eF-site ID 5nqu-ABF PDB Code 5nqu Chain A, B, F click to enlarge Title Tubulin Darpin cryo structure Classification CELL CYCLE Compound Tubulin alpha-1B chain Source ORGANISM_COMMON: cattle; ORGANISM_SCIENTIFIC: Bos taurus; Sequence A:  MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPDSF NTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHP EQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQC TGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEF SIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAI YDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALN VDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVA EITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVN AAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLA KVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYV GEGMEEGEFSEAREDMAALEKDYEEVGV B:  MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDS DLQLERINVYYNEAKYVPRAILVDLEPGTMDSVRSGPFGQ IFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKE SESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRI MNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYCID NEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFP GQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRLTVPELT QQMFDSKNMMAACDPRHGRYLTVAAIFRGRMSMKEVDEQM LNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGN STAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTE AESNMNDLVSEYQQYQDATAD F:  DLGKKLLEAARAGQDDEVRILMANGADVNATDASGLTPLH LAATYGHLEIVEVLLKHGADVNAIDIMGSTPLHLAALIGH LEIVEVLLKHGADVNAVDTWGDTPLHLAAIMGHLEIVEVL LKHGADVNAQDKFGKTAFDISIDNGNEDLAEILQK Description (1)  Lysozyme C (E.C.3.2.1.17) Functional site 1) chain A residue 10 type sequence G description binding site for residue GTP A 501 source : AC1 2) chain A residue 11 type sequence Q description binding site for residue GTP A 501 source : AC1 3) chain A residue 12 type sequence A description binding site for residue GTP A 501 source : AC1 4) chain A residue 15 type sequence Q description binding site for residue GTP A 501 source : AC1 5) chain A residue 98 type sequence D description binding site for residue GTP A 501 source : AC1 6) chain A residue 99 type sequence A description binding site for residue GTP A 501 source : AC1 7) chain A residue 101 type sequence N description binding site for residue GTP A 501 source : AC1 8) chain A residue 140 type sequence S description binding site for residue GTP A 501 source : AC1 9) chain A residue 143 type sequence G description binding site for residue GTP A 501 source : AC1 10) chain A residue 144 type sequence G description binding site for residue GTP A 501 source : AC1 11) chain A residue 145 type sequence T description binding site for residue GTP A 501 source : AC1 12) chain A residue 146 type sequence G description binding site for residue GTP A 501 source : AC1 13) chain A residue 177 type sequence V description binding site for residue GTP A 501 source : AC1 14) chain A residue 183 type sequence E description binding site for residue GTP A 501 source : AC1 15) chain A residue 206 type sequence N description binding site for residue GTP A 501 source : AC1 16) chain A residue 224 type sequence Y description binding site for residue GTP A 501 source : AC1 17) chain A residue 228 type sequence N description binding site for residue GTP A 501 source : AC1 18) chain A residue 231 type sequence I description binding site for residue GTP A 501 source : AC1 19) chain B residue 254 type sequence K description binding site for residue GTP A 501 source : AC1 20) chain B residue 10 type sequence G description binding site for residue GDP B 501 source : AC3 21) chain B residue 11 type sequence Q description binding site for residue GDP B 501 source : AC3 22) chain B residue 12 type sequence C description binding site for residue GDP B 501 source : AC3 23) chain B residue 15 type sequence Q description binding site for residue GDP B 501 source : AC3 24) chain B residue 140 type sequence S description binding site for residue GDP B 501 source : AC3 25) chain B residue 143 type sequence G description binding site for residue GDP B 501 source : AC3 26) chain B residue 144 type sequence G description binding site for residue GDP B 501 source : AC3 27) chain B residue 145 type sequence T description binding site for residue GDP B 501 source : AC3 28) chain B residue 146 type sequence G description binding site for residue GDP B 501 source : AC3 29) chain B residue 177 type sequence V description binding site for residue GDP B 501 source : AC3 30) chain B residue 178 type sequence S description binding site for residue GDP B 501 source : AC3 31) chain B residue 183 type sequence E description binding site for residue GDP B 501 source : AC3 32) chain B residue 206 type sequence N description binding site for residue GDP B 501 source : AC3 33) chain B residue 224 type sequence Y description binding site for residue GDP B 501 source : AC3 34) chain B residue 228 type sequence N description binding site for residue GDP B 501 source : AC3 35) chain B residue 11 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 36) chain B residue 140 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 37) chain B residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 38) chain B residue 145 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 39) chain B residue 146 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 40) chain B residue 206 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 41) chain B residue 228 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 42) chain A residue 326 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI12 43) chain A residue 370 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI12 44) chain B residue 71 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 45) chain A residue 71 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 46) chain A residue 140 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 47) chain A residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 48) chain A residue 145 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 49) chain A residue 179 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 50) chain A residue 206 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 51) chain A residue 228 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 52) chain B residue 174 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q9BVA1 source Swiss-Prot : SWS_FT_FI6 53) chain B residue 287 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 54) chain B residue 292 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 55) chain B residue 60 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI10 56) chain B residue 320 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI8 57) chain B residue 326 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI11 58) chain B residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 59) chain B residue 60 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI5 60) chain A residue 232 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI5 61) chain B residue 142-148 type prosite sequence GGGTGSG description TUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG source prosite : PS00227 62) chain A residue 142-148 type prosite sequence GGGTGSG description TUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG source prosite : PS00227 63) chain B residue 1-4 type prosite sequence MREI description TUBULIN_B_AUTOREG Tubulin-beta mRNA autoregulation signal. MREI source prosite : PS00228

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