eF-site ID 5nqu-B PDB Code 5nqu Chain B 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 B:  MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDS DLQLERINVYYNEAKYVPRAILVDLEPGTMDSVRSGPFGQ IFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKE SESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRI MNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYCID NEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFP GQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRLTVPELT QQMFDSKNMMAACDPRHGRYLTVAAIFRGRMSMKEVDEQM LNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGN STAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTE AESNMNDLVSEYQQYQDATAD Description (1)  Lysozyme C (E.C.3.2.1.17) Functional site 1) chain B residue 254 type sequence K description binding site for residue GTP A 501 source : AC1 2) chain B residue 10 type sequence G description binding site for residue GDP B 501 source : AC3 3) chain B residue 11 type sequence Q description binding site for residue GDP B 501 source : AC3 4) chain B residue 12 type sequence C description binding site for residue GDP B 501 source : AC3 5) chain B residue 15 type sequence Q description binding site for residue GDP B 501 source : AC3 6) chain B residue 140 type sequence S description binding site for residue GDP B 501 source : AC3 7) chain B residue 143 type sequence G description binding site for residue GDP B 501 source : AC3 8) chain B residue 144 type sequence G description binding site for residue GDP B 501 source : AC3 9) chain B residue 145 type sequence T description binding site for residue GDP B 501 source : AC3 10) chain B residue 146 type sequence G description binding site for residue GDP B 501 source : AC3 11) chain B residue 177 type sequence V description binding site for residue GDP B 501 source : AC3 12) chain B residue 178 type sequence S description binding site for residue GDP B 501 source : AC3 13) chain B residue 183 type sequence E description binding site for residue GDP B 501 source : AC3 14) chain B residue 206 type sequence N description binding site for residue GDP B 501 source : AC3 15) chain B residue 224 type sequence Y description binding site for residue GDP B 501 source : AC3 16) chain B residue 228 type sequence N description binding site for residue GDP B 501 source : AC3 17) 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 18) 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 19) chain B residue 142-148 type prosite sequence GGGTGSG description TUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG source prosite : PS00227 20) chain B residue 1-4 type prosite sequence MREI description TUBULIN_B_AUTOREG Tubulin-beta mRNA autoregulation signal. MREI source prosite : PS00228 21) chain B residue 140 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 22) chain B residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 23) chain B residue 145 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 24) chain B residue 146 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 25) chain B residue 206 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 26) chain B residue 228 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 27) chain B residue 11 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 28) chain B residue 71 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 29) chain B residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 30) chain B residue 60 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI5 31) chain B residue 174 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q9BVA1 source Swiss-Prot : SWS_FT_FI6 32) chain B residue 292 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 33) chain B residue 287 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 34) chain B residue 320 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI8

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