eF-site ID 3gtl-ABCEFHIJKLNRT
PDB Code 3gtl
Chain A, B, C, E, F, H, I, J, K, L, N, R, T

click to enlarge
Title Backtracked RNA polymerase II complex with 13mer with G<>U mismatch
Classification TRANSCRIPTION, TRANSFERASE/DNA-RNA HYBRID
Compound DNA-directed RNA polymerase II subunit RPB1
Source ORGANISM_COMMON: yeast; ORGANISM_SCIENTIFIC: Saccharomyces cerevisiae;
Sequence A:  GQQYSSAPLRTVKEVQFGLFSPEEVRAISVAKIRFPETMD
ETQTRAKIGGLNDPRLGSIDRNLKCQTCQEGMNECPGHFG
HIDLAKPVFHVGFIAKIKKVCECVCMHCGKLLLDEHNELM
RQALAIKDSKKRFAAIWTLCKTKMVCETDVPSLVSRGGCG
NTQPTIRKDGLKLVGSWKLRVLSTEEILNIFKHISVKDFT
SLGFNEVFSRPEWMILTCLPVPPPPVRPSISFNESQRGED
DLTFKLADILKANISLETLEHNGAPHHAIEEAESLLQFHV
ATYMDNDIAGQPQALQKSGRPVKSIRARLKGKEGRIRGNL
MGKRVDFSARTVISGDPNLELDQVGVPKSIAKTLTYPEVV
TPYNIDRLTQLVRNGPNEHPGAKYVIRDSGDRIDLRYSKR
AGDIQLQYGWKVERHIMDNDPVLFNRQPSLHKMSMMAHRV
KVIPYSTFRLNLSVTSPYNADFDGDEMNLHVPQSEETRAE
LSQLCAVPLQIVSPQSNKPCMGIVQDTLCGIRKLTLRDTF
IELDQVLNMLYWVPDWDGVIPTPAIIKPKPLWSGKQILSV
AIPNGIHLQRFDEGTTLLSPKDNGMLIIDGQIIFGVVEKK
TVGSSNGGLIHVVTREKGPQVCAKLFGNIQKVVNFWLLHN
GFSTGIGDTIADGPTMREITETIAEAKKKVLDVTKEAQAN
LLTAKHGMTLRESFEDNVVRFLNEARDKAGRLAEVNLKDL
NNVKQMVMAGSKGSFINIAQMSACVGQQSVEGKRIAFGFV
DRTLPHFSKDDYSPESKGFVENSYLRGLTPQEFFFHAMGG
REGLIDTAVKTAETGYIQRRLVKALEDIMVHYDNTTRNSL
GNVIQFIYGEDGMDAAHIEKQSLDTIGGSDAAFEKRYRVD
LLNTDHTLDPSLLESGSEILGDLKLQVLLDEEYKQLVKDR
KFLREVFVDGEANWPLPVNIRRIIQNAQQTFHIDHTKPSD
LTIKDIVLGVKDLQENLLVLRGKNEIIQNAQRDAVTLFCC
LLRSRLATRRVLQEYRLTKQAFDWVLSNIEAQFLRSVVHP
GEMVGVLAAQSIGEPATQMTLKKVTSGVPRLKEILNVAKN
MKTPSLTVYLEPGHAADQEQAKLIRSAIEHTTLKSVTIAS
EIYYDPDPRSTVIPEDEEIIQLHFSLQQSPWLLRLELDRA
AMNDKDLTMGQVGERIKQTFKNDLFVIWSEDNDEKLIIRC
RVVAEEDHMLKKIENTMLENITLRGVENIERVVMMKYDRK
VPSPTGEYVKEPEWVLETDGVNLSEVMTVPGIDPTRIYTN
SFIDIMEVLGIEAGRAALYKEVYNVIASDGSYVNYRHMAL
LVDVMTTQGGLTSVTRHGFNRSNTGALMRCSFEETVEILF
EAGASAELDDCRGVSENVILGQMAPIGTGAFDVMI
B:  DESAPITAEDSWAVISAFFREKGLVSQQLDSFNQFVDYTL
QDIICEDSTLIISFGKIYVTKPMVNESDGVTHALYPQEAR
LRNLTYSSGLFVDVKKKVFIGRLPIMLRSKNCYLSEATES
DLYKLKECPFDMGGYFIINGSEKVLIAQERSAGNIVQVFK
KAAPSPISHVAEIRSALEKGSRFISTLQVKLYGREGSSAR
TIKATLPYIKQDIPIVIIFRALGIIPDGEILEHICYDVND
WQMLEMLKPCVEDGFVIQDRETALDFIGKEKRIQYAKDIL
QKEFLPHITQLEGFESRKAFFLGYMINRLLLCALDRKDQD
DRDHFGKKRLDLAGPLLAQLFKTLFKKLTKDIFRYMQRTV
ELAINAKTITSGLKYALATGNWGEQKKAMSSRAGVSQVLN
RYTYSSTLSHLRRTNTPIAKPRQLHNTHWGLVCPAETPEG
QACGLVKNLSLMSCISVGTDPMPIITFLSEWGMEPLEDYV
PHQSPDATRVFVNGVWHGVHRNPARLMETLRTLRRKGDIN
PEVSMIRDIREKELKIFTDAGRVYRPLFIVEDDESLGHKE
LKVRKGHIAKLMATEYQDEYTWSSLLNEGLVEYIDAEEEE
SILIAMQPEDLEPAEADVDPAKRIRVSHHATTFTHCEIHP
SMILGVAASIIPFPDHNQSPRNTYQSAMGKQAMGVFLTNY
NVRMDTMANILYYPQKPLGTTRAMEYLKFRELPAGQNAIV
AIACYSGYNQEDSMIMNQSSIDRGLFRSLFFRSYMDQEKK
YGMSITETFEKPQRTNTLRMKHGTYDKLDDDGLIAPGVRV
SGEDVIIGKTTPISSKRDASTPLRSTENGIVDQVLVTTNQ
DGLKFVKVRVRTTKIPQIGDKFASRHGQKGTIGITYRRED
MPFTAEGIVPDLIINPHAIPSRMTVAHLIECLLSKVAALS
GNEGDASPFTDITVEGISKLLREHGYQSRGFEVMYNGHTG
KKLMAQIFFGPTYYQRLRHMVDDKIHARARGPMQVLTRQP
VEGRSRDGGLRFGEMERDCMIAHGAASFLKERLMEASDAF
RVHICGICGLMTVIAKLNHNQFECKGCDNKIDIYQIHIPY
AAKLLFQELMAMNITPRLYTDRSRDF
C:  EEGPQVKIREASKDNVDFILSNVDLAMANSLRRVMIAEIP
TLAIDSVEVETNTTVLADEFIAHRLGLIPLQSMDIEQLEY
SRDCFCEDHCDKCSVVLTLQAFGESESTTNVYSKDLVIVS
NLMGRNIGHPIIQDKEGNGVLICKLRKGQELKLTCVAKKG
IAKEHAKWGPAAAIEFEYDPWNKLKHTDYWYEQDSAKEWP
QSKNCEYEDPPNEGDPFDYKAQADTFYMNVESVGSIPVDQ
VVVRGIDTLQKKVASILLALTQMDQD
E:  DQENERNISRLWRAFRTVKEMVKDRGYFITQEEVELPLED
FKAKYCDSMGRPQRKMMSFQANPTEESISKFPDMGSLWVE
FCDEPSVGVKTMKTFVIHIQEKNFQTGIFVYQNNITPSAM
KLVPSIPPATIETFNEAALVVNITHHELVPKHIRLSSDEK
RELLKRYRLKESQLPRIQRADPVALYLGLKRGEVVKIIRK
SETSGRYASYRICM
F:  KAIPKDQRATTPYMTKYERARILGTRALQISMNAPVFVDL
EGETDPLRIAMKELAEKKIPLVIRRYLPDGSFEDWSVEEL
IVDL
H:  SNTLFDDIFQVSEVDPGRYNKVCRIEAASTTQDQCKLTLD
INVELFPVAAQDSLTVTIASSLTRSWRPPQAGDRSLADDY
DYVMYGTAYKFEEVSKDLIAVYYSFGGLLMRLEGNYRNLN
NLKQENAYLLIRR
I:  TTFRFCRDCNNMLYPREDKENNRLLFECRTCSYVEEAGSP
LVYRHELITNIGETAGVVQDIGSDPTLPRSDRECPKCHSR
ENVFFQSQQRRKDTSMVLFFVCLSCSHIFTSDQKNKRTQ
J:  MIVPVRCFSCGKVVGDKWESYLNLLQEDELDEGTALSRLG
LKRYCCRRMILTHVDLIEKFLRYNP
K:  MNAPDRFELFLLGEGESKLKIDPDTKAPNAVVITFEKEDH
TLGNLIRAELLNDRKVLFAAYKVEHPFFARFKLRIQTTEG
YDPKDALKNACNSIINKLGALKTNFETEWNLQTL
L:  ATLKYICAECSSKLSLSRTDAVRCKDCGHRILLKARTKRL
VQFEAR
N:  CTGCTTATCGGTAG
R:  AUCGAGAGGAUU
T:  CTACCGATAAGCAGACGATCCTCTCGAT
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 148
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1734
source : AC1
4) chain A
residue 167
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1734
source : AC1
5) chain A
residue 67
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1735
source : AC2
6) chain A
residue 70
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1735
source : AC2
7) chain A
residue 77
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1735
source : AC2
8) chain A
residue 80
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 1735
source : AC2
9) chain B
residue 1163
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 1307
source : AC3
10) chain B
residue 1166
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 1307
source : AC3
11) chain B
residue 1182
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 1307
source : AC3
12) chain B
residue 1185
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 1307
source : AC3
13) chain C
residue 86
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 319
source : AC4
14) chain C
residue 88
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 319
source : AC4
15) chain C
residue 92
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 319
source : AC4
16) chain C
residue 95
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 319
source : AC4
17) chain I
residue 7
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 203
source : AC5
18) chain I
residue 10
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 203
source : AC5
19) chain I
residue 29
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 203
source : AC5
20) chain I
residue 31
type
sequence T
description BINDING SITE FOR RESIDUE ZN I 203
source : AC5
21) chain I
residue 32
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 203
source : AC5
22) chain I
residue 75
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 204
source : AC6
23) chain I
residue 78
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 204
source : AC6
24) chain I
residue 103
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 204
source : AC6
25) chain I
residue 106
type
sequence C
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 10
type
sequence C
description BINDING SITE FOR RESIDUE ZN J 101
source : AC7
28) chain J
residue 45
type
sequence C
description BINDING SITE FOR RESIDUE ZN J 101
source : AC7
29) chain J
residue 46
type
sequence C
description BINDING SITE FOR RESIDUE ZN J 101
source : AC7
30) chain L
residue 31
type
sequence C
description BINDING SITE FOR RESIDUE ZN L 105
source : AC8
31) chain L
residue 34
type
sequence C
description BINDING SITE FOR RESIDUE ZN L 105
source : AC8
32) chain L
residue 48
type
sequence C
description BINDING SITE FOR RESIDUE ZN L 105
source : AC8
33) chain L
residue 51
type
sequence C
description BINDING SITE FOR RESIDUE ZN L 105
source : AC8
34) chain A
residue 481
type
sequence D
description BINDING SITE FOR RESIDUE MG A 1736
source : AC9
35) chain A
residue 483
type
sequence D
description BINDING SITE FOR RESIDUE MG A 1736
source : AC9
36) chain A
residue 485
type
sequence D
description BINDING SITE FOR RESIDUE MG A 1736
source : AC9
37) chain R
residue 10
type
sequence A
description BINDING SITE FOR RESIDUE MG A 1736
source : AC9
38) chain R
residue 11
type
sequence U
description BINDING SITE FOR RESIDUE MG A 1736
source : AC9
39) 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
40) 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
41) 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
42) 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
43) 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
44) 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
45) 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
46) 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
47) chain I
residue 40
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:18407956
source Swiss-Prot : SWS_FT_FI5
48) chain B
residue 977-989
type prosite
sequence GDKFASRHGQKGT
description RNA_POL_BETA RNA polymerases beta chain signature. GdKFASrHGQKGT
source prosite : PS01166
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 J
residue 2-11
type prosite
sequence IVPVRCFSCG
description RNA_POL_N_8KD RNA polymerases N / 8 Kd subunits signature. IVPVrCFSCG
source prosite : PS01112
51) 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
52) 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
53) 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
54) chain I
residue 75-110
type prosite
sequence CPKCHSRENVFFQSQQRRKDTSMVLFFVCLSCSHIF
description ZF_TFIIS_1 Zinc finger TFIIS-type signature. CpkChsrenvffqSQQRRkDTSmvlffvCls...CshiF
source prosite : PS00466
55) 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
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 483
type ZN_FING
sequence D
description C4-type
source Swiss-Prot : SWS_FT_FI1
60) chain A
residue 485
type ZN_FING
sequence D
description C4-type
source Swiss-Prot : SWS_FT_FI1
61) chain A
residue 107
type ZN_FING
sequence C
description C4-type
source Swiss-Prot : SWS_FT_FI1
62) chain A
residue 110
type ZN_FING
sequence C
description C4-type
source Swiss-Prot : SWS_FT_FI1
63) chain A
residue 148
type ZN_FING
sequence C
description C4-type
source Swiss-Prot : SWS_FT_FI1
64) chain A
residue 167
type ZN_FING
sequence C
description C4-type
source Swiss-Prot : SWS_FT_FI1
65) chain A
residue 481
type ZN_FING
sequence D
description C4-type
source Swiss-Prot : SWS_FT_FI1
66) chain L
residue 31-51
type ZN_FING
sequence CAECSSKLSLSRTDAVRCKDC
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 J
residue 10
type ZN_FING
sequence C
description C4-type
source Swiss-Prot : SWS_FT_FI1
69) chain J
residue 45
type ZN_FING
sequence C
description C4-type
source Swiss-Prot : SWS_FT_FI1
70) chain B
residue 1185
type BINDING
sequence C
description
source Swiss-Prot : SWS_FT_FI2
71) chain L
residue 34
type BINDING
sequence C
description
source Swiss-Prot : SWS_FT_FI2
72) chain L
residue 48
type BINDING
sequence C
description
source Swiss-Prot : SWS_FT_FI2
73) chain L
residue 51
type BINDING
sequence C
description
source Swiss-Prot : SWS_FT_FI2
74) chain L
residue 31
type BINDING
sequence C
description
source Swiss-Prot : SWS_FT_FI2

Display surface

Download
Links