain A
residue 481
type
sequence D
description BINDING SITE FOR RESIDUE MG A 2002
source : BC1

40) chain A
residue 483
type
sequence D
description BINDING SITE FOR RESIDUE MG A 2002
source : BC1

41) chain B
residue 837
type
sequence D
description BINDING SITE FOR RESIDUE MG A 2002
source : BC1

42) chain B
residue 1020
type
sequence R
description BINDING SITE FOR RESIDUE MG A 2002
source : BC1

43) chain A
residue 448
type
sequence P
description BINDING SITE FOR RESIDUE GTP T 3000
source : BC2

44) chain A
residue 481
type
sequence D
description BINDING SITE FOR RESIDUE GTP T 3000
source : BC2

45) chain A
residue 483
type
sequence D
description BINDING SITE FOR RESIDUE GTP T 3000
source : BC2

46) chain A
residue 485
type
sequence D
description BINDING SITE FOR RESIDUE GTP T 3000
source : BC2

47) chain A
residue 827
type
sequence T
description BINDING SITE FOR RESIDUE GTP T 3000
source : BC2

48) chain A
residue 1081
type
sequence L
description BINDING SITE FOR RESIDUE GTP T 3000
source : BC2

49) chain A
residue 1085
type
sequence H
description BINDING SITE FOR RESIDUE GTP T 3000
source : BC2

50) chain B
residue 766
type
sequence R
description BINDING SITE FOR RESIDUE GTP T 3000
source : BC2

51) chain B
residue 987
type
sequence K
description BINDING SITE FOR RESIDUE GTP T 3000
source : BC2

52) chain B
residue 1020
type
sequence R
description BINDING SITE FOR RESIDUE GTP T 3000
source : BC2

53) chain R
residue 10
type
sequence A
description BINDING SITE FOR RESIDUE GTP T 3000
source : BC2

54) chain T
residue 18
type
sequence C
description BINDING SITE FOR RESIDUE GTP T 3000
source : BC2

55) chain T
residue 19
type
sequence T
description BINDING SITE FOR RESIDUE GTP T 3000
source : BC2

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

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

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

59) chain A
residue 1085
type catalytic
sequence H
description 788
source MCSA : MCSA1

60) 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

61) 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

62) 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

63) 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

64) 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

65) 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

66) 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

67) 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

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

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 J
residue 10
type ZN_FING
sequence C
description C4-type
source Swiss-Prot : SWS_FT_FI1

72) chain J
residue 45
type ZN_FING
sequence C
description C4-type
source Swiss-Prot : SWS_FT_FI1

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

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

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

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

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

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

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

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

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

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

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

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

85) 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

86) 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

87) chain I
residue 75-110
type prosite
sequence CPKCHSRENVFFQSQQRRKDTSMVLFFVCLSCSHIF
description ZF_TFIIS_1 Zinc finger TFIIS-type signature. CpkChsrenvffqSQQRRkDTSmvlffvCls...CshiF
source prosite : PS00466

88) 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

89) 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

90) 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

91) 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

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


Display surface

Download
Links