eF-site ID 6eu2-ABCDEFGHIJKLMNOPQ
PDB Code 6eu2
Chain A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q
Title Apo RNA Polymerase III - open conformation (oPOL3)
Classification TRANSCRIPTION
Compound DNA-directed RNA polymerase III subunit RPC1
Source ORGANISM_COMMON: Baker's yeast; ORGANISM_SCIENTIFIC: Saccharomyces cerevisiae (strain ATCC 204508 / S288c);
Sequence A:  KEVVVSETPKRIKGLEFSALSAADIVAQSEVEVSTRDLFD
LEKDRAPKANGALDPKMGVSSSSLECATCHGNLASCHGHF
GHLKLALPVFHIGYFKATIQILQGICKNCSAILLSETDKR
QFLHELRRPGVDNLRRMGILKKILDQCKKQRRCLHCGALN
GVVKKAAALKIIHDTFRWVGKKSAPEKDIWVGEWKEVLAH
NPELERYVKRCMDDLNPLKTLNLFKQIKSADCELLGIDAT
VPSGRPETYIWRYLPAPPVCIRPSVMMQDSPASNEDDLTV
KLTEIVWTSSLIKAGLDKGISINNMMEHWDYLQLTVAMYI
NSGNLSGKRVDFSGRTVISPDPNLSIDEVAVPDRVAKVLT
YPEKVTRYNRHKLQELIVNGPNVHPGANYLLKRNEDARRN
LRYGDRMKLAKNLQIGDVVERHLEDGDVVLFNRQPSLHRL
SILSHYAKIRPWRTFRLNECVCTPYNADFDGDEMNLHVPQ
TEEARAEAINLMGVKNNLLTPKSGEPIIAATQDFITGSYL
ISHKDSFYDRATLTQLLSMMSDGIEHFDIPPPAIMKPYYL
WTGKQVFSLLIKPNHNSPVVINLDAKNKVFVPPKSKSLPN
EMSQNDGFVIIRGSQILSGVMDKSVLGDGKKHSVFYTILR
DYGPQEAANAMNRMAKLCARFLGNRGFSIGINDVTPADDL
KQKKEELVEIAYHKCDELITLFNKGELETQPGCNEEQTLE
AKIGGLLSKVREEVGDVCINELDNWNAPLIMATCGSKGST
LNVSQMVAVVGQQIISGNRVPDGFQDRSLPHFPKNSKTPQ
SKGFVRNSFFSGLSPPEFLFHAISGREGLVDTAVKTAETG
YMSRRLMKSLEDLSCQYDNTVRTSANGIVQFTYGGDGLDP
LEMEGNAQPVNFNRSWDHAYNITFNNQDKGLLPYAIMETA
NEILGPLEERLVRYDNSGCLVKREDLNKAEYVDQYDAERD
FYHSLREYINGKATALANLRKSRGMLGLLEPPAKELQGID
PDETVPDNVKTSVSQLYRISEKSVRKFLEIALFKYRKARL
EPGTAIGAIGAQSIGEPGTQMTLKTFHFAGVASMNVTLGV
PRIKEIINASKVISTPIINAVLVNDNDERAARVVKGRVEK
TLLSDVAFYVQDVYKDNLSFIQVRIDLGTIDKLQLELTIE
DIAVAITRASKLKIQASDVNIIGKDRIAINVFPSENDVFY
RMQQLRRALPDVVVKGLPDISRAVINIRDDGKRELLVEGY
GLRDVMCTDGVIGSRTTTNHVLEVFSVLGIEAARYSIIRE
INYTMSNHGMSVDPRHIQLLGDVMTYKGEVLGITRFGLSK
MRDSVLQLASFEKTTDHLFDAAFYMKKDAVEGVSECIILG
QTMSIGTGSFKVVKGTNISEKDLVPKRCLFESLSNEAALK
AN
B:  DEINTAQDKWHLLPAFLKVKGLVKQHLDSFNYFVDTDLKK
IIKANQLILSDVDPEFYLKYVDIRVGKKSSSSTKDYLTPP
HECRLRDMTYSAPIYVDIEYTRGRNIIMHKDVEIGRMPIM
LRSNKCILYDADESKMAKLNECPLDPGGYFIVNGTEKVIL
VQEQLSKNRIIVEADEKKGIVQASVTSSTHERKSKTYVIT
KNGKIYLKHNSIAEEIPIAIVLKACGILSDLEIMQLVCGN
DSSYQDIFAVNLEESSKLDIYTQQQALEYIGAKVKTMRRQ
KLTILQEGIEAIATTVIAHLTVEALDFREKALYIAMMTRR
VVMAMYNPKMIDDRDYVGNKRLELAGQLISLLFEDLFKKF
NNDFKLSIDKVLKKPNRAMEYDALLSINVHSNNITSGLNR
AISTGNWSLKRFKMERAGVTHVLSRLSYISALGMMTRISS
QFEKSRKVSGPRALQPSQFGMLCTADTPEGEACGLVKNLA
LMTHITTDDEEEPIKKLCYVLGVEDITLIDSASLHLNYGV
YLNGTLIGSIRFPTKFVTQFRHLRRTGKVSEFISIYSNSH
QMAVHIATDGGRICRPLIIVSDGQSRVKDIHLRKLLDGEL
DFDDFLKLGLVEYLDVNEENDSYIALYEKDIVPSMTHLEI
EPFTILGAVAGLIPYPHHNQSPRNTYQCAMGKQAIGAIAY
NQFKRIDTLLYLMTYPQQPMVKTKTIELIDYDKLPAGQNA
TVAVMSYSGYDIEDALVLNKSSIDRGFGRCETRRKTTTVL
KRYANHTQDIIGGMRVDENGDPIWQHQSLGPDGLGEVGMK
VQSGQIYINKSVPTNSADAPNPNNVNVQTQYREAPVIYRG
PEPSHIDQVMMSVSDNDQALIKVLLRQNRRPELGDKFSSR
HGQKGVCGIIVKQEDMPFNDQGIVPDIIMNPHGFPSRMTV
GKMIELISGKAGVLNGTLEYGTCFGGSKLEDMSKILVDQG
FNYSGKDMLYSGITGECLQAYIFFGPIYYQKLKHMVLDKM
HARARGPRAVLTRQPTEGRSRDGGLRLGEMERDCVIAYGA
SQLLLERLMISSDAFEVDVCDKCGLMGYSGWCTTCKSAEN
IIKMTIPYAAKLLFQELLSMNIAPRLRLEDIFQQ
C:  MSNIVGIEYNRVTNTTSTDFPGFSKDAENEWNVEKFKKDF
EVNISSLDAREANFDLINIDTSIANAFRRIMISEVPSVAA
EYVYFFNNTSVIQDEVLAHRIGLVPLKVDPDMLTWVDSNL
PDDEKFTDENTIVLSLNVKCTRNPDAPKGSTDPKELYNNA
HVYARDLKFEPQGRQSTTFADCPVVPADPDILLAKLRPGQ
EISLKAHCILGIGGDHAKFSPVSTASYRLLPQINILQPIK
GESARRFQKCFPPGVIGIDEGSDEAYVKDARKDTVSREVL
RYEEFADKVKLGRVRNHFIFNVESAGAMTPEEIFFKSVRI
LKNKAEYLKNCPITQ
D:  MKVLEERNAFLSDYEVLKFLTDLEKKHLWDQKSLAPELQG
ITRNVVNYLSINKNFMSDESFAELMTKLNSFKLFKAEKLQ
IVNQLPANMVHLYSIVEECDARFDEKTIEEMLEIISGYA
E:  MDQENERNISRLWRAFRTVKEMVKDRGYFITQEEVELPLE
DFKAKYCDSMGRPQRKMMSFQANPTEESISKFPDMGSLWV
EFCDEPSVGVKTMKTFVIHIQEKNFQTGIFVYQNNITPSA
MKLVPSIPPATIETFNEAALVVNITHHELVPKHIRLSSDE
KRELLKRYRLKESQLPRIQRADPVALYLGLKRGEVVKIIR
KSETSGRYASYRICM
F:  EKAIPKDQRATTPYMTKYERARILGTRALQISMNAPVFVD
LEGETDPLRIAMKELAEKKIPLVIRRYLPDGSFEDWSVEE
LIV
G:  FILSKIADLVRIPPDQFHRDTISAITHQLNNKFANKIIPN
VGLCITIYDLLTVEEGQLKPGDGSSYINVTFRAVVFKPFL
GEIVTGWISKCTAEGIKVSLLGIFDDIFIPQNMLFEGCYY
TPEESAWIWPKLYFDVNEKIRFRIEREVFVDVKPKSPKER
ELEERAQEKPPAYALLGSCQTDGMGLVSWWE
H:  MSNTLFDDIFQVSEVDPGRYNKVCRIEAASTTQDQCKLTL
DINVELFPVAAQDSLTVTIASSLNLEDSATRSWRPPQAGD
RSLADDYDYVMYGTAYKFEEVSKDLIAVYYSFGGLLMRLE
GNYRNLNNLKQENAYLLIRR
I:  MLSFCPSCNNMLLITSGDSGVYTLACRSCPYEFPIEGIEI
YD
J:  MIVPVRCFSCGKVVGDKWESYLNLLQEDELDEGTALSRLG
LKRYCCRRMILTHVDLIEKFLRYNPLEK
K:  PDREKIKLLTQATSEDGTSASFQIVEEDHTLGNALRYVIM
KNPDVEFCGYSIPHPSENLLNIRIQTYGETTAVDALQKGL
KDLMDLCDVVESKFTEKIKSM
L:  TLKYICAECSSKLSLSRTDAVRCKDCGHRILLKARTKRLV
QFEAR
M:  IEEFPLKISGEEESLHVFQYANRPRLVGRKPAEHPFISAA
RYKPKSHLWEIDIPLDEQAFYNKDKAESEWNGVNVQTLKG
VGVENNGQYAAFVKDMQVYLVPIERVAQLKPFFKYIDDAN
VTRKQEQNRLTGSLLAHKVADEEANIELTWAEGTFEQFKD
TIVKE
N:  KEAAAELELLNADHQHILRKLKKMNNKPERFMVFQLPTRL
PAVGSIRVHKSGKLSVKIGNVVMDIGKGAETTFLQDVIAL
SIADDASSAELLGRVDGKIVVTPQI
O:  VMTISSLEQRTLNPDLFLYKELVKAHLGERAASVIGMLVA
LGRLSVRELVEKIDGMDVDSVKTTLVSLTQLRCVKYLQET
AISGKKTTYYYYNEEGIHILLYSGLIIDEIITQMRVNDEE
EHKQLVAEIVQNVISLGSLTVEDYLSSVTSDSMKYTISSL
FVQLCEMGYLIQISKLHYTPIEDLWQFLYEKHYKNIPRNS
PLSDLKKRSQAKMNAKTDFAKIINKPNELSQILTVDPKTS
LRIVKPTVSLTINLDRFMKGRRSKQLINLAKTRVGSVTAQ
VYKIALRLTEQKSPKIRDPLTQTGLLQDLEEAKSFQDEAE
LVEEKTPGLTFNAIDLARHLASLINSHLKILASSNFPFLN
ETKPGVYYVPYSKLMPVLKSSVYEYVIASTLGPSAMRLSR
CIRDNKLVSEKIINSTALMKEKDIRSTLASLIRYNSVEIQ
EVPRTADRSASRAVFLFRCKETHSYNFMRQNLEWNMANLL
FKKEKLKQENSTLLKKANRDDLLPSELNQLKMVNERELNV
FARLSRLLSLWEVFQMA
P:  DIEFINSLLTIVWRFISENTFPNGFKNFENGPKKNVFYAP
NVKNYSTTQEILEFITAAQVANVELTPSNIRSLCEVLVYD
DKLEKVTHDCYRVTLESILQMFNYFKMFPASKHDKEVVYF
DEW
Q:  EFPSIPLPINGPITNKERSLAVKYINFGKTVKDGPFYTGS
Description


Functional site

1) chain A
residue 67
type
sequence C
description binding site for residue ZN A 2000
source : AC1

2) chain A
residue 69
type
sequence T
description binding site for residue ZN A 2000
source : AC1

3) chain A
residue 70
type
sequence C
description binding site for residue ZN A 2000
source : AC1

4) chain A
residue 77
type
sequence C
description binding site for residue ZN A 2000
source : AC1

5) chain A
residue 80
type
sequence H
description binding site for residue ZN A 2000
source : AC1

6) chain A
residue 107
type
sequence C
description binding site for residue ZN A 2001
source : AC2

7) chain A
residue 110
type
sequence C
description binding site for residue ZN A 2001
source : AC2

8) chain A
residue 154
type
sequence C
description binding site for residue ZN A 2001
source : AC2

9) chain A
residue 157
type
sequence C
description binding site for residue ZN A 2001
source : AC2

10) chain A
residue 511
type
sequence D
description binding site for residue MG A 2002
source : AC3

11) chain A
residue 513
type
sequence D
description binding site for residue MG A 2002
source : AC3

12) chain A
residue 515
type
sequence D
description binding site for residue MG A 2002
source : AC3

13) chain B
residue 1095
type
sequence C
description binding site for residue ZN B 1201
source : AC4

14) chain B
residue 1097
type
sequence K
description binding site for residue ZN B 1201
source : AC4

15) chain B
residue 1098
type
sequence C
description binding site for residue ZN B 1201
source : AC4

16) chain B
residue 1107
type
sequence C
description binding site for residue ZN B 1201
source : AC4

17) chain I
residue 5
type
sequence C
description binding site for residue ZN I 201
source : AC5

18) chain I
residue 8
type
sequence C
description binding site for residue ZN I 201
source : AC5

19) chain I
residue 29
type
sequence C
description binding site for residue ZN I 201
source : AC5

20) chain J
residue 7
type
sequence C
description binding site for residue ZN J 101
source : AC6

21) chain J
residue 10
type
sequence C
description binding site for residue ZN J 101
source : AC6

22) chain J
residue 43
type
sequence R
description binding site for residue ZN J 101
source : AC6

23) chain J
residue 45
type
sequence C
description binding site for residue ZN J 101
source : AC6

24) chain J
residue 46
type
sequence C
description binding site for residue ZN J 101
source : AC6

25) chain L
residue 31
type
sequence C
description binding site for residue ZN L 101
source : AC7

26) chain L
residue 34
type
sequence C
description binding site for residue ZN L 101
source : AC7

27) chain L
residue 48
type
sequence C
description binding site for residue ZN L 101
source : AC7

28) chain L
residue 51
type
sequence C
description binding site for residue ZN L 101
source : AC7

29) 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

30) chain I
residue 4-29
type prosite
sequence FCPSCNNMLLITSGDSGVYTLACRSC
description RNA_POL_M_15KD RNA polymerases M / 15 Kd subunits signature. FCPSCNNMLlitsgdsgvytla.CrsC
source prosite : PS01030

31) 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

32) 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

33) 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

34) 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

35) chain B
residue 909-921
type prosite
sequence GDKFSSRHGQKGV
description RNA_POL_BETA RNA polymerases beta chain signature. GdKFSSrHGQKGV
source prosite : PS01166

36) chain A
residue 515
type MOD_RES
sequence D
description Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
source Swiss-Prot : SWS_FT_FI1

37) chain J
residue 45
type MOD_RES
sequence C
description Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
source Swiss-Prot : SWS_FT_FI1

38) chain J
residue 46
type MOD_RES
sequence C
description Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
source Swiss-Prot : SWS_FT_FI1

39) chain A
residue 107
type MOD_RES
sequence C
description Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
source Swiss-Prot : SWS_FT_FI1

40) chain A
residue 110
type MOD_RES
sequence C
description Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
source Swiss-Prot : SWS_FT_FI1

41) chain A
residue 154
type MOD_RES
sequence C
description Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
source Swiss-Prot : SWS_FT_FI1

42) chain A
residue 511
type MOD_RES
sequence D
description Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
source Swiss-Prot : SWS_FT_FI1

43) chain A
residue 513
type MOD_RES
sequence D
description Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
source Swiss-Prot : SWS_FT_FI1

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

46) chain I
residue 8
type MOD_RES
sequence C
description Phosphoserine => ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956
source Swiss-Prot : SWS_FT_FI3

47) chain I
residue 26
type MOD_RES
sequence C
description Phosphoserine => ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956
source Swiss-Prot : SWS_FT_FI3

48) chain I
residue 29
type MOD_RES
sequence C
description Phosphoserine => ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956
source Swiss-Prot : SWS_FT_FI3


Display surface

Download
Links