eF-site ID 1n32-BCDEFGHIJKLMNOPQRSTV PDB Code 1n32 Chain B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, V click to enlarge Title Structure of the Thermus thermophilus 30S ribosomal subunit bound to codon and near-cognate transfer RNA anticodon stem-loop mismatched at the first codon position at the a site with paromomycin Classification RIBOSOME Compound 16S RIBOSOMAL RNA Source ORGANISM_SCIENTIFIC: Thermus thermophilus; Sequence B:  VKELLEAGVHFGHERKRWNPKFARYIYAERNGIHIIDLQK TMEELERTFRFIEDLAMRGGTILFVGTKKQAQDIVRMEAE RAGMPYVNQRWLGGMLTNFKTISQRVHRLEELEALFASPE IEERPKKEQVRLKHELERLQKYLSGFRLLKRLPDAIFVVD PTKEAIAVREARKLFIPVIALADTDSDPDLVDYIIPGNDD AIRSIQLILSRAVDLIIQARGGVVEPSPSYALVQ C:  GNKIHPIGFRLGITRDWESRWYAGKKQYRHLLLEDQRIRG LLEKELYSAGLARVDIERAADNVAVTVHVAKPGVVIGRGG ERIRVLREELAKLTGKNVALNVQEVQNPNLSAPLVAQRVA EQIERRFAVRRAIKQAVQRVMESGAKGAKVIVSGRIGGAE QARTEWAAQGRVPLHTLRANIDYGFALARTTYGVLGVKAY IFLGEV D:  GRYIGPVCRLCRREGVKLYLKGERCYSPKCAMERRPYPPG QHGQKRARRPSDYAVRLREKQKLRRIYGISERQFRNLFEE ASKKKGVTGSVFLGLLESRLDNVVYRLGFAVSRRQARQLV RHGHITVNGRRVDLPSYRVRPGDEIAVAEKSRNLELIRQN LEAMKGRKVGPWLSLDVEGMKGKFLRLPDREDLALPVNEQ LVIEFYSR E:  DFEEKMILIRRTARMQAGGRRFRFGALVVVGDRQGRVGLG FGKAPEVPLAVQKAGYYARRNMVEVPLQNGTIPHEIEVEF GASKIVLKPAAPGTGVIAGAVPRAILELAGVTDILTKELG SRNPINIAYATMEALRQLRTKADVERLRKG F:  MRRYEVNIVLNPNLDQSQLALEKEIIQRALENYGARVEKV EELGLRRLAYPIAKDPQGYFLWYQVEMPEDRVNDLARELR IRDNVRRVMVVKSQEPFLANA G:  ARRRRAEVRQLQPDLVYGDVLVTAFINKIMRDGKKNLAAR IFYDACKIIQEKTGQEPLKVFKQAVENVKPRMEVRSRRVG GANYQVPMEVSPRRQQSLALRWLVQAANQRPERRAAVRIA HELMDAAEGKGGAVKKKEDVERMAEANRAYAHYRW H:  MLTDPIADMLTRIRNATRVYKESTDVPASRFKEEILRILA REGFIKGYERVDVDGKPYLRVYLKYGPRRQGPDPRPEQVI HHIRRISKPGRRVYVGVKEIPRVRRGLGIAILSTSKGVLT DREARKLGVGGELICEVW I:  EQYYGTGRRKEAVARVFLRPGNGKVTVNGQDFNEYFQGLV RAVAALEPLRAVDALGRFDAYITVRGGGKSGQIDAIKLGI ARALVQYNPDYRAKLKPLGFLTRDARVVERKKYGKHKARR APQYSKR J:  KIRIKLRGFDHKTLDASAQKIVEAARRSGAQVSGPIPLPT RVRRFTVIRGPFKHKDSREHFELRTHNRLVDIINPNRKTI EQLMTLDLPTGVEIEIKT K:  KRQVASGRAYIHASYNNTIVTITDPDGNPITWSSGGVIGY KGSRKGTPYAAQLAALDAAKKAMAYGMQSVDVIVRGTGAG REQAIRALQASGLQVKSIVDDTPVPHNGCRPKKKFRKAS L:  PTINQLVRKGREKVRKKSKVPALKGAPFRRGVCTVVRTVT PKKPNSALRKVAKVRLTSGYEVTAYIPGEGHNLQEHSVVL IRGGRVKDLPGVRYHIVRGVYDAAGVKDRKKSRSKYGTKK PKEA M:  ARIAGVEIPRNKRVDVALTYIYGIGKARAKEALEKTGINP ATRVKDLTEAEVVRLREYVENTWKLEGELRAEVAANIKRL MDIGCYRGLRHRRGLPVRGQRTRTNARTRKGPRKTVAG N:  ARKALIEKAKRTPKFKVRAYTRCVRCGRARSVYRFFGLCR ICLRELAHKGQLPGVRKASW O:  PITKEEKQKVIQEFARFPGDTGSTEVQVALLTLRINRLSE HLKVHKKDHHSHRGLLMMVGQRRRLLRYLQREDPERYRAL IEKLGIRG P:  MVKIRLARFGSKHNPHYRIVVTDARRKRDGKYIEKIGYYD PRKTTPDWLKVDVERARYWLSVGAQPTDTARRLLRQAGVF RQE Q:  PKKVLTGVVVSDKMQKTVTVLVERQFPHPLYGKVIKRSKK YLAHDPEEKYKLGDVVEIIESRPISKRKRFRVLRLVESGR MDLVEKYLIRRQNYQSLSKRGGKA R:  PSRKAKVKATLGEFDLRDYRNVEVLKRFLSETGKILPRRR TGLSGKEQRILAKTIKRARILGLLPFTEKLVRK S:  PRSLKKGVFVDDHLLEKVLELNAKGEKRLIKTWSRRSTIV PEMVGHTIAVYNGKQHVPVYITENMVGHKLGEFAPTRTYR T:  RNLSALKRHRQSLKRRLRNKAKKSAIKTLSKKAIQLAQEG KAEEALKIMRKAESLIDKAAKGSTLHKNAAARRKSRLMRK VRQLLEAAGAPLIGGGLSA V:  GKGDRRTRRGKIWRGTYGKYRPRK Description (1)  30S Ribosomal Subunit Functional site 1) chain D residue 82 type sequence A description BINDING SITE FOR RESIDUE MG D 215 source : GC2 2) chain D residue 83 type sequence S description BINDING SITE FOR RESIDUE MG D 215 source : GC2 3) chain D residue 85 type sequence K description BINDING SITE FOR RESIDUE MG D 215 source : GC2 4) chain D residue 87 type sequence G description BINDING SITE FOR RESIDUE MG D 215 source : GC2 5) chain D residue 89 type sequence T description BINDING SITE FOR RESIDUE MG D 215 source : GC2 6) chain L residue 48 type sequence P description BINDING SITE FOR RESIDUE MG A 1605 source : GC5 7) chain L residue 49 type sequence N description BINDING SITE FOR RESIDUE MG A 1605 source : GC5 8) chain L residue 48 type sequence P description BINDING SITE FOR RESIDUE MG A 1614 source : HC2 9) chain J residue 57 type sequence K description BINDING SITE FOR RESIDUE MG A 1634 source : JC2 10) chain N residue 2 type sequence A description BINDING SITE FOR RESIDUE MG A 1635 source : JC3 11) chain G residue 2 type sequence A description BINDING SITE FOR RESIDUE MG A 1650 source : KC9 12) chain J residue 57 type sequence K description BINDING SITE FOR RESIDUE MG J 449 source : LC2 13) chain J residue 60 type sequence R description BINDING SITE FOR RESIDUE MG J 449 source : LC2 14) chain E residue 103 type sequence G description BINDING SITE FOR RESIDUE MG E 468 source : MC6 15) chain E residue 104 type sequence A description BINDING SITE FOR RESIDUE MG E 468 source : MC6 16) chain E residue 105 type sequence V description BINDING SITE FOR RESIDUE MG E 468 source : MC6 17) chain E residue 106 type sequence P description BINDING SITE FOR RESIDUE MG E 468 source : MC6 18) chain E residue 122 type sequence E description BINDING SITE FOR RESIDUE MG E 468 source : MC6 19) chain M residue 20 type sequence T description BINDING SITE FOR RESIDUE MG M 475 source : NC3 20) chain M residue 22 type sequence I description BINDING SITE FOR RESIDUE MG M 475 source : NC3 21) chain M residue 23 type sequence Y description BINDING SITE FOR RESIDUE MG M 475 source : NC3 22) chain M residue 25 type sequence I description BINDING SITE FOR RESIDUE MG M 475 source : NC3 23) chain D residue 9 type sequence C description BINDING SITE FOR RESIDUE ZN D 306 source : PC3 24) chain D residue 12 type sequence C description BINDING SITE FOR RESIDUE ZN D 306 source : PC3 25) chain D residue 19 type sequence L description BINDING SITE FOR RESIDUE ZN D 306 source : PC3 26) chain D residue 26 type sequence C description BINDING SITE FOR RESIDUE ZN D 306 source : PC3 27) chain D residue 31 type sequence C description BINDING SITE FOR RESIDUE ZN D 306 source : PC3 28) chain N residue 24 type sequence C description BINDING SITE FOR RESIDUE ZN N 307 source : PC4 29) chain N residue 27 type sequence C description BINDING SITE FOR RESIDUE ZN N 307 source : PC4 30) chain N residue 40 type sequence C description BINDING SITE FOR RESIDUE ZN N 307 source : PC4 31) chain N residue 43 type sequence C description BINDING SITE FOR RESIDUE ZN N 307 source : PC4 32) chain D residue 97-121 type prosite sequence LESRLDNVVYRLGFAVSRRQARQLV description RIBOSOMAL_S4 Ribosomal protein S4 signature. LEsRLdnvVYRlgfAvSrrqARqLV source prosite : PS00632 33) chain B residue 7-18 type prosite sequence VKELLEAGVHFG description RIBOSOMAL_S2_1 Ribosomal protein S2 signature 1. VkELLEAGVHFG source prosite : PS00962 34) chain J residue 27-42 type prosite sequence ARRSGAQVSGPIPLPT description RIBOSOMAL_S10 Ribosomal protein S10 signature. ArrsGAqvsGPIpLPT source prosite : PS00361 35) chain K residue 95-117 type prosite sequence IRALQASGLQVKSIVDDTPVPHN description RIBOSOMAL_S11 Ribosomal protein S11 signature. IrALqaS.GLqVksivDdTPvPHN source prosite : PS00054 36) chain G residue 20-46 type prosite sequence DVLVTAFINKIMRDGKKNLAARIFYDA description RIBOSOMAL_S7 Ribosomal protein S7 signature. DvLvtaFInkimrdGKKnlaarIFydA source prosite : PS00052 37) chain O residue 39-69 type prosite sequence LSEHLKVHKKDHHSHRGLLMMVGQRRRLLRY description RIBOSOMAL_S15 Ribosomal protein S15 signature. LseHLkvhKkDhhShrgLlmMvgqrrrLlrY source prosite : PS00362 38) chain R residue 32-55 type prosite sequence RDYRNVEVLKRFLSETGKILPRRR description RIBOSOMAL_S18 Ribosomal protein S18 signature. RDYrn.VevLkrFLSEt.GKIlprRR source prosite : PS00057 39) 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 40) chain S residue 53-77 type prosite sequence NGKQHVPVYITENMVGHKLGEFAPT description RIBOSOMAL_S19 Ribosomal protein S19 signature. NGKqhvpvyItenmVGhkLGEFapT source prosite : PS00323 41) chain C residue 163-197 type prosite sequence ARTEWAAQGRVPLHTLRANIDYGFALARTTYGVLG description RIBOSOMAL_S3 Ribosomal protein S3 signature. ARtewaaqGrVplHt..LranIDygfalarTtyGvlG source prosite : PS00548 42) chain I residue 67-85 type prosite sequence GGGKSGQIDAIKLGIARAL description RIBOSOMAL_S9 Ribosomal protein S9 signature. GGGksGQidAiklGiARAL source prosite : PS00360 43) chain Q residue 54-66 type prosite sequence GDVVEIIESRPIS description RIBOSOMAL_S17 Ribosomal protein S17 signature. GDvVeIiEsRPIS source prosite : PS00056 44) chain H residue 108-125 type prosite sequence GIAILSTSKGVLTDREAR description RIBOSOMAL_S8 Ribosomal protein S8 signature. GiaILSTSkGVLtdreAR source prosite : PS00053 45) chain F residue 44-53 type prosite sequence GLRRLAYPIA description RIBOSOMAL_S6 Ribosomal protein S6 signature. GlRRLAYpIA source prosite : PS01048 46) chain L residue 46-53 type prosite sequence KKPNSALR description RIBOSOMAL_S12 Ribosomal protein S12 signature. KkPNSAlR source prosite : PS00055 47) chain E residue 23-55 type prosite sequence GRRFRFGALVVVGDRQGRVGLGFGKAPEVPLAV description RIBOSOMAL_S5 Ribosomal protein S5 signature. GRrfrFgAlvVVGDrq.GrVGlGfgkap.EVpl.AV source prosite : PS00585 48) chain M residue 88-101 type prosite sequence RGLRHRRGLPVRGQ description RIBOSOMAL_S13_1 Ribosomal protein S13 signature. RGlRHrrGlpVRGQ source prosite : PS00646 49) chain N residue 23-45 type prosite sequence RCVRCGRARSVYRFFGLCRICLR description RIBOSOMAL_S14 Ribosomal protein S14 signature. R.CvrcgrarsvyrfFGLCRiCLR source prosite : PS00527 50) chain N residue 25 type BINDING sequence V description BINDING => ECO:0000255|HAMAP-Rule:MF_01364 source Swiss-Prot : SWS_FT_FI1 51) chain N residue 28 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_01364 source Swiss-Prot : SWS_FT_FI1 52) chain N residue 41 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_01364 source Swiss-Prot : SWS_FT_FI1 53) chain N residue 44 type BINDING sequence L description BINDING => ECO:0000255|HAMAP-Rule:MF_01364 source Swiss-Prot : SWS_FT_FI1 54) chain N residue 24 type BINDING sequence C description BINDING => ECO:0000269|PubMed:11866529 source Swiss-Prot : SWS_FT_FI2 55) chain N residue 27 type BINDING sequence C description BINDING => ECO:0000269|PubMed:11866529 source Swiss-Prot : SWS_FT_FI2 56) chain N residue 40 type BINDING sequence C description BINDING => ECO:0000269|PubMed:11866529 source Swiss-Prot : SWS_FT_FI2 57) chain N residue 43 type BINDING sequence C description BINDING => ECO:0000269|PubMed:11866529 source Swiss-Prot : SWS_FT_FI2

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