eF-site ID 3i4n-ABCDEFGHIJKLNPT
PDB Code 3i4n
Chain A, B, C, D, E, F, G, H, I, J, K, L, N, P, T
Title 8-oxoguanine containing RNA polymerase II elongation complex E
Classification TRANSCRIPTION,TRANSFERASE/DNA-RNA HYBRID
Compound DNA-directed RNA polymerase II subunit RPB1
Source ORGANISM_COMMON: baker's yeast; ORGANISM_SCIENTIFIC: Saccharomyces cerevisiae;
Sequence A:  VGQQYSSAPLRTVKEVQFGLFSPEEVRAISVAKIRFPETM
DETQTRAKIGGLNDPRLGSIDRNLKCQTCQEGMNECPGHF
GHIDLAKPVFHVGFIAKIKKVCECVCMHCGKLLLDEHNEL
MRQALAIKDSKKRFAAIWTLCKTKMVCETDVPSEDDPTQL
VSRGGCGNTQPTIRKDGLKLVGSWKKDRATGDADEPELRV
LSTEEILNIFKHISVKDFTSLGFNEVFSRPEWMILTCLPV
PPPPVRPSISFNESQRGEDDLTFKLADILKANISLETLEH
NGAPHHAIEEAESLLQFHVATYMDNDIAGQPQALQKSGRP
VKSIRARLKGKEGRIRGNLMGKRVDFSARTVISGDPNLEL
DQVGVPKSIAKTLTYPEVVTPYNIDRLTQLVRNGPNEHPG
AKYVIRDSGDRIDLRYSKRAGDIQLQYGWKVERHIMDNDP
VLFNRQPSLHKMSMMAHRVKVIPYSTFRLNLSVTSPYNAD
FDGDEMNLHVPQSEETRAELSQLCAVPLQIVSPQSNKPCM
GIVQDTLCGIRKLTLRDTFIELDQVLNMLYWVPDWDGVIP
TPAIIKPKPLWSGKQILSVAIPNGIHLQRFDEGTTLLSPK
DNGMLIIDGQIIFGVVEKKTVGSSNGGLIHVVTREKGPQV
CAKLFGNIQKVVNFWLLHNGFSTGIGDTIADGPTMREITE
TIAEAKKKVLDVTKEAQANLLTAKHGMTLRESFEDNVVRF
LNEARDKAGRLAEVNLKDLNNVKQMVMAGSKGSFINIAQM
SACVGQQSVEGKRIAFGFVDRTLPHFSKDDYSPESKGFVE
NSYLRGLTPQEFFFHAMGGREGLIDTAVKTAETGYIQRRL
VKALEDIMVHYDNTTRNSLGNVIQFIYGEDGMDAAHIEKQ
SLDTIGGSDAAFEKRYRVDLLNTDHTLDPSLLESGSEILG
DLKLQVLLDEEYKQLVKDRKFLREVFVDGEANWPLPVNIR
RIIQNAQQTFHIDHTKPSDLTIKDIVLGVKDLQENLLVLR
GKNEIIQNAQRDAVTLFCCLLRSRLATRRVLQEYRLTKQA
FDWVLSNIEAQFLRSVVHPGEMVGVLAAQSIGEPATQMTL
KVTSGVPRLKEILNVAKNMKTPSLTVYLEPGHAADQEQAK
LIRSAIEHTTLKSVTIASEIYYDPDPRSTVIPEDEEIIQL
HFSLLDEQQSPWLLRLELDRAAMNDKDLTMGQVGERIKQT
FKNDLFVIWSEDNDEKLIIRCRVVRPKAEEDHMLKKIENT
MLENITLRGVENIERVVMMKYDRKVPSPTGEYVKEPEWVL
ETDGVNLSEVMTVPGIDPTRIYTNSFIDIMEVLGIEAGRA
ALYKEVYNVIASDGSYVNYRHMALLVDVMTTQGGLTSVTR
HGFNRSNTGALMRCSFEETVEILFEAGASAELDDCRGVSE
NVILGQMAPIGTGAFDVMIDEESLVKYMP
B:  DESAPITAEDSWAVISAFFREKGLVSQQLDSFNQFVDYTL
QDIICEDSTLIISFGKIYVTKPMVNESDGVTHALYPQEAR
LRNLTYSSGLFVDVKKRTYEKVFIGRLPIMLRSKNCYLSE
ATESDLYKLKECPFDMGGYFIINGSEKVLIAQERSAGNIV
QVFKKAAPSPISHVAEIRSALEKGSRFISTLQVKLYGREG
SSARTIKATLPYIKQDIPIVIIFRALGIIPDGEILEHICY
DVNDWQMLEMLKPCVEDGFVIQDRETALDFIGRRGTALGI
KKEKRIQYAKDILQKEFLPHITQLEGFESRKAFFLGYMIN
RLLLCALDRKDQDDRDHFGKKRLDLAGPLLAQLFKTLFKK
LTKDIFRYMQRTVELAINAKTITSGLKYALATGNWGEQKK
AMSSRAGVSQVLNRYTYSSTLSHLRRTNTPIGRDGKLAKP
RQLHNTHWGLVCPAETPEGQACGLVKNLSLMSCISVGTDP
MPIITFLSEWGMEPLEDYVPHQSPDATRVFVNGVWHGVHR
NPARLMETLRTLRRKGDINPEVSMIRDIREKELKIFTDAG
RVYRPLFIVEDDESLGHKELKVRKGHIAKLMATEYQDEYT
WSSLLNEGLVEYIDAEEEESILIAMQPEDLEPAEADVDPA
KRIRVSHHATTFTHCEIHPSMILGVAASIIPFPDHNQSPR
NTYQSAMGKQAMGVFLTNYNVRMDTMANILYYPQKPLGTT
RAMEYLKFRELPAGQNAIVAIACYSGYNQEDSMIMNQSSI
DRGLFRSLFFRSYMDQEKKYGMSITETFEKPQRTNTLRMK
HGTYDKLDDDGLIAPGVRVSGEDVIIGKTTPISSKRDAST
PLRSTENGIVDQVLVTTNQDGLKFVKVRVRTTKIPQIGDK
FASRHGQKGTIGITYRREDMPFTAEGIVPDLIINPHAIPS
RMTVAHLIECLLSKVAALSGNEGDASPFTDITVEGISKLL
REHGYQSRGFEVMYNGHTGKKLMAQIFFGPTYYQRLRHMV
DDKIHARARGPMQVLTRQPVEGRSRDGGLRFGEMERDCMI
AHGAASFLKERLMEASDAFRVHICGICGLMTVIAKLNHNQ
FECKGCDNKIDIYQIHIPYAAKLLFQELMAMNITPRLYTD
RSRDF
C:  MSEEGPQVKIREASKDNVDFILSNVDLAMANSLRRVMIAE
IPTLAIDSVEVETNTTVLADEFIAHRLGLIPLQSMDIEQL
EYSRDCFCEDHCDKCSVVLTLQAFGESESTTNVYSKDLVI
VSNLMGRNIGHPIIQDKEGNGVLICKLRKGQELKLTCVAK
KGIAKEHAKWGPAAAIEFEYDPWNKLKHTDYWYEQDSAKE
WPQSKNCEYEDPPNEGDPFDYKAQADTFYMNVESVGSIPV
DQVVVRGIDTLQKKVASILLALTQMDQDKV
D:  MNVSTSTFQTRRRRLKKVEEEENAATLQLGQEFQLKQINH
QGEEEELIALNLSEARLVIKEALVERRRAFKRSQKKSETR
EKELESIDVLLEQTTGGNNKDLKNTMQYLTNFSRFRDQET
VGAVIQLLKSTGLHPFEVAQLGSLACDTADEAKTLIPSLN
NKISDDELERILKELSNLETLY
E:  DQENERNISRLWRAFRTVKEMVKDRGYFITQEEVELPLED
FKAKYCDSMGRPQRKMMSFQANPTEESISKFPDMGSLWVE
FCDEPSVGVKTMKTFVIHIQEKNFQTGIFVYQNNITPSAM
KLVPSIPPATIETFNEAALVVNITHHELVPKHIRLSSDEK
RELLKRYRLKESQLPRIQRADPVALYLGLKRGEVVKIIRK
SETSGRYASYRICM
F:  TLKEKAIPKDQRATTPYMTKYERARILGTRALQISMNAPV
FVDLEGETDPLRIAMKELAEKKIPLVIRRYLPDGSFEDWS
VEELIVDL
G:  MFFIKDLSLNITLHPSFFGPRMKQYLKTKLLEEVEGSCTG
KFGYILCVLDYDNIDIQRGRILPTDGSAEFNVKYRAVVFK
PFKGEVVDGTVVSCSQHGFEVQVGPMKVFVTKHLMPQDLT
FNAGSNPPSYQSSEDVITIKSRIRVKIEGCISQVSSIHAI
GSIKEDYLGAI
H:  MSNTLFDDIFQVSEVDPGRYNKVCRIEAASTTQDQCKLTL
DINVELFPVAAQDSLTVTIASSLNLETRSWRPPQAGDRSL
ADDYDYVMYGTAYKFEEVSKDLIAVYYSFGGLLMRLEGNY
RNLNNLKQENAYLLIRR
I:  MTTFRFCRDCNNMLYPREDKENNRLLFECRTCSYVEEAGS
PLVYRHELITNIGETAGVVQDIGSDPTLPRSDRECPKCHS
RENVFFQSQQRRKDTSMVLFFVCLSCSHIFTSDQKNK
J:  MIVPVRCFSCGKVVGDKWESYLNLLQEDELDEGTALSRLG
LKRYCCRRMILTHVDLIEKFLRYNP
K:  MNAPDRFELFLLGEGESKLKIDPDTKAPNAVVITFEKEDH
TLGNLIRAELLNDRKVLFAAYKVEHPFFARFKLRIQTTEG
YDPKDALKNACNSIINKLGALKTNFETEWNLQTLAA
L:  TATLKYICAECSSKLSLSRTDAVRCKDCGHRILLKARTKR
LVQFEAR
N:  AGTACTTGAGC
P:  UUCCAGGCAU
T:  CTCAAGTACTTAXGCCXGGT
Description


Functional site
1) chain A
residue 481
type
sequence D
description BINDING SITE FOR RESIDUE MG A 2458
source : AC1
2) chain A
residue 483
type
sequence D
description BINDING SITE FOR RESIDUE MG A 2458
source : AC1
3) chain A
residue 485
type
sequence D
description BINDING SITE FOR RESIDUE MG A 2458
source : AC1
4) chain P
residue 10
type
sequence A
description BINDING SITE FOR RESIDUE MG A 2458
source : AC1
5) chain P
residue 11
type
sequence U
description BINDING SITE FOR RESIDUE MG A 2458
source : AC1
6) chain A
residue 107
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 2456
source : AC2
7) chain A
residue 108
type
sequence M
description BINDING SITE FOR RESIDUE ZN A 2456
source : AC2
8) chain A
residue 110
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 2456
source : AC2
9) chain A
residue 148
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 2456
source : AC2
10) chain A
residue 167
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 2456
source : AC2
11) chain A
residue 67
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 2457
source : AC3
12) chain A
residue 70
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 2457
source : AC3
13) chain A
residue 77
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 2457
source : AC3
14) chain A
residue 80
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 2457
source : AC3
15) chain B
residue 1163
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 2225
source : AC4
16) chain B
residue 1166
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 2225
source : AC4
17) chain B
residue 1182
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 2225
source : AC4
18) chain B
residue 1185
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 2225
source : AC4
19) chain C
residue 86
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 1269
source : AC5
20) chain C
residue 88
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 1269
source : AC5
21) chain C
residue 92
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 1269
source : AC5
22) chain C
residue 95
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 1269
source : AC5
23) chain I
residue 7
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 1121
source : AC6
24) chain I
residue 10
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 1121
source : AC6
25) chain I
residue 29
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 1121
source : AC6
26) chain I
residue 32
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 1121
source : AC6
27) chain I
residue 75
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 1122
source : AC7
28) chain I
residue 78
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 1122
source : AC7
29) chain I
residue 103
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 1122
source : AC7
30) chain I
residue 106
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 1122
source : AC7
31) chain I
residue 108
type
sequence H
description BINDING SITE FOR RESIDUE ZN I 1122
source : AC7
32) chain J
residue 7
type
sequence C
description BINDING SITE FOR RESIDUE ZN J 1066
source : AC8
33) chain J
residue 10
type
sequence C
description BINDING SITE FOR RESIDUE ZN J 1066
source : AC8
34) chain J
residue 45
type
sequence C
description BINDING SITE FOR RESIDUE ZN J 1066
source : AC8
35) chain J
residue 46
type
sequence C
description BINDING SITE FOR RESIDUE ZN J 1066
source : AC8
36) chain L
residue 31
type
sequence C
description BINDING SITE FOR RESIDUE ZN L 1071
source : AC9
37) chain L
residue 34
type
sequence C
description BINDING SITE FOR RESIDUE ZN L 1071
source : AC9
38) chain L
residue 48
type
sequence C
description BINDING SITE FOR RESIDUE ZN L 1071
source : AC9
39) chain L
residue 51
type
sequence C
description BINDING SITE FOR RESIDUE ZN L 1071
source : AC9
40) chain B
residue 837
type catalytic
sequence D
description 788
source MCSA : MCSA1
41) chain A
residue 483
type catalytic
sequence D
description 788
source MCSA : MCSA1
42) chain A
residue 485
type catalytic
sequence D
description 788
source MCSA : MCSA1
43) chain I
residue 40
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:18407956
source Swiss-Prot : SWS_FT_FI5
44) 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
45) 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
46) chain I
residue 75-110
type prosite
sequence CPKCHSRENVFFQSQQRRKDTSMVLFFVCLSCSHIF
description ZF_TFIIS_1 Zinc finger TFIIS-type signature. CpkChsrenvffqSQQRRkDTSmvlffvCls...CshiF
source prosite : PS00466
47) 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
48) 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
49) 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
50) 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
51) chain B
residue 977-989
type prosite
sequence GDKFASRHGQKGT
description RNA_POL_BETA RNA polymerases beta chain signature. GdKFASrHGQKGT
source prosite : PS01166
52) chain L
residue 31-51
type ZN_FING
sequence CAECSSKLSLSRTDAVRCKDC
description C4-type
source Swiss-Prot : SWS_FT_FI1
53) chain A
residue 483
type ZN_FING
sequence D
description C4-type
source Swiss-Prot : SWS_FT_FI1
54) chain A
residue 485
type ZN_FING
sequence D
description C4-type
source Swiss-Prot : SWS_FT_FI1
55) chain J
residue 10
type ZN_FING
sequence C
description C4-type
source Swiss-Prot : SWS_FT_FI1
56) chain J
residue 45
type ZN_FING
sequence C
description C4-type
source Swiss-Prot : SWS_FT_FI1
57) chain J
residue 46
type ZN_FING
sequence C
description C4-type
source Swiss-Prot : SWS_FT_FI1
58) chain A
residue 107
type ZN_FING
sequence C
description C4-type
source Swiss-Prot : SWS_FT_FI1
59) chain A
residue 110
type ZN_FING
sequence C
description C4-type
source Swiss-Prot : SWS_FT_FI1
60) chain A
residue 148
type ZN_FING
sequence C
description C4-type
source Swiss-Prot : SWS_FT_FI1
61) chain A
residue 167
type ZN_FING
sequence C
description C4-type
source Swiss-Prot : SWS_FT_FI1
62) chain A
residue 481
type ZN_FING
sequence D
description C4-type
source Swiss-Prot : SWS_FT_FI1
63) chain L
residue 31
type BINDING
sequence C
description
source Swiss-Prot : SWS_FT_FI2
64) chain L
residue 34
type BINDING
sequence C
description
source Swiss-Prot : SWS_FT_FI2
65) chain L
residue 48
type BINDING
sequence C
description
source Swiss-Prot : SWS_FT_FI2
66) chain L
residue 51
type BINDING
sequence C
description
source Swiss-Prot : SWS_FT_FI2
67) chain B
residue 1185
type BINDING
sequence C
description
source Swiss-Prot : SWS_FT_FI2
68) 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
69) 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
70) 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
71) 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
72) 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
73) 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
74) 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
75) 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

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