eF-site ID 4u3j-ABC PDB Code 4u3j Chain A, B, C click to enlarge Title TOG2:alpha/beta-tubulin complex Classification STRUCTURAL PROTEIN/Protein binding Compound Tubulin alpha-1 chain Source (STU2_YEAST) Sequence A:  MREVISINVGQAGCQIGNACWELYSLEHGIKPDGHLEDGL SKPKGGEEGFSTFFHETGYGKFVPRAIYVDLEPNVIDEVR NGPYKDLFHPEQLISGKEDAANNYARGHYTVGREILGDVL DRIRKLADQCDGLQGFLFTHSLGGGTGSGLGSLLLEELSA EYGKKSKLEFAVYPAPQVSTSVVEPYNTVLTTHTTLEHAD CTFMVDNEAIYDMCKRNLDIPRPSFANLNNLIAQVVSSVT ASLRFDGSLNVDLNEFQTNLVPYPRIHFPLVSYSPVLSKS SVSEITNACFEPGNQMVKCDPRDGKYMATCLLYRGDVVTR DVQRAVEQVKNKKTVQLVDWCPTGFKIGICYEPPTATPNS QLATVDRAVCMLSNTTSIAEAWKRIDRKFDLMYAKRAFVH WYVGEGMEEGEFTEAREDLAALERDYIEVGA B:  MREIIHISTGQCGNQIGAAFWETICGEHGLDFNGTYHGHD DIQKERLNVYFNEASSGKWVPRSINVDLEPGTIDAVRNSA IGNLFRPDNYIFGQSSAGNVWAKGHYTEGAELVDSVMDVI RREAEGCDSLQGFQITHSLGGGTGSGMGTLLISKIREEFP DRMMATFSVLPSPKTRVEPYNATLSVHQLVEHSDETFCID NEALYDICQLKQPSYGDLNNLVSSVMSGVTTSLRYPGQLN SDLRKLAVNLVPFPRLHFFMVGYAPLTARSLTVPELTQQM FDAKNMMAAADPRNGRYLTVAAFFRGKVSVKEVEDEMHKV QSKNSDYFVEWIPNNVQTAVCSVAPQGLDMAATFIANSTS IQELFKRVGDQFSAMFKRKAFLHWYTSEGMDELEFSEAES NMNDLVSEYQQYQEATV C:  LPEETILDKLPKDFQERITSSKWKDRVEALEEFWDSVLSQ TKKLKSTSQNYSNLLGIYGHIIQKDANIQAVALAAQSVEL ICDKLKTPGFSKDYVSLVFTPLLDRTKEKKPSVIEAIRKA LLTICKYYDPLASSGRNEDMLKDILEHMKHKTPQIRMECT QLFNASMKEEKDGYSTLQRYLKDEVVPIVIQIVNDTQPAI RTIGFESFAILIKIFGMNTFVKTLEHLDNLKRKKIEETVK T Description Functional site 1) chain A residue 11 type sequence Q description binding site for residue MG A 501 source : AC1 2) chain A residue 72 type sequence E description binding site for residue MG A 501 source : AC1 3) chain A residue 10 type sequence G description binding site for residue GTP A 502 source : AC2 4) chain A residue 11 type sequence Q description binding site for residue GTP A 502 source : AC2 5) chain A residue 12 type sequence A description binding site for residue GTP A 502 source : AC2 6) chain A residue 15 type sequence Q description binding site for residue GTP A 502 source : AC2 7) chain A residue 101 type sequence A description binding site for residue GTP A 502 source : AC2 8) chain A residue 102 type sequence N description binding site for residue GTP A 502 source : AC2 9) chain A residue 141 type sequence S description binding site for residue GTP A 502 source : AC2 10) chain A residue 144 type sequence G description binding site for residue GTP A 502 source : AC2 11) chain A residue 145 type sequence G description binding site for residue GTP A 502 source : AC2 12) chain A residue 146 type sequence T description binding site for residue GTP A 502 source : AC2 13) chain A residue 147 type sequence G description binding site for residue GTP A 502 source : AC2 14) chain A residue 178 type sequence V description binding site for residue GTP A 502 source : AC2 15) chain A residue 180 type sequence T description binding site for residue GTP A 502 source : AC2 16) chain A residue 184 type sequence E description binding site for residue GTP A 502 source : AC2 17) chain A residue 207 type sequence N description binding site for residue GTP A 502 source : AC2 18) chain A residue 225 type sequence F description binding site for residue GTP A 502 source : AC2 19) chain A residue 229 type sequence N description binding site for residue GTP A 502 source : AC2 20) chain A residue 232 type sequence I description binding site for residue GTP A 502 source : AC2 21) chain B residue 252 type sequence K description binding site for residue GTP A 502 source : AC2 22) chain B residue 10 type sequence G description binding site for residue GTP B 502 source : AC4 23) chain B residue 11 type sequence Q description binding site for residue GTP B 502 source : AC4 24) chain B residue 12 type sequence C description binding site for residue GTP B 502 source : AC4 25) chain B residue 15 type sequence Q description binding site for residue GTP B 502 source : AC4 26) chain B residue 97 type sequence A description binding site for residue GTP B 502 source : AC4 27) chain B residue 99 type sequence N description binding site for residue GTP B 502 source : AC4 28) chain B residue 138 type sequence S description binding site for residue GTP B 502 source : AC4 29) chain B residue 141 type sequence G description binding site for residue GTP B 502 source : AC4 30) chain B residue 142 type sequence G description binding site for residue GTP B 502 source : AC4 31) chain B residue 143 type sequence T description binding site for residue GTP B 502 source : AC4 32) chain B residue 144 type sequence G description binding site for residue GTP B 502 source : AC4 33) chain B residue 181 type sequence E description binding site for residue GTP B 502 source : AC4 34) chain B residue 204 type sequence N description binding site for residue GTP B 502 source : AC4 35) chain B residue 222 type sequence Y description binding site for residue GTP B 502 source : AC4 36) chain B residue 226 type sequence N description binding site for residue GTP B 502 source : AC4 37) chain A residue 143-149 type prosite sequence GGGTGSG description TUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG source prosite : PS00227 38) chain B residue 140-146 type prosite sequence GGGTGSG description TUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG source prosite : PS00227 39) chain B residue 1-4 type prosite sequence MREI description TUBULIN_B_AUTOREG Tubulin-beta mRNA autoregulation signal. MREI source prosite : PS00228 40) chain B residue 11 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 41) chain B residue 138 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 42) chain B residue 142 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 43) chain B residue 143 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 44) chain B residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 45) chain B residue 204 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 46) chain B residue 226 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 47) chain B residue 69 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 48) chain A residue 72 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 49) chain A residue 141 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 50) chain A residue 145 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 51) chain A residue 146 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 52) chain A residue 180 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 53) chain A residue 207 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 54) chain A residue 229 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2

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