eF-site ID 5zxh-B PDB Code 5zxh Chain B click to enlarge Title The structure of MT189-tubulin complex Classification STRUCTURAL PROTEIN Compound Tubulin alpha-1B chain Source (E1BQ43_CHICK) Sequence B:  MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDS DLQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGP FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP DRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETY CIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSQYRAL TVPELTQQMFDSKNMMAACDPRHGRYLTVAAVFRGRMSMK EVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMS ATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMD EMEFTEAESNMNDLVSEYQQYQDA Description Functional site 1) chain B residue 252 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 : AC4 3) chain B residue 11 type sequence Q description binding site for residue GDP B 501 source : AC4 4) chain B residue 12 type sequence C description binding site for residue GDP B 501 source : AC4 5) chain B residue 15 type sequence Q description binding site for residue GDP B 501 source : AC4 6) chain B residue 138 type sequence S description binding site for residue GDP B 501 source : AC4 7) chain B residue 141 type sequence G description binding site for residue GDP B 501 source : AC4 8) chain B residue 142 type sequence G description binding site for residue GDP B 501 source : AC4 9) chain B residue 143 type sequence T description binding site for residue GDP B 501 source : AC4 10) chain B residue 144 type sequence G description binding site for residue GDP B 501 source : AC4 11) chain B residue 171 type sequence P description binding site for residue GDP B 501 source : AC4 12) chain B residue 175 type sequence V description binding site for residue GDP B 501 source : AC4 13) chain B residue 177 type sequence D description binding site for residue GDP B 501 source : AC4 14) chain B residue 181 type sequence E description binding site for residue GDP B 501 source : AC4 15) chain B residue 204 type sequence N description binding site for residue GDP B 501 source : AC4 16) chain B residue 222 type sequence Y description binding site for residue GDP B 501 source : AC4 17) chain B residue 226 type sequence N description binding site for residue GDP B 501 source : AC4 18) chain B residue 11 type sequence Q description binding site for residue MG B 502 source : AC5 19) chain B residue 177 type sequence D description binding site for residue MG B 502 source : AC5 20) chain B residue 156 type sequence R description binding site for residue MES B 503 source : AC6 21) chain B residue 160 type sequence P description binding site for residue MES B 503 source : AC6 22) chain B residue 161 type sequence D description binding site for residue MES B 503 source : AC6 23) chain B residue 162 type sequence R description binding site for residue MES B 503 source : AC6 24) chain B residue 195 type sequence N description binding site for residue MES B 503 source : AC6 25) chain B residue 197 type sequence D description binding site for residue MES B 503 source : AC6 26) chain B residue 251 type sequence R description binding site for residue MES B 503 source : AC6 27) chain B residue 111 type sequence E description binding site for residue CA B 504 source : AC7 28) chain B residue 294 type sequence F description binding site for residue MES B 505 source : AC8 29) chain B residue 295 type sequence D description binding site for residue MES B 505 source : AC8 30) chain B residue 296 type sequence S description binding site for residue MES B 505 source : AC8 31) chain B residue 305 type sequence P description binding site for residue MES B 505 source : AC8 32) chain B residue 306 type sequence R description binding site for residue MES B 505 source : AC8 33) chain B residue 310 type sequence Y description binding site for residue MES B 505 source : AC8 34) chain B residue 337 type sequence N description binding site for residue MES B 505 source : AC8 35) chain B residue 236 type sequence V description binding site for residue 9LX B 506 source : AC9 36) chain B residue 239 type sequence C description binding site for residue 9LX B 506 source : AC9 37) chain B residue 246 type sequence L description binding site for residue 9LX B 506 source : AC9 38) chain B residue 249 type sequence D description binding site for residue 9LX B 506 source : AC9 39) chain B residue 253 type sequence L description binding site for residue 9LX B 506 source : AC9 40) chain B residue 256 type sequence N description binding site for residue 9LX B 506 source : AC9 41) chain B residue 257 type sequence M description binding site for residue 9LX B 506 source : AC9 42) chain B residue 313 type sequence V description binding site for residue 9LX B 506 source : AC9 43) chain B residue 314 type sequence A description binding site for residue 9LX B 506 source : AC9 44) chain B residue 316 type sequence V description binding site for residue 9LX B 506 source : AC9 45) chain B residue 348 type sequence N description binding site for residue 9LX B 506 source : AC9 46) chain B residue 350 type sequence K description binding site for residue 9LX B 506 source : AC9 47) chain B residue 351 type sequence T description binding site for residue 9LX B 506 source : AC9 48) chain B residue 352 type sequence A description binding site for residue 9LX B 506 source : AC9 49) chain B residue 58 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 50) chain B residue 324 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 51) chain B residue 140-146 type prosite sequence GGGTGSG description TUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG source prosite : PS00227 52) chain B residue 1-4 type prosite sequence MREI description TUBULIN_B_AUTOREG Tubulin-beta mRNA autoregulation signal. MREI source prosite : PS00228 53) chain B residue 142 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 54) chain B residue 143 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 55) chain B residue 144 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 56) chain B residue 204 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 57) chain B residue 226 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 58) chain B residue 138 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 59) chain B residue 69 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 60) chain B residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 61) chain B residue 55 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q3KRE8 source Swiss-Prot : SWS_FT_FI4 62) chain B residue 58 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI5 63) chain B residue 172 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q9BVA1 source Swiss-Prot : SWS_FT_FI6 64) chain B residue 285 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 65) chain B residue 290 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 66) chain B residue 318 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI8

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