eF-site ID 5ezy-D PDB Code 5ezy Chain D click to enlarge Title Crystal structure of T2R-TTL-taccalonolide AJ complex Classification STRUCTURAL PROTEIN Compound Tubulin alpha-1B chain Source ORGANISM_COMMON: Pig; ORGANISM_SCIENTIFIC: Sus scrofa; Sequence D:  MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDS DLQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGP FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP DRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETY CIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQ YRALTVPELTQQMFDSKNMMAACDPRHGRYLTVAAIFRGR MSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG LKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG EGMDEMEFTEAESNMNDLVSEYQQYQDATAD Description Functional site 1) chain D residue 254 type sequence K description binding site for residue GTP C 501 source : AC9 2) chain D residue 10 type sequence G description binding site for residue GTP D 501 source : AD3 3) chain D residue 11 type sequence Q description binding site for residue GTP D 501 source : AD3 4) chain D residue 12 type sequence C description binding site for residue GTP D 501 source : AD3 5) chain D residue 15 type sequence Q description binding site for residue GTP D 501 source : AD3 6) chain D residue 98 type sequence G description binding site for residue GTP D 501 source : AD3 7) chain D residue 99 type sequence A description binding site for residue GTP D 501 source : AD3 8) chain D residue 100 type sequence G description binding site for residue GTP D 501 source : AD3 9) chain D residue 101 type sequence N description binding site for residue GTP D 501 source : AD3 10) chain D residue 140 type sequence S description binding site for residue GTP D 501 source : AD3 11) chain D residue 143 type sequence G description binding site for residue GTP D 501 source : AD3 12) chain D residue 144 type sequence G description binding site for residue GTP D 501 source : AD3 13) chain D residue 145 type sequence T description binding site for residue GTP D 501 source : AD3 14) chain D residue 146 type sequence G description binding site for residue GTP D 501 source : AD3 15) chain D residue 177 type sequence V description binding site for residue GTP D 501 source : AD3 16) chain D residue 178 type sequence S description binding site for residue GTP D 501 source : AD3 17) chain D residue 183 type sequence E description binding site for residue GTP D 501 source : AD3 18) chain D residue 206 type sequence N description binding site for residue GTP D 501 source : AD3 19) chain D residue 224 type sequence Y description binding site for residue GTP D 501 source : AD3 20) chain D residue 228 type sequence N description binding site for residue GTP D 501 source : AD3 21) chain D residue 217 type sequence L description binding site for residue TAJ D 503 source : AD5 22) chain D residue 219 type sequence L description binding site for residue TAJ D 503 source : AD5 23) chain D residue 225 type sequence G description binding site for residue TAJ D 503 source : AD5 24) chain D residue 226 type sequence D description binding site for residue TAJ D 503 source : AD5 25) chain D residue 229 type sequence H description binding site for residue TAJ D 503 source : AD5 26) chain D residue 278 type sequence R description binding site for residue TAJ D 503 source : AD5 27) chain D residue 282 type sequence Q description binding site for residue TAJ D 503 source : AD5 28) chain D residue 370 type sequence G description binding site for residue TAJ D 503 source : AD5 29) chain D 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 30) chain D 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 31) chain D residue 60 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI5 32) chain D residue 174 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q9BVA1 source Swiss-Prot : SWS_FT_FI6 33) chain D residue 287 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 34) chain D residue 292 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 35) chain D residue 144 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 36) chain D residue 145 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 37) chain D residue 146 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 38) chain D residue 206 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 39) chain D residue 228 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 40) chain D residue 11 type MOD_RES sequence Q description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 41) chain D residue 140 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 42) chain D residue 71 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 43) chain D residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 44) chain D residue 57 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q3KRE8 source Swiss-Prot : SWS_FT_FI4 45) chain D 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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