eF-site ID 2uua-BCDEFGHIJKLMNOPQRSTU
PDB Code 2uua
Chain B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U

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Title Structure of the Thermus thermophilus 30S ribosomal subunit complexed with a Valine-ASL with cmo5U in position 34 bound to an mRNA with a GUC-codon in the A-site and paromomycin.
Classification RIBOSOME
Compound 16S RRNA
Source ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
Sequence B:  VKELLEAGVHFGHERKRWNPKFARYIYAERNGIHIIDLQK
TMEELERTFRFIEDLAMRGGTILFVGTKKQAQDIVRMEAE
RAGMPYVNQRWLGGMLTNFKTISQRVHRLEELEALFASPE
IEERPKKEQVRLKHELERLQKYLSGFRLLKRLPDAIFVVD
PTKEAIAVREARKLFIPVIALADTDSDPDLVDYIIPGNDD
AIRSIQLILSRAVDLIIQARGGVVEPSPSYALVQE
C:  GNKIHPIGFRLGITRDWESRWYAGKKQYRHLLLEDQRIRG
LLEKELYSAGLARVDIERAADNVAVTVHVAKPGVVIGRGG
ERIRVLREELAKLTGKNVALNVQEVQNPNLSAPLVAQRVA
EQIERRFAVRRAIKQAVQRVMESGAKGAKVIVSGRIGGAE
QARTEWAAQGRVPLHTLRANIDYGFALARTTYGVLGVKAY
IFLGEVI
D:  GRYIGPVCRLCRREGVKLYLKGERCYSPKCAMERRPYPPG
QHGQKRARRPSDYAVRLREKQKLRRIYGISERQFRNLFEE
ASKKKGVTGSVFLGLLESRLDNVVYRLGFAVSRRQARQLV
RHGHITVNGRRVDLPSYRVRPGDEIAVAEKSRNLELIRQN
LEAMKGRKVGPWLSLDVEGMKGKFLRLPDREDLALPVNEQ
LVIEFYSR
E:  DFEEKMILIRRTARMQAGGRRFRFGALVVVGDRQGRVGLG
FGKAPEVPLAVQKAGYYARRNMVEVPLQNGTIPHEIEVEF
GASKIVLKPAAPGTGVIAGAVPRAILELAGVTDILTKELG
SRNPINIAYATMEALRQLRTKADVERLRKGE
F:  MRRYEVNIVLNPNLDQSQLALEKEIIQRALENYGARVEKV
EELGLRRLAYPIAKDPQGYFLWYQVEMPEDRVNDLARELR
IRDNVRRVMVVKSQEPFLANA
G:  ARRRRAEVRQLQPDLVYGDVLVTAFINKIMRDGKKNLAAR
IFYDACKIIQEKTGQEPLKVFKQAVENVKPRMEVRSRRVG
GANYQVPMEVSPRRQQSLALRWLVQAANQRPERRAAVRIA
HELMDAAEGKGGAVKKKEDVERMAEANRAYAHYRW
H:  MLTDPIADMLTRIRNATRVYKESTDVPASRFKEEILRILA
REGFIKGYERVDVDGKPYLRVYLKYGPRRQGPDPRPEQVI
HHIRRISKPGRRVYVGVKEIPRVRRGLGIAILSTSKGVLT
DREARKLGVGGELICEVW
I:  EQYYGTGRRKEAVARVFLRPGNGKVTVNGQDFNEYFQGLV
RAVAALEPLRAVDALGHFDAYITVRGGGKSGQIDAIKLGI
ARALVQYNPDYRAKLKPLGFLTRDARVVERKKYGKHKARR
APQYSKR
J:  KIRIKLRGFDHKTLDASAQKIVEAARRSGAQVSGPIPLPT
RVRRFTVIRGPFKHKDSREHFELRTHNRLVDIINPNRKTI
EQLMTLDLPTGVEIEIKTV
K:  KRQVASGRAYIHASYNNTIVTITDPDGNPITWSSGGVIGY
KGSRKGTPYAAQLAALDAAKKAMAYGMQSVDVIVRGTGAG
REQAIRALQASGLQVKSIVDDTPVPHNGCRPKKKFRKAS
L:  PTINQLVRKGREKVRKKSKVPALKGAPFRRGVCTVVRTVT
PKKPNSALRKVAKVRLTSGYEVTAYIPGEGHNLQEHSVVL
IRGGRVKDLPGVRYHIVRGVYDAAGVKDRKKSRSKYGTKK
PKEAA
M:  ARIAGVEIPRNKRVDVALTYIYGIGKARAKEALEKTGINP
ATRVKDLTEAEVVRLREYVENTWKLEGELRAEVAANIKRL
MDIGCYRGLRHRRGLPVRGQRTRTNARTRKGPRKTVAGKK
KAPRK
N:  ARKALIEKAKRTPKFKVRAYTRCVRCGRARSVYRFFGLCR
ICLRELAHKGQLPGVRKASW
O:  PITKEEKQKVIQEFARFPGDTGSTEVQVALLTLRINRLSE
HLKVHKKDHHSHRGLLMMVGQRRRLLRYLQREDPERYRAL
IEKLGIRG
P:  MVKIRLARFGSKHNPHYRIVVTDARRKRDGKYIEKIGYYD
PRKTTPDWLKVDVERARYWLSVGAQPTDTARRLLRQAGVF
RQEA
Q:  PKKVLTGVVVSDKMQKTVTVLVERQFPHPLYGKVIKRSKK
YLAHDPEEKYKLGDVVEIIESRPISKRKRFRVLRLVESGR
MDLVEKYLIRRQNYESLSKRGGKA
R:  PSRKAKVKATLGEFDLRDYRNVEVLKRFLSETGKILPRRR
TGLSAKEQRILAKTIKRARILGLLPFTEKLVRK
S:  PRSLKKGVFVDDHLLEKVLELNAKGEKRLIKTWSRRSTIV
PEMVGHTIAVYNGKQHVPVYITENMVGHKLGEFAPTRTYR
G
T:  RNLSALKRHRQSLKRRLRNKAKKSAIKTLSKKAIQLAQEG
KAEEALKIMRKAESLIDKAAKGSTLHKNAAARRKSRLMRK
VRQLLEAAGAPLIGGGLSA
U:  GKGDRRTRRGKIWRGTYGKYRPRKK
Description


Functional site

1) chain N
residue 2
type
sequence A
description binding site for residue MG A 1610
source : AC8

2) chain T
residue 83
type
sequence R
description binding site for residue MG A 1611
source : AC9

3) chain T
residue 35
type
sequence T
description binding site for residue MG A 1666
source : AH5

4) chain U
residue 5
type
sequence D
description binding site for residue MG A 1698
source : AK6

5) chain L
residue 48
type
sequence P
description binding site for residue MG A 1709
source : AL5

6) chain L
residue 49
type
sequence N
description binding site for residue MG A 1709
source : AL5

7) chain L
residue 44
type
sequence T
description binding site for residue MG A 1710
source : AL6

8) chain L
residue 20
type
sequence K
description binding site for residue MG A 1722
source : AM8

9) chain L
residue 15
type
sequence R
description binding site for residue MG A 1723
source : AM9

10) chain Q
residue 32
type
sequence Y
description binding site for residue MG A 1723
source : AM9

11) chain Q
residue 39
type
sequence S
description binding site for residue MG A 1739
source : AO7

12) chain M
residue 101
type
sequence Q
description binding site for residue MG A 1751
source : AQ1

13) chain E
residue 27
type
sequence R
description binding site for residue MG A 1753
source : AQ3

14) chain U
residue 3
type
sequence K
description binding site for residue K A 1775
source : AS7

15) chain G
residue 78
type
sequence R
description binding site for residue K A 1778
source : AT1

16) chain M
residue 20
type
sequence T
description binding site for residue MG A 1781
source : AT4

17) chain M
residue 22
type
sequence I
description binding site for residue MG A 1781
source : AT4

18) chain M
residue 23
type
sequence Y
description binding site for residue MG A 1781
source : AT4

19) chain M
residue 25
type
sequence I
description binding site for residue MG A 1781
source : AT4

20) chain Q
residue 65
type
sequence I
description binding site for residue MG A 1782
source : AT5

21) chain L
residue 48
type
sequence P
description binding site for residue MG A 1783
source : AT6

22) chain B
residue 20
type
sequence E
description binding site for residue MG B 301
source : AT7

23) chain B
residue 166
type
sequence D
description binding site for residue MG B 301
source : AT7

24) chain B
residue 189
type
sequence D
description binding site for residue MG B 301
source : AT7

25) chain B
residue 191
type
sequence D
description binding site for residue MG B 301
source : AT7

26) chain B
residue 205
type
sequence D
description binding site for residue MG B 301
source : AT7

27) chain D
residue 9
type
sequence C
description binding site for residue ZN D 301
source : AT8

28) chain D
residue 12
type
sequence C
description binding site for residue ZN D 301
source : AT8

29) chain D
residue 19
type
sequence L
description binding site for residue ZN D 301
source : AT8

30) chain D
residue 26
type
sequence C
description binding site for residue ZN D 301
source : AT8

31) chain D
residue 31
type
sequence C
description binding site for residue ZN D 301
source : AT8

32) chain D
residue 82
type
sequence A
description binding site for residue MG D 302
source : AT9

33) chain D
residue 83
type
sequence S
description binding site for residue MG D 302
source : AT9

34) chain D
residue 85
type
sequence K
description binding site for residue MG D 302
source : AT9

35) chain D
residue 87
type
sequence G
description binding site for residue MG D 302
source : AT9

36) chain D
residue 89
type
sequence T
description binding site for residue MG D 302
source : AT9

37) chain E
residue 13
type
sequence I
description binding site for residue MG E 202
source : AU1

38) chain E
residue 83
type
sequence E
description binding site for residue K E 203
source : AU2

39) chain F
residue 80
type
sequence R
description binding site for residue MG F 201
source : AU3

40) chain F
residue 82
type
sequence R
description binding site for residue MG F 201
source : AU3

41) chain F
residue 85
type
sequence V
description binding site for residue MG F 201
source : AU3

42) chain G
residue 35
type
sequence K
description binding site for residue MG G 201
source : AU4

43) chain G
residue 37
type
sequence N
description binding site for residue MG G 201
source : AU4

44) chain G
residue 38
type
sequence L
description binding site for residue MG G 201
source : AU4

45) chain H
residue 7
type
sequence A
description binding site for residue MG H 201
source : AU5

46) chain H
residue 11
type
sequence T
description binding site for residue MG H 201
source : AU5

47) chain H
residue 14
type
sequence R
description binding site for residue MG H 201
source : AU5

48) chain H
residue 14
type
sequence R
description binding site for residue MG H 202
source : AU6

49) chain H
residue 82
type
sequence H
description binding site for residue MG H 202
source : AU6

50) chain H
residue 83
type
sequence I
description binding site for residue MG H 202
source : AU6

51) chain N
residue 24
type
sequence C
description binding site for residue ZN N 101
source : AU7

52) chain N
residue 27
type
sequence C
description binding site for residue ZN N 101
source : AU7

53) chain N
residue 40
type
sequence C
description binding site for residue ZN N 101
source : AU7

54) chain N
residue 43
type
sequence C
description binding site for residue ZN N 101
source : AU7

55) chain Q
residue 13
type
sequence D
description binding site for residue MG Q 201
source : AU8

56) chain Q
residue 15
type
sequence M
description binding site for residue MG Q 201
source : AU8

57) chain Q
residue 49
type
sequence E
description binding site for residue MG Q 201
source : AU8

58) chain G
residue 20-46
type prosite
sequence DVLVTAFINKIMRDGKKNLAARIFYDA
description RIBOSOMAL_S7 Ribosomal protein S7 signature. DvLvtaFInkimrdGKKnlaarIFydA
source prosite : PS00052

59) chain H
residue 108-125
type prosite
sequence GIAILSTSKGVLTDREAR
description RIBOSOMAL_S8 Ribosomal protein S8 signature. GiaILSTSkGVLtdreAR
source prosite : PS00053

60) chain K
residue 95-117
type prosite
sequence IRALQASGLQVKSIVDDTPVPHN
description RIBOSOMAL_S11 Ribosomal protein S11 signature. IrALqaS.GLqVksivDdTPvPHN
source prosite : PS00054

61) chain L
residue 46-53
type prosite
sequence KKPNSALR
description RIBOSOMAL_S12 Ribosomal protein S12 signature. KkPNSAlR
source prosite : PS00055

62) chain Q
residue 54-66
type prosite
sequence GDVVEIIESRPIS
description RIBOSOMAL_S17 Ribosomal protein S17 signature. GDvVeIiEsRPIS
source prosite : PS00056

63) chain R
residue 32-55
type prosite
sequence RDYRNVEVLKRFLSETGKILPRRR
description RIBOSOMAL_S18 Ribosomal protein S18 signature. RDYrn.VevLkrFLSEt.GKIlprRR
source prosite : PS00057

64) chain R
residue 66-81
type prosite
sequence LAKTIKRARILGLLPF
description ALDOKETO_REDUCTASE_3 Aldo/keto reductase family putative active site signature. LAKTIKraRIlGLlPF
source prosite : PS00063

65) chain S
residue 53-77
type prosite
sequence NGKQHVPVYITENMVGHKLGEFAPT
description RIBOSOMAL_S19 Ribosomal protein S19 signature. NGKqhvpvyItenmVGhkLGEFapT
source prosite : PS00323

66) chain I
residue 67-85
type prosite
sequence GGGKSGQIDAIKLGIARAL
description RIBOSOMAL_S9 Ribosomal protein S9 signature. GGGksGQidAiklGiARAL
source prosite : PS00360

67) chain J
residue 27-42
type prosite
sequence ARRSGAQVSGPIPLPT
description RIBOSOMAL_S10 Ribosomal protein S10 signature. ArrsGAqvsGPIpLPT
source prosite : PS00361

68) chain O
residue 39-69
type prosite
sequence LSEHLKVHKKDHHSHRGLLMMVGQRRRLLRY
description RIBOSOMAL_S15 Ribosomal protein S15 signature. LseHLkvhKkDhhShrgLlmMvgqrrrLlrY
source prosite : PS00362

69) chain N
residue 23-45
type prosite
sequence RCVRCGRARSVYRFFGLCRICLR
description RIBOSOMAL_S14 Ribosomal protein S14 signature. R.CvrcgrarsvyrfFGLCRiCLR
source prosite : PS00527

70) chain C
residue 163-197
type prosite
sequence ARTEWAAQGRVPLHTLRANIDYGFALARTTYGVLG
description RIBOSOMAL_S3 Ribosomal protein S3 signature. ARtewaaqGrVplHt..LranIDygfalarTtyGvlG
source prosite : PS00548

71) chain E
residue 23-55
type prosite
sequence GRRFRFGALVVVGDRQGRVGLGFGKAPEVPLAV
description RIBOSOMAL_S5 Ribosomal protein S5 signature. GRrfrFgAlvVVGDrq.GrVGlGfgkap.EVpl.AV
source prosite : PS00585

72) chain D
residue 97-121
type prosite
sequence LESRLDNVVYRLGFAVSRRQARQLV
description RIBOSOMAL_S4 Ribosomal protein S4 signature. LEsRLdnvVYRlgfAvSrrqARqLV
source prosite : PS00632

73) chain M
residue 88-101
type prosite
sequence RGLRHRRGLPVRGQ
description RIBOSOMAL_S13_1 Ribosomal protein S13 signature. RGlRHrrGlpVRGQ
source prosite : PS00646

74) chain B
residue 7-18
type prosite
sequence VKELLEAGVHFG
description RIBOSOMAL_S2_1 Ribosomal protein S2 signature 1. VkELLEAGVHFG
source prosite : PS00962

75) chain F
residue 44-53
type prosite
sequence GLRRLAYPIA
description RIBOSOMAL_S6 Ribosomal protein S6 signature. GlRRLAYpIA
source prosite : PS01048

76) chain N
residue 25
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:11866529
source Swiss-Prot : SWS_FT_FI1

77) chain N
residue 28
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:11866529
source Swiss-Prot : SWS_FT_FI1

78) chain N
residue 41
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:11866529
source Swiss-Prot : SWS_FT_FI1

79) chain N
residue 44
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:11866529
source Swiss-Prot : SWS_FT_FI1


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