eF-site ID 5ezy-C PDB Code 5ezy Chain C 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 C:  MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDK TIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT GTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD RIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVD YGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDC AFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEK AYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR GDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPP TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYA KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSV Description Functional site 1) chain C residue 10 type sequence G description binding site for residue GTP C 501 source : AC9 2) chain C residue 11 type sequence Q description binding site for residue GTP C 501 source : AC9 3) chain C residue 12 type sequence A description binding site for residue GTP C 501 source : AC9 4) chain C residue 15 type sequence Q description binding site for residue GTP C 501 source : AC9 5) chain C residue 98 type sequence D description binding site for residue GTP C 501 source : AC9 6) chain C residue 99 type sequence A description binding site for residue GTP C 501 source : AC9 7) chain C residue 100 type sequence A description binding site for residue GTP C 501 source : AC9 8) chain C residue 101 type sequence N description binding site for residue GTP C 501 source : AC9 9) chain C residue 140 type sequence S description binding site for residue GTP C 501 source : AC9 10) chain C residue 143 type sequence G description binding site for residue GTP C 501 source : AC9 11) chain C residue 144 type sequence G description binding site for residue GTP C 501 source : AC9 12) chain C residue 145 type sequence T description binding site for residue GTP C 501 source : AC9 13) chain C residue 146 type sequence G description binding site for residue GTP C 501 source : AC9 14) chain C residue 171 type sequence I description binding site for residue GTP C 501 source : AC9 15) chain C residue 177 type sequence V description binding site for residue GTP C 501 source : AC9 16) chain C residue 183 type sequence E description binding site for residue GTP C 501 source : AC9 17) chain C residue 206 type sequence N description binding site for residue GTP C 501 source : AC9 18) chain C residue 224 type sequence Y description binding site for residue GTP C 501 source : AC9 19) chain C residue 228 type sequence N description binding site for residue GTP C 501 source : AC9 20) chain C residue 231 type sequence I description binding site for residue GTP C 501 source : AC9 21) chain C residue 39 type sequence D description binding site for residue CA C 503 source : AD2 22) chain C residue 41 type sequence T description binding site for residue CA C 503 source : AD2 23) chain C residue 44 type sequence G description binding site for residue CA C 503 source : AD2 24) chain C residue 55 type sequence E description binding site for residue CA C 503 source : AD2 25) chain C residue 326 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 26) chain C residue 370 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 27) chain C residue 71 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 28) chain C residue 140 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 29) chain C residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 30) chain C residue 145 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 31) chain C residue 179 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 32) chain C residue 206 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 33) chain C residue 228 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 34) chain C residue 11 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 35) chain C residue 48 type MOD_RES sequence S description Phosphothreonine => ECO:0000250|UniProtKB:Q3KRE8 source Swiss-Prot : SWS_FT_FI4 36) chain C residue 232 type MOD_RES sequence S description Phosphothreonine => ECO:0000250|UniProtKB:Q3KRE8 source Swiss-Prot : SWS_FT_FI4

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