eF-site ID 4r71-ABCDEF PDB Code 4r71 Chain A, B, C, D, E, F click to enlarge Title Structure of the Qbeta holoenzyme complex in the P1211 crystal form Classification VIRAL PROTEIN/RIBOSOMAL PROTEIN Compound Elongation factor Ts, Elongation factor Tu Source null (RS1_ECOLI) Sequence A:  ITASLVKELRERTGAGMMDCKKALTEANGDIELAIENMRK SGAIKAAKKAGNVAADGVIKTKIDGNYGIILEVNCQTDFV AKDAGFQAFADKVLDAAVAGKITDVEVLKAQFEEERVALV AKIGENINIRRVAALEGDVLGSYQHGARIGVLVAAKGADE ELVKHIAMHVAASKPEFIKPEDVSAEVVEKEYQVQLDIAM QSGKPKEIAEKMVEGRMKKFTGEVSLTGQPFVMEPSKTVG QLLKEHNAEVTGFIRFEVGEGIEKVETDFAAEVAAMSKQS KEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGG TSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAIL VVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDE ELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALEGDAE WEAKILELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGR GTVVTGRVERGIIKVGEEVEIVGIKETQKSTCTGVEMFRK LLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIKPHTK FESEVYILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIEL PEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIREGGRTV GAGVVAKVLS B:  MSKTASSRNSLSAQLRRAANTRIEVEGNLALSIANDLLLA YGQSPFNSEAECISFSPRFDGTPDDFRINYLKAEIMSKYD DFSLGIDTEAVAWEKFLAAEAECALTNARLYRPDYSEDFN FSLGESCIHMARRKIAKLIGDVPSVEGMLRHCRFSGGATT TNNRSYGHPSFKFALPQACTPRALKYVLALRASTHFDTRI SDISPFNKAVTVPKNSKTDRCIAIEPGWNMFFQLGIGGIL RDRLRCWGIDLNDQTINQRRAHEGSVTNNLATVDLSAASD SISLALCELLLPPGWFEVLMDLRSPKGRLPDGSVVTYEKI SSMGNGYTFELESLIFASLARSVCEILDLDSSEVTVYGDD IILPSCAVPALREVFKYVGFTTNTKKTFSEGPFRESCGKH YYSGVDVTPFYIRHRIVSPADLILVLNNLYRWATIDGVWD PRAHSVYLKYRKLLPKQLQRNTIPDGYGDGALVGSVLINP FAKNRGWIRYVPVITDHTRDRERAELGSYLYDLFSRCLSS ADLFAIDQLICRSNPTKISRSTGKFDIQYIACSSRV C:  AEITASLVKELRERTGAGMMDCKKALTEANGDIELAIENM RKSGAIKAAKKAGNVAADGVIKTKIDGNYGIILEVNCQTD FVAKDAGFQAFADKVLDAAVAGKITDVEVLKAQFEEERVA LVAKIGENINIRRVAALEGDVLGSYQHGARIGVLVAAKGA DEELVKHIAMHVAASKPEFIKPEDVSAEVVEKEYQVQLDI AMQSGKPKEIAEKMVEGRMKKFTGEVSLTGQPFVMEPSKT VGQLLKEHNAEVTGFIRFEVGEGIEKVETDFAAEVAAMSK KEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGG TSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAIL VVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDE ELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALEGDAE WEAKILELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGR GTVVTGRVERGIIKVGEEVEIVGIKETQKSTCTGVEMFRK LLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIKPHTK FESEVYILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIEL PEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIREGGRTV GAGVVAKVLS D:  SRNSLSAQLRRAANTRIEVEGNLALSIANDLLLAYGQSPF NSEAECISFSPRFDGTPDDFRINYLKAEIMSKYDDFSLGI DTEAVAWEKFLAAEAECALTNARLYRPDYSEDFNFSLGES CIHMARRKIAKLIGDVPSVEGMLRHCRFSGGATTTNNRSY GHPSFKFALPQACTPRALKYVLALRASTHFDTRISDISPF NKAVTVPKNSKTDRCIAIEPGWNMFFQLGIGGILRDRLRC WGIDLNDQTINQRRAHEGSVTNNLATVDLSAASDSISLAL CELLLPPGWFEVLMDLRSPKGRLPDGSVVTYEKISSMGNG YTFELESLIFASLARSVCEILDLDSSEVTVYGDDIILPSC AVPALREVFKYVGFTTNTKKTFSEGPFRESCGKHYYSGVD VTPFYIRHRIVSPADLILVLNNLYRWATIDGVWDPRAHSV YLKYRKLLPKQLQRNTIPDGYGDGALVGSVLINPFAKNRG WIRYVPVITDHTRDRERAELGSYLYDLFSRCLSCDSADLF AIDQLICRSNPTKISRSTGKFDIQYIACSSRVL E:  GTESFAQLFEESLKEIETRPGSIVRGVVVAIDKDVVLVDA GLKSESAIPAEQFKNAQGELEIQVGDEVDVALDAVELLSR EKAKRHEAWITLEKAYEDAETVTGVINGKVKGGFTVELNG IRAFLPGSLTLHLEGKELEFKVIKLDQKRNNVVVSRR F:  GTESFAQLFEESLKEIETRPGSIVRGVVVAIDKDVVLVDA GLKSESAIPAEQFKNAQGELEIQVGDEVDVALDAVETLLS REKAKRHEAWITLEKAYEDAETVTGVINGKVKGGFTVELN GIRAFLPGSLVDVHLEGKELEFKVIKLDQKRNNVVVSRR Description Functional site 1) chain B residue 274 type BINDING sequence D description BINDING => ECO:0000269|PubMed:20798060, ECO:0000269|PubMed:22245970, ECO:0000269|PubMed:22884418 source Swiss-Prot : SWS_FT_FI1 2) chain B residue 359 type BINDING sequence D description BINDING => ECO:0000269|PubMed:20798060, ECO:0000269|PubMed:22245970, ECO:0000269|PubMed:22884418 source Swiss-Prot : SWS_FT_FI1 3) chain B residue 360 type BINDING sequence D description BINDING => ECO:0000269|PubMed:20798060, ECO:0000269|PubMed:22245970, ECO:0000269|PubMed:22884418 source Swiss-Prot : SWS_FT_FI1 4) chain D residue 274 type BINDING sequence D description BINDING => ECO:0000269|PubMed:20798060, ECO:0000269|PubMed:22245970, ECO:0000269|PubMed:22884418 source Swiss-Prot : SWS_FT_FI1 5) chain D residue 359 type BINDING sequence D description BINDING => ECO:0000269|PubMed:20798060, ECO:0000269|PubMed:22245970, ECO:0000269|PubMed:22884418 source Swiss-Prot : SWS_FT_FI1 6) chain D residue 360 type BINDING sequence D description BINDING => ECO:0000269|PubMed:20798060, ECO:0000269|PubMed:22245970, ECO:0000269|PubMed:22884418 source Swiss-Prot : SWS_FT_FI1 7) chain A residue 1002 type MOD_RES sequence S description N-acetylserine => ECO:0000269|PubMed:6997043, ECO:0000269|PubMed:7021545 source Swiss-Prot : SWS_FT_FI2 8) chain A residue 1038 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI3 9) chain A residue 1177 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI3 10) chain A residue 1249 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI3 11) chain A residue 1253 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI3 12) chain A residue 1295 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI3 13) chain C residue 1037 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI3 14) chain C residue 1176 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI3 15) chain C residue 1248 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI3 16) chain C residue 1252 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI3 17) chain C residue 1294 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI3 18) chain A residue 1314 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI5 19) chain C residue 1313 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI5 20) chain A residue 1383 type MOD_RES sequence T description Phosphothreonine => ECO:0000305|PubMed:19150849, ECO:0000305|PubMed:24141193, ECO:0000305|PubMed:8416965 source Swiss-Prot : SWS_FT_FI6 21) chain C residue 1382 type MOD_RES sequence T description Phosphothreonine => ECO:0000305|PubMed:19150849, ECO:0000305|PubMed:24141193, ECO:0000305|PubMed:8416965 source Swiss-Prot : SWS_FT_FI6 22) chain A residue 12-27 type prosite sequence LRERTGAGMMDCKKAL description EF_TS_1 Elongation factor Ts signature 1. LRerTGaGMmDcKKAL source prosite : PS01126 23) chain A residue 75-85 type prosite sequence EVNCQTDFVAK description EF_TS_2 Elongation factor Ts signature 2. EVNCQTDFVAK source prosite : PS01127

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