eF-site ID 4c3h-ABCDEFGHIJKLMN
PDB Code 4c3h
Chain A, B, C, D, E, F, G, H, I, J, K, L, M, N

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Title Structure of 14-subunit RNA polymerase I at 3.27 A resolution, crystal form C2-93
Classification TRANSCRIPTION
Compound DNA-DIRECTED RNA POLYMERASE I SUBUNIT RPA190
Source ORGANISM_COMMON: BAKER'S YEAST; ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
Sequence A:  MDISKPVGSEITSVDFGILTAKEIRNLSAKQITNPTVLDN
LGHPVSGGLYDLALGAFLRNLCSTCGLDEKFCPGHQGHIE
LPVPCYNPLFFNQLYIYLRASCLFCHHFRLKSVEVHRYAC
KLRLLQYGLIDESYKLDEITLDISSTLLNELKSKRSEYVD
MAIAKALSDGRTTERGSFTATVNDERKKLVHEFHKKLLSR
GKCDNCGMFSPKFRKDGFTKIFETALNEKQITNNRVKGFI
RQDMISTYILSTEVKNILDTVFRKEQCVLQYVFHSRPNLS
RKLVKADSFFMDVLVVPPTRFRLPSKLGEEVHENSQNQLL
SKVLTTSLLIRDLNDDLSKLKVSLEDRRVIFSRLMNAFVT
IQNDVNAFIDSTKAQGRTVPIPGVKQALEKKEGLFRKHMM
GKRVNYAARSVISPDPNIETNEIGVPPVFAVKLTYPEPVT
AYNIAELRQAVINGPDKWPGATQIQNEDGSLVSLIGMSVE
QRKALANQLLTPSSNVSTHTLNKKVYRHIKNRDVVLMNRQ
PTLHKASMMGHKVRVLPNEKTLRLHYANTGAYNADFDGDE
MNMHFPQNENARAEALNLANTDSQYLTPTSGSPVRGLIQD
HISAGVWLTSKDSFFTREQYQQYIYGCIRPEDGHTTRSKI
VTLPPTIFKPYPLWTGKQIITTVLLNVTPPDMPGINLISK
NKIKNEYWGKGSLENEVLFKDGALLCGILDKSQYGASKYG
IVHSLHEVYGPEVAAKVLSVLGRLFTNYITATAFTCGMDD
LRLTAEGNKWRTDILKTSVDTGREAAAEVTNLDKDTPADD
PELLKRLQEILRDNNKSGILDAVTSSKVNAITSQVVSKCV
PDGTMKKFPCNSMQAMALSGAKGSNVNVSQIMCLLGQQAL
EGRRVPVMVSGKTLPSFKPYETDAMAGGYVKGRFYSGIKP
QEYYFHCMAGREGLIDTAVKTSRSGYLQRCLTKQLEGVHV
SYDNSIRDADGTLVQFMYGGDAIDITKESHMTQFEFCLDN
YYALLKKYNPSALIEHLDVESALKYSKKTLKYRKKHSKEP
HYKQSVKYDPVLAKYNPAKYLGSVSENFQDKLESFLDKNS
KGVNEKKFRALMQLKYMRSLINPGEAVGIIASQSVGEPST
QMTLNTFNVTLGIPRLREIVMTASAAIKTPQMTLPIWNDV
SDEQADTFCKSISKVLLSEVIDKVIVTETTGTARSYVIHM
RFFDNNEYSEEYDVSKEELQNVISNQFIHLLEAAIVKEIK
KQKRTTGPDIGVAVPRLQNSKRLEEDNDEEQSHKKTKQAV
SYDEPDEDEIETMREAENMNKVQRDRQSAIISHHRFITKY
NFDDESGKWCEFKLELAADTEKLLMVNIVEEICRKSIIRQ
IPHIDRCVHPEPENGKRVLVTEGVNFQAMWDQEAFIDVDG
ITSNDVAAVLKTYGVEAARNTIVNEINNVFSRYAISVSFR
HLDLIADMMTRQGTYLAFNRQGMETSTSSFMKMSYETTCQ
FLTKAVLDNEREQLDSPSARIVVGKLNNVGTGSFDVLAKV
PNA
B:  RTADFRTLERESRFINPPKDKSAFPLLQEAVQPHIGSFNA
LTEGPDGGLLNLGVKDIGEKVIFDGKPLNSEEISNSGYLG
NKLSVSVEQVSIAKPMSNDSAVERKVYPSESRQRLTSYRG
KLLLKLKWSVNNGEENLFEVRDCGGLPVMLQSNRCHLNKM
SPYELVQHKEESDEIGGYFIVNGIEKLIRMLIVQRRNHPM
AIIRPSFANRGASYSHYGIQIRSVRPDQTSQTNVLHYLND
GQVTFRFSWRKNEYLVPVVMILKALCHTSDREIFDGIIGN
DVKDSFLTDRLELLLRGFKKRYPHLQNRTQVLQYLGDKFR
VVFQASPDQSDLEVGQEVLDRIVLVHLGKDGSQDKFRMLL
FMIRKLYSLVAGECSPDNPDATQHQEVLLGGFLYGMILKE
KIDEYLQNIIAQVRMDINRGMAINFKDKRYMSRVLMRVNE
NIGSKMQYFLSTGNLVSQSGLDLQQVSGYTVVAEKINFYR
FISHFRMVHRGSFFAQLKTTTVRKLLPESWGFLCPVHTPD
GSPCGLLNHFAHKCRISTQQSDVSRIPSILYSLGVAPASH
TFAAGPSLCCVQIDGKIIGWVSHEQGKIIADTLRYWKVEG
KTPGLPIDLEIGYVPPSTRGQYPGLYLFGGHSRMLRPVRY
LPLDKEDIVGPFEQVYMNIAVTPQEIQNNVHTHVEFTPTN
ILSILANLTPFSDFNQSPRNMYQCQMGKQTMGTPGVALCH
RSDNKLYRLQTGQTPIVKANLYDDYGMDNFPNGFNAVVAV
ISYTGYDMDDAMIINKSADERGFGYGTMYKTEKVDLALDP
ITQHFGFGNDEWPKEWLEKLDEDGLPYIGTYVEEGDPICA
YFDDTLNKTKIKTYHSSEPAYIEEVNLIGDESNKFQELQT
VSIKYRIRRTPQIGDKFSSRHGQKGVCSRKWPTIDMPFSE
TGIQPDIIINPHAFPSRMTIGMFVESLAGKAGALHGIAQD
STPWIFNEDDTPADYFGEQLAKAGYNYHGNEPMYSGATGE
ELRADIYVGVVYYQRLRHMVNDKFQVRSTGPVNSLTMQPV
KGRKRHGGIRVGEMERDALIGHGTSFLLQDRLLNSSDYTQ
ASVCRECGSILTTQQSVPRIGSISTVCCRRCSMRFEDAKK
GEKIFIDDSQIWEDGQGNKFVGGNETTTVAIPFVLKYLDS
ELSAMGIRLRYNVEPK
C:  EWNVEKFKKDFEVNISSLDAREANFDLINIDTSIANAFRR
IMISEVPSVAAEYVYFFNNTSVIQDEVLAHRIGLVPLKVD
PDMLTWVDSNLPDDEKFTDENTIVLSLNVKCTRNPDAPST
DPKELYNNAHVYARDLKFEPQGRQSTTFADCPVVPADPDI
LLAKLRPGQEISLKAHCILGIGGDHAKFSPVSTASYRLLP
QINILQPIKGESARRFQKCFPPGVIGIDEGSDEAYVKDAR
KDTVSREVLRYEEFADKVKLGRVRNHFIFNVESAGAMTPE
EIFFKSVRILKNKAEYLKNCPITQ
D:  SATTLNTPVVIHATQLPQHVSTDEVLQFLESFIDEKENTN
LSSSISQLKRIQRDFKGLP
E:  MDQENERNISRLWRAFRTVKEMVKDRGYFITQEEVELPLE
DFKAKYCDSMGRPQRKMMSFQANPTEESISKFPDMGSLWV
EFCDEPSVGVKTMKTFVIHIQEKNFQTGIFVYQNNITPSA
MKLVPSIPPATIETFNEAALVVNITHHELVPKHIRLSSDE
KRELLKRYRLKESQLPRIQRADPVALYLGLKRGEVVKIIR
KSETSGRYASYRICM
F:  PEDFQQHEQIRRKTLKEKAIPKDQRATTPYMTKYERARIL
GTRALQISMNAPVFVDLEGETDPLRIAMKELAEKKIPLVI
RRYLPDGSFEDWSVEELIVD
G:  NENRETARFIKKHKKQVTNPIDEKNGTSNCIVRVPIALYV
SLAPMYLENPLQGVMKQHLNPLVMKYNNKVGGVVLGYEGL
KILDADPLDTSEKLIKITPDTPFGFTWCHVNLYVWQPQVG
DVLEGYIFIQSASHIGLLIHDAFNASIKKNNIPVDWTFVH
NDVELGHWVDSNGEPIDGKLRFTVRNVHTTGRVVSVDGTL
ISYNSSRSQAESLPIVSNKKIVFDDEVSIENKESHKELDL
PEVKEDNGSEIVYEENTSE
H:  NTLFDDIFQVSEVDPGRYNKVCRIEAASTTQDQCKLTLDI
NVELFPVAAQDSLTVTIASSLNATRSWRPPQAGDRSLADD
YDYVMYGTAYKFEEVSKDLIAVYYSFGGLLMRLEGNYRNL
NNLKQENAYLLIRR
I:  SVVGSLIFCLDCGDLLENPNAVLGSNVECSQCKAIYPKSQ
FSNLKVVTTTADDAFPSSLRAKKSVVKTSLKKNELKDGAT
IKEKCPQCGNEEMNYHTLQLRSADEGATVFYTCTSCGYKF
RTNN
J:  MIVPVRCFSCGKVVGDKWESYLNLLQEDELDEGTALSRLG
LKRYCCRRMILTHVDLIEKFLRYNPLEKR
K:  EEPDREKIKLLTQATSEDGTSASFQIVEEDHTLGNALRYV
IMKNPDVEFCGYSIPHPSENLLNIRIQTYGETTAVDALQK
GLKDLMDLCDVVESKFTEKIKSM
L:  TLKYICAECSSKLSLSRTDAVRCKDCGHRILLKARTKRLV
QFEAR
M:  SEIEIESVQDQPSVAVGSFFKGFRAPSDTTFDLYKKKEKD
EFVLHGENERLEYEGYTDSSSQASNQYVVGLFNPEKKSIQ
LYKAPVLVSKVVSKSSKNLRGPKIK
N:  FSIPDGFKKCKHLKNFPLNGDNKQQQVWLIKFPSNVDISK
LKSLPVDFESSTTMTIDKHDYKIMDDTDNMTLLVPSESKE
SLKIASTAPLQFDKVFSVSETAKIPAIDYSKVRVPRKDVP
KVEGLKLEHFATGYDAEDF
Description (1)  DNA-DIRECTED RNA POLYMERASE I SUBUNIT RPA190 (E.C.2.7.7.6), DNA-DIRECTED RNA POLYMERASE I SUBUNIT RPA135 (E.C.2.7.7.6), DNA-DIRECTED RNA POLYMERASES I AND III SUBUNIT RPAC1, DNA-DIRECTED RNA POLYMERASE I SUBUNIT RPA14, DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC 1, DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC 2, DNA-DIRECTED RNA POLYMERASE I SUBUNIT RPA43, DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC 3, DNA-DIRECTED RNA POLYMERASE I SUBUNIT RPA12, DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC 5, DNA-DIRECTED RNA POLYMERASES I AND III SUBUNIT RPAC2, DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC 4, DNA-DIRECTED RNA POLYMERASE I SUBUNIT RPA49, DNA-DIRECTED RNA POLYMERASE I SUBUNIT RPA34


Functional site

1) chain A
residue 102
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 2664
source : AC1

2) chain A
residue 105
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 2664
source : AC1

3) chain A
residue 233
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 2664
source : AC1

4) chain A
residue 236
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 2664
source : AC1

5) chain A
residue 62
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 2665
source : AC2

6) chain A
residue 65
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 2665
source : AC2

7) chain A
residue 72
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 2665
source : AC2

8) chain A
residue 75
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 2665
source : AC2

9) chain B
residue 1104
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 2204
source : AC3

10) chain B
residue 1107
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 2204
source : AC3

11) chain B
residue 1128
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 2204
source : AC3

12) chain B
residue 1131
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 2204
source : AC3

13) chain L
residue 31
type
sequence C
description BINDING SITE FOR RESIDUE ZN L 1071
source : AC4

14) chain L
residue 34
type
sequence C
description BINDING SITE FOR RESIDUE ZN L 1071
source : AC4

15) chain L
residue 48
type
sequence C
description BINDING SITE FOR RESIDUE ZN L 1071
source : AC4

16) chain L
residue 51
type
sequence C
description BINDING SITE FOR RESIDUE ZN L 1071
source : AC4

17) chain J
residue 7
type
sequence C
description BINDING SITE FOR RESIDUE ZN J 1070
source : AC5

18) chain J
residue 10
type
sequence C
description BINDING SITE FOR RESIDUE ZN J 1070
source : AC5

19) chain J
residue 45
type
sequence C
description BINDING SITE FOR RESIDUE ZN J 1070
source : AC5

20) chain J
residue 46
type
sequence C
description BINDING SITE FOR RESIDUE ZN J 1070
source : AC5

21) chain I
residue 10
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 1126
source : AC6

22) chain I
residue 13
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 1126
source : AC6

23) chain I
residue 30
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 1126
source : AC6

24) chain I
residue 33
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 1126
source : AC6

25) chain I
residue 86
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 1127
source : AC7

26) chain I
residue 89
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 1127
source : AC7

27) chain I
residue 114
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 1127
source : AC7

28) chain I
residue 117
type
sequence C
description BINDING SITE FOR RESIDUE ZN I 1127
source : AC7

29) chain J
residue 45
type MOD_RES
sequence C
description Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198
source Swiss-Prot : SWS_FT_FI1

30) chain J
residue 46
type MOD_RES
sequence C
description Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198
source Swiss-Prot : SWS_FT_FI1

31) chain A
residue 102
type MOD_RES
sequence C
description Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198
source Swiss-Prot : SWS_FT_FI1

32) chain A
residue 105
type MOD_RES
sequence C
description Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198
source Swiss-Prot : SWS_FT_FI1

33) chain A
residue 233
type MOD_RES
sequence C
description Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198
source Swiss-Prot : SWS_FT_FI1

34) chain A
residue 236
type MOD_RES
sequence C
description Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198
source Swiss-Prot : SWS_FT_FI1

35) 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

36) 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

37) chain B
residue 914-926
type prosite
sequence GDKFSSRHGQKGV
description RNA_POL_BETA RNA polymerases beta chain signature. GdKFSSrHGQKGV
source prosite : PS01166

38) chain K
residue 65-96
type prosite
sequence IVEEDHTLGNALRYVIMKNPDVEFCGYSIPHP
description RNA_POL_L_13KD RNA polymerases L / 13 to 16 Kd subunits signature. IveEdHTLgNaLryvImknpdVefcgYsipHP
source prosite : PS01154

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 C
residue 65-105
type prosite
sequence NAFRRIMISEVPSVAAEYVYFFNNTSVIQDEVLAHRIGLV
P
description RNA_POL_D_30KD RNA polymerases D / 30 to 40 Kd subunits signature. NAFRRimisevpsvAaeyVyffnNtSviqDEvLAhRIGLVP
source prosite : PS00446

41) chain I
residue 86-121
type prosite
sequence CPQCGNEEMNYHTLQLRSADEGATVFYTCTSCGYKF
description ZF_TFIIS_1 Zinc finger TFIIS-type signature. CpqCgneemnyhtLQLRSaDEGatvfytCts...CgykF
source prosite : PS00466

42) chain I
residue 9-33
type prosite
sequence FCLDCGDLLENPNAVLGSNVECSQC
description RNA_POL_M_15KD RNA polymerases M / 15 Kd subunits signature. FClDCGDLLenpnavlgsnve..CsqC
source prosite : PS01030

43) chain L
residue 34
type MOD_RES
sequence C
description Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
source Swiss-Prot : SWS_FT_FI2

44) chain L
residue 48
type MOD_RES
sequence C
description Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
source Swiss-Prot : SWS_FT_FI2

45) chain L
residue 51
type MOD_RES
sequence C
description Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
source Swiss-Prot : SWS_FT_FI2

46) chain N
residue 60
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:18407956
source Swiss-Prot : SWS_FT_FI3

47) chain I
residue 89
type MOD_RES
sequence C
description Phosphoserine => ECO:0007744|PubMed:18407956
source Swiss-Prot : SWS_FT_FI3

48) chain I
residue 114
type MOD_RES
sequence C
description Phosphoserine => ECO:0007744|PubMed:18407956
source Swiss-Prot : SWS_FT_FI3

49) chain I
residue 117
type MOD_RES
sequence C
description Phosphoserine => ECO:0007744|PubMed:18407956
source Swiss-Prot : SWS_FT_FI3

50) chain B
residue 1156
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:19779198
source Swiss-Prot : SWS_FT_FI4


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