eF-site ID 2r7z-ABCDEFGHIJKL
PDB Code 2r7z
Chain A, B, C, D, E, F, G, H, I, J, K, L
Title Cisplatin lesion containing RNA polymerase II elongation complex
Classification TRANSCRIPTION/DNA-RNA HYBRID
Compound 5'-D(*TP*AP*CP*TP*TP*GUP*CP*CP*CP*TP*CP*CP*TP*CP*AP*T)-3'
Source ORGANISM_COMMON: baker's yeast; ORGANISM_SCIENTIFIC: Saccharomyces cerevisiae;
Sequence A:  VGQQYSSAPLRTVKEVQFGLFSPEEVRAISVAKIRFPETM
DETQTRAKIGGLNDPRLGSIDRNLKCQTCQEGMNECPGHF
GHIDLAKPVFHVGFIAKIKKVCECVCMHCGKLLLDEHNEL
MRQALAIKDSKKRFAAIWTLCKTKMVCETDVPSEDDPTQL
VSRGGCGNTQPTIRKDGLKLVGSWKDEPELRVLSTEEILN
IFKHISVKDFTSLGFNEVFSRPEWMILTCLPVPPPPVRPS
ISFNESQRGEDDLTFKLADILKANISLETLEHNGAPHHAI
EEAESLLQFHVATYMDNDIAGQPQALQKSGRPVKSIRARL
KGKEGRIRGNLMGKRVDFSARTVISGDPNLELDQVGVPKS
IAKTLTYPEVVTPYNIDRLTQLVRNGPNEHPGAKYVIRDS
GDRIDLRYSKRAGDIQLQYGWKVERHIMDNDPVLFNRQPS
LHKMSMMAHRVKVIPYSTFRLNLSVTSPYNADFDGDEMNL
HVPQSEETRAELSQLCAVPLQIVSPQSNKPCMGIVQDTLC
GIRKLTLRDTFIELDQVLNMLYWVPDWDGVIPTPAIIKPK
PLWSGKQILSVAIPNGIHLQRFDEGTTLLSPKDNGMLIID
GQIIFGVVEKKTVGSSNGGLIHVVTREKGPQVCAKLFGNI
QKVVNFWLLHNGFSTGIGDTIADGPTMREITETIAEAKKK
VLDVTKEAQANLLTAKHGMTLRESFEDNVVRFLNEARDKA
GRLAEVNLKDLNNVKQMVMAGSKGSFINIAQMSACVGQQS
VEGKRIAFGFVDRTLPHFSKDDYSPESKGFVENSYLRGLT
PQEFFFHAMGGREGLIDTAVKTAETGYIQRRLVKALEDIM
VHYDNTTRNSLGNVIQFIYGEDGMDAAHIEKQSLDTIGGS
DAAFEKRYRVDLLNTDHTLDPSLLESGSEILGDLKLQVLL
DEEYKQLVKDRKFLREVFVDGEANWPLPVNIRRIIQNAQQ
TFHIDHTKPSDLTIKDIVLGVKDLQENLLVLRGKNEIIQN
AQRDAVTLFCCLLRSRLATRRVLQEYRLTKQAFDWVLSNI
EAQFLRSVVHPGEMVGVLAAQSIGEPATQMTLKKVTSGVP
RLKEILNVAKNMKTPSLTVYLEPGHAADQEQAKLIRSAIE
HTTLKSVTIASEIYYDPDPRSTVIPEDEEIIQLHFSLQQS
PWLLRLELDRAAMNDKDLTMGQVGERIKQTFKNDLFVIWS
EDNDEKLIIRCRVVAEEDHMLKKIENTMLENITLRGVENI
ERVVMMKYDRKVPSPTGEYVKEPEWVLETDGVNLSEVMTV
PGIDPTRIYTNSFIDIMEVLGIEAGRAALYKEVYNVIASD
GSYVNYRHMALLVDVMTTQGGLTSVTRHGFNRSNTGALMR
CSFEETVEILFEAGASAELDDCRGVSENVILGQMAPIGTG
AFDVMIDEESLVKYMP
B:  DESAPITAEDSWAVISAFFREKGLVSQQLDSFNQFVDYTL
QDIICEDSTLIISFGKIYVTKPMVNESDGVTHALYPQEAR
LRNLTYSSGLFVDVKKKVFIGRLPIMLRSKNCYLSEATES
DLYKLKECPFDMGGYFIINGSEKVLIAQERSAGNIVQVFK
KAAPSPISHVAEIRSALEKGSRFISTLQVKLYGREGSSAR
TIKATLPYIKQDIPIVIIFRALGIIPDGEILEHICYDVND
WQMLEMLKPCVEDGFVIQDRETALDFIGKEKRIQYAKDIL
QKEFLPHITQLEGFESRKAFFLGYMINRLLLCALDRKDQD
DRDHFGKKRLDLAGPLLAQLFKTLFKKLTKDIFRYMQRTV
ELAINAKTITSGLKYALATGNWGEQKKAMSSRAGVSQVLN
RYTYSSTLSHLRRTNTPIKLAKPRQLHNTHWGLVCPAETP
EGQACGLVKNLSLMSCISVGTDPMPIITFLSEWGMEPLED
YVPHQSPDATRVFVNGVWHGVHRNPARLMETLRTLRRKGD
INPEVSMIRDIREKELKIFTDAGRVYRPLFIVEDDESLGH
KELKVRKGHIAKLMATEYQDEYTWSSLLNEGLVEYIDAEE
EESILIAMQPEDLEPAEADVDPAKRIRVSHHATTFTHCEI
HPSMILGVAASIIPFPDHNQSPRNTYQSAMGKQAMGVFLT
NYNVRMDTMANILYYPQKPLGTTRAMEYLKFRELPAGQNA
IVAIACYSGYNQEDSMIMNQSSIDRGLFRSLFFRSYMDQE
KKYGMSITETFEKPQRTNTLRMKHGTYDKLDDDGLIAPGV
RVSGEDVIIGKTTPISSKRDASTPLRSTENGIVDQVLVTT
NQDGLKFVKVRVRTTKIPQIGDKFASRHGQKGTIGITYRR
EDMPFTAEGIVPDLIINPHAIPSRMTVAHLIECLLSKVAA
LSGNEGDASPFTDITVEGISKLLREHGYQSRGFEVMYNGH
TGKKLMAQIFFGPTYYQRLRHMVDDKIHARARGPMQVLTR
QPVEGRSRDGGLRFGEMERDCMIAHGAASFLKERLMEASD
AFRVHICGICGLMTVIAKLNHNQFECKGCDNKIDIYQIHI
PYAAKLLFQELMAMNITPRLYTDRSRDF
C:  EEGPQVKIREASKDNVDFILSNVDLAMANSLRRVMIAEIP
TLAIDSVEVETNTTVLADEFIAHRLGLIPLQSMDIEQLEY
SRDCFCEDHCDKCSVVLTLQAFGESESTTNVYSKDLVIVS
NLMGRNIGHPIIQDKEGNGVLICKLRKGQELKLTCVAKKG
IAKEHAKWGPAAAIEFEYDPWNKLKHTDYWYEQDSAKEWP
QSKNCEYEDPPNEGDPFDYKAQADTFYMNVESVGSIPVDQ
VVVRGIDTLQKKVASILLALTQMDQD
D:  STSTFQTRRRRLKKVEEEENAATLQLGQEFQLKQINHQGE
EEELIALNLSEARLVIKEALVERRRAFKRSQKKTREKELE
SIDVLLEQTTGGNNKDLKNTMQYLTNFSRFRDQETVGAVI
QLLKSTGLHPFEVAQLGSLACDTADEAKTLIPSLNNKISD
DELERILKELSNLETLY
E:  DQENERNISRLWRAFRTVKEMVKDRGYFITQEEVELPLED
FKAKYCDSMGRPQRKMMSFQANPTEESISKFPDMGSLWVE
FCDEPSVGVKTMKTFVIHIQEKNFQTGIFVYQNNITPSAM
KLVPSIPPATIETFNEAALVVNITHHELVPKHIRLSSDEK
RELLKRYRLKESQLPRIQRADPVALYLGLKRGEVVKIIRK
SETSGRYASYRICM
F:  KAIPKDQRATTPYMTKYERARILGTRALQISMNAPVFVDL
EGETDPLRIAMKELAEKKIPLVIRRYLPDGSFEDWSVEEL
IVDL
G:  MFFIKDLSLNITLHPSFFGPRMKQYLKTKLLEEVEGSCTG
KFGYILCVLDYDNIDIQRGRILPTDGSAEFNVKYRAVVFK
PFKGEVVDGTVVSCSQHGFEVQVGPMKVFVTKHLMPQDLT
FNAGSNPPSYQSSEDVITIKSRIRVKIEGCISQVSSIHAI
GSIKEDYLGAI
H:  SNTLFDDIFQVSEVDPGRYNKVCRIEAASTTQDQCKLTLD
INVELFPVAAQDSLTVTIASSLTRSWRPPQAGDRSLADDY
DYVMYGTAYKFEEVSKDLIAVYYSFGGLLMRLEGNYRNLN
NLKQENAYLLIRR
I:  TTFRFCRDCNNMLYPREDKENNRLLFECRTCSYVEEAGSP
LVYRHELITNIGETAGVVQDIGSDPTLPRSDRECPKCHSR
ENVFFQSQQRRKDTSMVLFFVCLSCSHIFTSDQKNKRTQ
J:  MIVPVRCFSCGKVVGDKWESYLNLLQEDELDEGTALSRLG
LKRYCCRRMILTHVDLIEKFLRYNP
K:  MNAPDRFELFLLGEGESKLKIDPDTKAPNAVVITFEKEDH
TLGNLIRAELLNDRKVLFAAYKVEHPFFARFKLRIQTTEG
YDPKDALKNACNSIINKLGALKTNFETEWNLQTL
L:  ATLKYICAECSSKLSLSRTDAVRCKDCGHRILLKARTKRL
VQFEAR
Description (1)  DNA-DIRECTED RNA POLYMERASE II (E.C.2.7.7.6)/DNA-DIRECTED RNA POLYMERASES POLYPEPTIDES/RNA


Functional site
1) chain A
residue 108
type
sequence M
description BINDING SITE FOR RESIDUE ZN A 1734
source : AC2
2) chain A
residue 110
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1734
source : AC2
3) chain A
residue 148
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1734
source : AC2
4) chain A
residue 167
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1734
source : AC2
5) chain A
residue 67
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1735
source : AC3
6) chain A
residue 70
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1735
source : AC3
7) chain A
residue 77
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1735
source : AC3
8) chain A
residue 80
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 1735
source : AC3
9) chain B
residue 1163
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 1307
source : AC4
10) chain B
residue 1166
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 1307
source : AC4
11) chain B
residue 1182
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 1307
source : AC4
12) chain B
residue 1185
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 1307
source : AC4
13) chain C
residue 86
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 319
source : AC5
14) chain C
residue 88
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 319
source : AC5
15) chain C
residue 91
type
sequence H
description BINDING SITE FOR RESIDUE ZN C 319
source : AC5
16) chain C
residue 92
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 319
source : AC5
17) chain C
residue 95
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 319
source : AC5
18) chain I
residue 7
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 203
source : AC6
19) chain I
residue 10
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 203
source : AC6
20) chain I
residue 29
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 203
source : AC6
21) chain I
residue 32
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 203
source : AC6
22) chain I
residue 75
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 204
source : AC7
23) chain I
residue 78
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 204
source : AC7
24) chain I
residue 106
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 204
source : AC7
25) chain I
residue 108
type
sequence H
description BINDING SITE FOR RESIDUE ZN I 204
source : AC7
26) chain J
residue 7
type
sequence C
description BINDING SITE FOR RESIDUE ZN J 101
source : AC8
27) chain J
residue 10
type
sequence C
description BINDING SITE FOR RESIDUE ZN J 101
source : AC8
28) chain J
residue 45
type
sequence C
description BINDING SITE FOR RESIDUE ZN J 101
source : AC8
29) chain J
residue 46
type
sequence C
description BINDING SITE FOR RESIDUE ZN J 101
source : AC8
30) chain L
residue 31
type
sequence C
description BINDING SITE FOR RESIDUE ZN L 105
source : AC9
31) chain L
residue 34
type
sequence C
description BINDING SITE FOR RESIDUE ZN L 105
source : AC9
32) chain L
residue 48
type
sequence C
description BINDING SITE FOR RESIDUE ZN L 105
source : AC9
33) chain L
residue 51
type
sequence C
description BINDING SITE FOR RESIDUE ZN L 105
source : AC9
34) chain A
residue 481
type
sequence D
description BINDING SITE FOR RESIDUE MG A 1736
source : BC1
35) chain A
residue 483
type
sequence D
description BINDING SITE FOR RESIDUE MG A 1736
source : BC1
36) chain A
residue 485
type
sequence D
description BINDING SITE FOR RESIDUE MG A 1736
source : BC1
37) 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
38) chain B
residue 977-989
type prosite
sequence GDKFASRHGQKGT
description RNA_POL_BETA RNA polymerases beta chain signature. GdKFASrHGQKGT
source prosite : PS01166
39) 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
40) 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
41) 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
42) 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
43) chain I
residue 75-110
type prosite
sequence CPKCHSRENVFFQSQQRRKDTSMVLFFVCLSCSHIF
description ZF_TFIIS_1 Zinc finger TFIIS-type signature. CpkChsrenvffqSQQRRkDTSmvlffvCls...CshiF
source prosite : PS00466
44) 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
45) chain B
residue 837
type catalytic
sequence D
description 788
source MCSA : MCSA1
46) chain A
residue 483
type catalytic
sequence D
description 788
source MCSA : MCSA1
47) chain A
residue 485
type catalytic
sequence D
description 788
source MCSA : MCSA1
48) chain I
residue 40
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:18407956
source Swiss-Prot : SWS_FT_FI5
49) 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
50) 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
51) 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
52) 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
53) 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
54) 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
55) 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
56) 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
57) chain A
residue 483
type ZN_FING
sequence D
description C4-type
source Swiss-Prot : SWS_FT_FI1
58) chain A
residue 485
type ZN_FING
sequence D
description C4-type
source Swiss-Prot : SWS_FT_FI1
59) chain A
residue 107
type ZN_FING
sequence C
description C4-type
source Swiss-Prot : SWS_FT_FI1
60) chain A
residue 110
type ZN_FING
sequence C
description C4-type
source Swiss-Prot : SWS_FT_FI1
61) chain A
residue 148
type ZN_FING
sequence C
description C4-type
source Swiss-Prot : SWS_FT_FI1
62) chain A
residue 167
type ZN_FING
sequence C
description C4-type
source Swiss-Prot : SWS_FT_FI1
63) chain A
residue 481
type ZN_FING
sequence D
description C4-type
source Swiss-Prot : SWS_FT_FI1
64) chain J
residue 45
type ZN_FING
sequence C
description C4-type
source Swiss-Prot : SWS_FT_FI1
65) chain J
residue 46
type ZN_FING
sequence C
description C4-type
source Swiss-Prot : SWS_FT_FI1
66) chain J
residue 10
type ZN_FING
sequence C
description C4-type
source Swiss-Prot : SWS_FT_FI1
67) chain L
residue 31-51
type ZN_FING
sequence CAECSSKLSLSRTDAVRCKDC
description C4-type
source Swiss-Prot : SWS_FT_FI1
68) chain L
residue 34
type BINDING
sequence C
description
source Swiss-Prot : SWS_FT_FI2
69) chain L
residue 48
type BINDING
sequence C
description
source Swiss-Prot : SWS_FT_FI2
70) chain L
residue 51
type BINDING
sequence C
description
source Swiss-Prot : SWS_FT_FI2
71) chain B
residue 1185
type BINDING
sequence C
description
source Swiss-Prot : SWS_FT_FI2
72) chain L
residue 31
type BINDING
sequence C
description
source Swiss-Prot : SWS_FT_FI2

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