eF-site ID 5xkg-D PDB Code 5xkg Chain D click to enlarge Title Crystal structure of T2R-TTL-CH1 complex Classification STRUCTURAL PROTEIN Compound Tubulin alpha-1B chain Source Sus scrofa (Pig) (E1BQ43_CHICK) Sequence D:  MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDS DLQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGP FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP DRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETY CIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLLTVPELT QQMFDSKNMMAACDPRHGRYLTVAAIFRGRMSMKEVDEQM LNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGN STAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTE AESNMNDLVSEYQQYQDATAD Description Functional site 1) chain D residue 252 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 97 type sequence A description binding site for residue GTP D 501 source : AD3 7) chain D residue 98 type sequence G description binding site for residue GTP D 501 source : AD3 8) chain D residue 99 type sequence N description binding site for residue GTP D 501 source : AD3 9) chain D residue 138 type sequence S description binding site for residue GTP D 501 source : AD3 10) chain D residue 141 type sequence G description binding site for residue GTP D 501 source : AD3 11) chain D residue 142 type sequence G description binding site for residue GTP D 501 source : AD3 12) chain D residue 143 type sequence T description binding site for residue GTP D 501 source : AD3 13) chain D residue 144 type sequence G description binding site for residue GTP D 501 source : AD3 14) chain D residue 175 type sequence V description binding site for residue GTP D 501 source : AD3 15) chain D residue 181 type sequence E description binding site for residue GTP D 501 source : AD3 16) chain D residue 204 type sequence N description binding site for residue GTP D 501 source : AD3 17) chain D residue 222 type sequence Y description binding site for residue GTP D 501 source : AD3 18) chain D residue 226 type sequence N description binding site for residue GTP D 501 source : AD3 19) chain D residue 11 type sequence Q description binding site for residue MG D 502 source : AD4 20) chain D residue 239 type sequence C description binding site for residue 890 D 503 source : AD5 21) chain D residue 248 type sequence A description binding site for residue 890 D 503 source : AD5 22) chain D residue 252 type sequence K description binding site for residue 890 D 503 source : AD5 23) chain D residue 253 type sequence L description binding site for residue 890 D 503 source : AD5 24) chain D residue 256 type sequence N description binding site for residue 890 D 503 source : AD5 25) chain D residue 257 type sequence M description binding site for residue 890 D 503 source : AD5 26) chain D residue 315 type sequence A description binding site for residue 890 D 503 source : AD5 27) chain D residue 316 type sequence I description binding site for residue 890 D 503 source : AD5 28) chain D residue 348 type sequence N description binding site for residue 890 D 503 source : AD5 29) chain D residue 350 type sequence K description binding site for residue 890 D 503 source : AD5 30) chain D 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_FI9 31) chain D residue 142 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 32) chain D residue 143 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 33) chain D residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 34) chain D residue 204 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 35) chain D residue 226 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 36) chain D residue 11 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 37) chain D residue 138 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 38) chain D residue 69 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 39) chain D residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 40) chain D residue 58 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI4 41) chain D residue 172 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885 source Swiss-Prot : SWS_FT_FI5 42) chain D residue 285 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 43) chain D residue 290 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 44) chain D residue 318 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 45) chain D 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_FI10

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