eF-site ID 4yj3-C PDB Code 4yj3 Chain C click to enlarge Title Crystal structure of tubulin bound to compound 2 Classification CELL CYCLE Compound Tubulin alpha-1B chain Source ORGANISM_COMMON: Bovine; ORGANISM_SCIENTIFIC: Bos taurus; Sequence C:  MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDK TIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT GTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD RIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVD YGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDC AFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEK AYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR GDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPP TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYA KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSV Description Functional site 1) chain C residue 282 type sequence Y description binding site for residue CA B 504 source : AC7 2) chain C residue 11 type sequence Q description binding site for residue MG C 501 source : AC9 3) chain C residue 71 type sequence E description binding site for residue MG C 501 source : AC9 4) chain C residue 10 type sequence G description binding site for residue GTP C 502 source : AD1 5) chain C residue 11 type sequence Q description binding site for residue GTP C 502 source : AD1 6) chain C residue 12 type sequence A description binding site for residue GTP C 502 source : AD1 7) chain C residue 15 type sequence Q description binding site for residue GTP C 502 source : AD1 8) chain C residue 98 type sequence D description binding site for residue GTP C 502 source : AD1 9) chain C residue 99 type sequence A description binding site for residue GTP C 502 source : AD1 10) chain C residue 100 type sequence A description binding site for residue GTP C 502 source : AD1 11) chain C residue 101 type sequence N description binding site for residue GTP C 502 source : AD1 12) chain C residue 140 type sequence S description binding site for residue GTP C 502 source : AD1 13) chain C residue 143 type sequence G description binding site for residue GTP C 502 source : AD1 14) chain C residue 144 type sequence G description binding site for residue GTP C 502 source : AD1 15) chain C residue 145 type sequence T description binding site for residue GTP C 502 source : AD1 16) chain C residue 146 type sequence G description binding site for residue GTP C 502 source : AD1 17) chain C residue 171 type sequence I description binding site for residue GTP C 502 source : AD1 18) chain C residue 179 type sequence T description binding site for residue GTP C 502 source : AD1 19) chain C residue 183 type sequence E description binding site for residue GTP C 502 source : AD1 20) chain C residue 206 type sequence N description binding site for residue GTP C 502 source : AD1 21) chain C residue 224 type sequence Y description binding site for residue GTP C 502 source : AD1 22) chain C residue 228 type sequence N description binding site for residue GTP C 502 source : AD1 23) chain C residue 39 type sequence D description binding site for residue CA C 503 source : AD2 24) chain C residue 41 type sequence T description binding site for residue CA C 503 source : AD2 25) chain C residue 44 type sequence G description binding site for residue CA C 503 source : AD2 26) chain C residue 55 type sequence E description binding site for residue CA C 503 source : AD2 27) chain C residue 262 type sequence Y description binding site for residue IMD C 504 source : AD3 28) chain C residue 431 type sequence D description binding site for residue IMD C 504 source : AD3 29) chain C residue 434 type sequence E description binding site for residue IMD C 504 source : AD3 30) chain C residue 180 type sequence A description binding site for residue 4EE D 503 source : AD6 31) chain C residue 181 type sequence V description binding site for residue 4EE D 503 source : AD6 32) chain C residue 326 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI12 33) chain C residue 370 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI12 34) chain C residue 71 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 35) chain C residue 140 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 36) chain C residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 37) chain C residue 145 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 38) chain C residue 179 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 39) chain C residue 206 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 40) chain C residue 228 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 41) chain C residue 11 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 42) chain C residue 48 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI5 43) chain C residue 232 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI5

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