eF-site ID 1r9s-ABCEFHIJKL
PDB Code 1r9s
Chain A, B, C, E, F, H, I, J, K, L
Title RNA POLYMERASE II STRAND SEPARATED ELONGATION COMPLEX, MATCHED NUCLEOTIDE
Classification TRANSCRIPTION/DNA-RNA HYBRID
Compound RNA strand
Source ORGANISM_COMMON: baker's yeast; ORGANISM_SCIENTIFIC: Saccharomyces cerevisiae;
Sequence A:  VGQQYSSAPLRTVKEVQFGLFSPEEVRAISVAKIRFPETM
DETQTRAKIGGLNDPRLGSIDRNLKCQTCQEGMNECPGHF
GHIDLAKPVFHVGFIAKIKKVCECVCMHCGKLLLDEHNEL
MRQALAIKDSKKRFAAIWTLCKTKMVCETDVPSLVSRGGC
GNTQPTIRKDGLKLVGSWKLRVLSTEEILNIFKHISVKDF
TSLGFNEVFSRPEWMILTCLPVPPPPVRPSEDDLTFKLAD
ILKANISLETLEHNGAPHHAIEEAESLLQFHVATYMDNDI
AGQPQAPVKSIRARLKGKEGRIRGNLMGKRVDFSARTVIS
GDPNLELDQVGVPKSIAKTLTYPEVVTPYNIDRLTQLVRN
GPNEHPGAKYVIRDSGDRIDLRYSKRAGDIQLQYGWKVER
HIMDNDPVLFNRQPSLHKMSMMAHRVKVIPYSTFRLNLSV
TSPYNADFDGDEMNLHVPQSEETRAELSQLCAVPLQIVSP
QSNKPCMGIVQDTLCGIRKLTLRDTFIELDQVLNMLYWVP
DWDGVIPTPAIIKPKPLWSGKQILSVAIPNGIHLQRFDEG
TTLLSPKDNGMLIIDGQIIFGVVEKKTVGSSNGGLIHVVT
REKGPQVCAKLFGNIQKVVNFWLLHNGFSTGIGDTIADGP
TMREITETIAEAKKKVLDVTKEAQANLLTAKHGMTLRESF
EDNVVRFLNEARDKAGRLAEVNLKDLNNVKQMVMAGSKGS
FINIAQMSACVGQQSVEGKRIAFGFVDRTLPHFSKDDYSP
ESKGFVENSYLRGLTPQEFFFHAMGGREGLIDTAVKTAET
GYIQRRLVKALEDIMVHYDNTTRNSLGNVIQFIYGEDGMD
AAHIEKQSLDTIGGSDAAFEKRYRVDLLNTDHTLDPSLLE
SGSEILGDLKLQVLLDEEYKQLVKDRKFLREVFVDGEANW
PLPVNIRRIIQNAQQTFHIDHTKPSDLTIKDIVLGVKDLQ
ENLLVLRGKNEIIQNAQRDAVTLFCCLLRSRLATRRVLQE
YRLTKQAFDWVLSNIEAQFLRSVVHPGEMVGVLAAQSIGE
PATQMTLKKVTSGVPRLKEILNVAKNMKTPSLTVYLEPGH
AADQEQAKLIRSAIEHTTLKSVTIASEIYYDPDPRSTVIP
EDEEIIQLHFSLQQSPWLLRLELDRAAMNDKDLTMGQVGE
RIKQTFKNDLFVIWSEDNDEKLIIRCRVVAEEDHMLKKIE
NTMLENITLRGVENIERVVMMKYDRKVPSPTGEYVKEPEW
VLETDGVNLSEVMTVPGIDPTRIYTNSFIDIMEVLGIEAG
RAALYKEVYNVIASDGSYVNYRHMALLVDVMTTQGGLTSV
TRHGFNRSNTGALMRCSFEETVEILFEAGASAELDDCRGV
SENVILGQMAPIGTGAFDVMI
B:  DESAPITAEDSWAVISAFFREKGLVSQQLDSFNQFVDYTL
QDIICEDSTLIISFGKIYVTKPMVNESDGVTHALYPQEAR
LRNLTYSSGLFVDVKKKVFIGRLPIMLRSKNCYLSEATES
DLYKLKECPFDMGGYFIINGSEKVLIAQERSAGNIVQVFK
KAAPSPISHVAEIRSALEKGSRFISTLQVKLYGREGSSAR
TIKATLPYIKQDIPIVIIFRALGIIPDGEILEHICYDVND
WQMLEMLKPCVEDGFVIQDRETALDFIGKEKRIQYAKDIL
QKEFLPHITQLEGFESRKAFFLGYMINRLLLCALDRKDQD
DRDHFGKKRLDLAGPLLAQLFKTLFKKLTKDIFRYMQRTV
ELAINAKTITSGLKYALATGNWGAGVSQVLNRYTYSSTLS
HLRRTNTPIAKPRQLHNTHWGLVCPAETPEGQACGLVKNL
SLMSCISVGTDPMPIITFLSEWGMEPLEDYVPHQSPDATR
VFVNGVWHGVHRNPARLMETLRTLRRKGDINPEVSMIRDI
REKELKIFTDAGRVYRPLFIVEDDESLGHKELKVRKGHIA
KLMATEYQDEYTWSSLLNEGLVEYIDAEEEESILIAMQPE
DLEPAEADVDPAKRIRVSHHATTFTHCEIHPSMILGVAAS
IIPFPDHNQSPRNTYQSAMGKQAMGVFLTNYNVRMDTMAN
ILYYPQKPLGTTRAMEYLKFRELPAGQNAIVAIACYSGYN
QEDSMIMNQSSIDRGLFRSLFFRSYMDQEKKYGMSITETF
EKPQRTNTLRMKHGTYDKLDDDGLIAPGVRVSGEDVIIGK
TTPISSKRDASTPLRSTENGIVDQVLVTTNQDGLKFVKVR
VRTTKIPQIGDKFASRHGQKGTIGITYRREDMPFTAEGIV
PDLIINPHAIPSRMTVAHLIECLLSKVAALSGNEGDASPF
TDITVEGISKLLREHGYQSRGFEVMYNGHTGKKLMAQIFF
GPTYYQRLRHMVDDKIHARARGPMQVLTRQPVEGRSRDGG
LRFGEMERDCMIAHGAASFLKERLMEASDAFRVHICGICG
LMTVIAKLNHNQFECKGCDNKIDIYQIHIPYAAKLLFQEL
MAMNITPRLYTDRSRDF
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
Description


Functional site

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

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

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

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

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

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

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

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

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

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

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

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

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

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

15) chain I
residue 7
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 203
source : AC5

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 31
type
sequence T
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 103
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 204
source : AC6

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

39) chain A
residue 446
type
sequence R
description BINDING SITE FOR RESIDUE UTP R 3000
source : BC2

40) chain A
residue 483
type
sequence D
description BINDING SITE FOR RESIDUE UTP R 3000
source : BC2

41) chain B
residue 766
type
sequence R
description BINDING SITE FOR RESIDUE UTP R 3000
source : BC2

42) chain B
residue 769
type
sequence Y
description BINDING SITE FOR RESIDUE UTP R 3000
source : BC2

43) chain B
residue 987
type
sequence K
description BINDING SITE FOR RESIDUE UTP R 3000
source : BC2

44) chain B
residue 1020
type
sequence R
description BINDING SITE FOR RESIDUE UTP R 3000
source : BC2

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 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

49) 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

50) 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

51) 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

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

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

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

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

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

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

58) 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

59) 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

60) 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

61) 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

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

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

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

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

66) chain J
residue 45
type ZN_FING
sequence C
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 A
residue 107
type ZN_FING
sequence C
description C4-type
source Swiss-Prot : SWS_FT_FI1

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

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

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

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

73) 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

74) 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

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

76) 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

77) 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

78) 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

79) 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

80) 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