eF-site ID 6bqf-ABCEFHIJKL
PDB Code 6bqf
Chain A, B, C, E, F, H, I, J, K, L
Title Pol II elongation complex with 'dT-AP' at i+1, i-1 position
Classification TRANSFERASE/TRANSCRIPTION
Compound DNA-directed RNA polymerase II subunit RPB1
Source (6BQF)
Sequence A:  GQQYSSAPLRTVKEVQFGLFSPEEVRAISVAKIRFPETMD
ETQTRAKIGGLNDPRLGSIDRNLKCQTCQEGMNECPGHFG
HIDLAKPVFHVGFIAKIKKVCECVCMHCGKLLLDEHNELM
RQALAIKDSKKRFAAIWTLCKTKMVCGGCGNTQPTIRKDG
LKLVGSWVLSTEEILNIFKHISVKDFTSLGFNEVFSRPEW
MILTCLPVPPPPVRPSIEDDLTFKLADILKANISLETLEH
NGAPHHAIEEAESLLQFHVATYMDNDIAGQPQALQKSGRP
VKSIRARLKGKEGRIRGNLMGKRVDFSARTVISGDPNLEL
DQVGVPKSIAKTLTYPEVVTPYNIDRLTQLVRNGPNEHPG
AKYVIRDSGDRIDLRYSKRAGDIQLQYGWKVERHIMDNDP
VLFNRQPSLHKMSMMAHRVKVIPYSTFRLNLSVTSPYNAD
FDGDEMNLHVPQSEETRAELSQLCAVPLQIVSPQSNKPCM
GIVQDTLCGIRKLTLRDTFIELDQVLNMLYWVPDWDGVIP
TPAIIKPKPLWSGKQILSVAIPNGIHLQRFDEGTTLLSPK
DNGMLIIDGQIIFGVVEKKTVGSSNGGLIHVVTREKGPQV
CAKLFGNIQKVVNFWLLHNGFSTGIGDTIADGPTMREITE
TIAEAKKKVLDVTKEAQANLLTAKHGMTLRESFEDNVVRF
LNEARDKAGRLAEVNLKDLNNVKQMVMAGSKGSFINIAQM
SACVGQQSVEGKRIAFGFVDRTLPHFSKDDYSPESKGFVE
NSYLRGLTPQEFFFHAMGGREGLIDTAVKTAETGYIQRRL
VKALEDIMVHYDNTTRNSLGNVIQFIYGEDGMDAAHIEKQ
SLDTIGGSDAAFEKRYRVDLLNTDHTLDPSLLESGSEILG
DLKLQVLLDEEYKQLVKDRKFLREVFVDGEANWPLPVNIR
RIIQNAQQTFHIDHTKPSDLTIKDIVLGVKDLQENLLVLR
GKNEIIQNAQRDAVTLFCCLLRSRLATRRVLQEYRLTKQA
FDWVLSNIEAQFLRSVVHPGEMVGVLAAQSIGEPATQMTK
VTSGVPRLKEILNVAKNMKTPSLTVYLEPGHAADQEQAKL
IRSAIEHTTLKSVTIASEIYYDPDPRSTVIPEDEEIIQLH
FSQQSPWLLRLELDRAAMNDKDLTMGQVGERIKQTFKNDL
FVIWSEDNDEKLIIRCRVVAEEDHMLKKIENTMLENITLR
GVENIERVVMMKYDRKVPSPTGEYVKEPEWVLETDGVNLS
EVMTVPGIDPTRIYTNSFIDIMEVLGIEAGRAALYKEVYN
VIASDGSYVNYRHMALLVDVMTTQGGLTSVTRHGFNRSNT
GALMRCSFEETVEILFEAGASAELDDCRGVSENVILGQMA
PIGTGAFDVMID
B:  DESAPITAEDSWAVISAFFREKGLVSQQLDSFNQFVDYTL
QDIICEDSTLIEISFGKIYVTKPMVNESDGVTHALYPQEA
RLRNLTYSSGLFVDVKKKVFIGRLPIMLRSKNCYLSEATE
SDLYKLKECPFDMGGYFIINGSEKVLIAQERSAGNIVQVF
KKAAPSPISHVAEIRSAISTLQVKLYGREGSSARTIKATL
PYIKQDIPIVIIFRALGIIPDGEILEHICYDVNDWQMLEM
LKPCVEDGFVIQDRETALDFIGRRGKEKRIQYAKDILQKE
FLPHITQLEGFESRKAFFLGYMINRLLLCALDRKDQDDRD
HFGKKRLDLAGPLLAQLFKTLFKKLTKDIFRYMQRTLAIN
AKTITSGLKYALATGNWGEQKKAMSSRAGVSQVLNRYTYS
STLSHLRRTNTPIAKPRQLHNTHWGLVCPAETPEGQACGL
VKNLSLMSCISVGTDPMPIITFLSEWGMEPLEDYVPHQSP
DATRVFVNGVWHGVHRNPARLMETLRTLRRKGDINPEVSM
IRDIREKELKIFTDAGRVYRPLFIVEDDESLGHKELKVRK
GHIAKLMATEYQDEYTWSSLLNEGLVEYIDAEEEESILIA
MQPEDLEPDVDPAKRIRVSHHATTFTHCEIHPSMILGVAA
SIIPFPDHNQSPRNTYQSAMGKQAMGVFLTNYNVRMDTMA
NILYYPQKPLGTTRAMEYLKFRELPAGQNAIVAIACYSGY
NQEDSMIMNQSSIDRGLFRSLFFRSYMDQEKKYGMSITET
FEKPQRTNTLRMKHGTYDKLDDDGLIAPGVRVSGEDVIIG
KTTPITAYHSKRDASTPLRSTENGIVDQVLVTTNQDGLKF
VKVRVRTTKIPQIGDKFASRHGQKGTIGITYRREDMPFTA
EGIVPDLIINPHAIPSRMTVAHLIECLLSKVAALSGNEGD
ASPFTDITVEGISKLLREHGYQSRGFEVMYNGHTGKKLMA
QIFFGPTYYQRLRHMVDDKIHARARGPMQVLTRQPVEGRS
RDGGLRFGEMERDCMIAHGAASFLKERLMEASDAFRVHIC
GICGLMTVIAKLNHNQFECKGCDNKIDIYQIHIPYAAKLL
FQELMAMNITPRLYTDR
C:  EEGPQVKIREASKDNVDFILSNVDLAMANSLRRVMIAEIP
TLAIDSVEVETNTTVLADEFIAHRLGLIPLQSMDIEQLEY
SRDCFCEDHCDKCSVVLTLQAFGESESTTNVYSKDLVIVS
NLMGRNIGHPIIQDKEGNGVLICKLRKGQELKLTCVAKKG
IAKEHAKWGPAAAIEFEYDPWNKLKHTDYWYEQDSAKEWP
QSKNCEYEDPPNEGDPFDYKAQADTFYMNVESVGSIPVDQ
VVVRGIDTLQKKVASILLALTQMDQD
E:  QENERNISRLWRAFRTVKEMVKDRGYFITQEEVELPLEDF
KAKYCDSMGRPQRKMMSFQANPTEESISKFPDMGSLWVEF
CDEPSVGVKTMKTFVIHIQEKNFQTGIFVYQNNITPSAMK
LVPSIPPATIETFNEAALVVNITHHELVPKHIRLSSDEKR
ELLKRYRLKESQLPRIQRADPVALYLGLKRGEVVKIIRKS
ETSGRYASYRICM
F:  KAIPKDQRATTPYMTKYERARILGTRALQISMNAPVFVDL
EGETDPLRIAMKELAEKKIPLVIRRYLPDGSFEDWSVEEL
IVDL
H:  NTLFDDIFQVSEVDPGRYNKVCRIEAASTTQDQCKLTLDI
NVELFPVAAQDSLTVTIASSLTRSWRPPQAGDRSLADDYD
YVMYGTAYKFEEVSKDLIAVYYSFGGLLMRLEGNYLNNLK
QENAYLLIRR
I:  TTFRFCRDCNNMLYPREDKENNRLLFECRTCSYVEEAGSP
LVYRHELITNIGETAGVVQDIGSDPTLPRSDRECPKCHSR
ENVFFQSQQRRKDTSMVLFFVCLSCSHIFTSDQKN
J:  MIVPVRCFSCGKVVGDKWESYLNLLQEDELDEGTALSRLG
LKRYCCRRMILTHVDLIEKFLRYNP
K:  MNAPDRFELFLLGEGESKLKIDPDTKAPNAVVITFEKEDH
TLGNLIRAELLNDRKVLFAAYKVEHPFFARFKLRIQTTEG
YDPKDALKNACNSIINKLGALKTNFETEWNLQTL
L:  LKYICAECSSKLSLSRTDAVRCKDCGHRILLKARTKRLVQ
FEAR
Description


Functional site

1) chain A
residue 107
type
sequence C
description binding site for residue ZN A 1801
source : AC1

2) chain A
residue 108
type
sequence M
description binding site for residue ZN A 1801
source : AC1

3) chain A
residue 110
type
sequence C
description binding site for residue ZN A 1801
source : AC1

4) chain A
residue 148
type
sequence C
description binding site for residue ZN A 1801
source : AC1

5) chain A
residue 167
type
sequence C
description binding site for residue ZN A 1801
source : AC1

6) chain A
residue 67
type
sequence C
description binding site for residue ZN A 1802
source : AC2

7) chain A
residue 70
type
sequence C
description binding site for residue ZN A 1802
source : AC2

8) chain A
residue 77
type
sequence C
description binding site for residue ZN A 1802
source : AC2

9) chain A
residue 80
type
sequence H
description binding site for residue ZN A 1802
source : AC2

10) chain A
residue 481
type
sequence D
description binding site for residue MG A 1803
source : AC3

11) chain A
residue 483
type
sequence D
description binding site for residue MG A 1803
source : AC3

12) chain A
residue 485
type
sequence D
description binding site for residue MG A 1803
source : AC3

13) chain B
residue 1163
type
sequence C
description binding site for residue ZN B 1301
source : AC4

14) chain B
residue 1166
type
sequence C
description binding site for residue ZN B 1301
source : AC4

15) chain B
residue 1182
type
sequence C
description binding site for residue ZN B 1301
source : AC4

16) chain B
residue 1185
type
sequence C
description binding site for residue ZN B 1301
source : AC4

17) chain C
residue 86
type
sequence C
description binding site for residue ZN C 401
source : AC5

18) chain C
residue 88
type
sequence C
description binding site for residue ZN C 401
source : AC5

19) chain C
residue 92
type
sequence C
description binding site for residue ZN C 401
source : AC5

20) chain C
residue 95
type
sequence C
description binding site for residue ZN C 401
source : AC5

21) chain I
residue 7
type
sequence C
description binding site for residue ZN I 201
source : AC6

22) chain I
residue 10
type
sequence C
description binding site for residue ZN I 201
source : AC6

23) chain I
residue 29
type
sequence C
description binding site for residue ZN I 201
source : AC6

24) chain I
residue 32
type
sequence C
description binding site for residue ZN I 201
source : AC6

25) chain I
residue 75
type
sequence C
description binding site for residue ZN I 202
source : AC7

26) chain I
residue 78
type
sequence C
description binding site for residue ZN I 202
source : AC7

27) chain I
residue 103
type
sequence C
description binding site for residue ZN I 202
source : AC7

28) chain I
residue 106
type
sequence C
description binding site for residue ZN I 202
source : AC7

29) chain J
residue 7
type
sequence C
description binding site for residue ZN J 101
source : AC8

30) chain J
residue 10
type
sequence C
description binding site for residue ZN J 101
source : AC8

31) chain J
residue 45
type
sequence C
description binding site for residue ZN J 101
source : AC8

32) chain J
residue 46
type
sequence C
description binding site for residue ZN J 101
source : AC8

33) chain L
residue 31
type
sequence C
description binding site for residue ZN L 101
source : AC9

34) chain L
residue 34
type
sequence C
description binding site for residue ZN L 101
source : AC9

35) chain L
residue 48
type
sequence C
description binding site for residue ZN L 101
source : AC9

36) chain L
residue 51
type
sequence C
description binding site for residue ZN L 101
source : AC9

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

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

39) chain A
residue 485
type ZN_FING
sequence D
description C4-type
source Swiss-Prot : SWS_FT_FI1

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

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

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

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

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

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

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

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

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

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

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

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

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

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

54) 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

55) 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

56) 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

57) 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

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

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

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

61) 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

62) 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

63) 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

64) 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

65) 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

66) 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

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

68) 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

69) 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

70) 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

71) 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

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


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