eF-site ID 4yj3-A PDB Code 4yj3 Chain A 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 A:  MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDK TIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT GTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD RIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVD YGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDC AFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEK AYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR GDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPP TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYA KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVD Description Functional site 1) chain A residue 71 type sequence E description binding site for residue MG A 501 source : AC1 2) chain A residue 10 type sequence G description binding site for residue GTP A 502 source : AC2 3) chain A residue 11 type sequence Q description binding site for residue GTP A 502 source : AC2 4) chain A residue 12 type sequence A description binding site for residue GTP A 502 source : AC2 5) chain A residue 15 type sequence Q description binding site for residue GTP A 502 source : AC2 6) chain A residue 98 type sequence D description binding site for residue GTP A 502 source : AC2 7) chain A residue 99 type sequence A description binding site for residue GTP A 502 source : AC2 8) chain A residue 100 type sequence A description binding site for residue GTP A 502 source : AC2 9) chain A residue 101 type sequence N description binding site for residue GTP A 502 source : AC2 10) chain A residue 140 type sequence S description binding site for residue GTP A 502 source : AC2 11) chain A residue 143 type sequence G description binding site for residue GTP A 502 source : AC2 12) chain A residue 144 type sequence G description binding site for residue GTP A 502 source : AC2 13) chain A residue 145 type sequence T description binding site for residue GTP A 502 source : AC2 14) chain A residue 177 type sequence V description binding site for residue GTP A 502 source : AC2 15) chain A residue 178 type sequence S description binding site for residue GTP A 502 source : AC2 16) chain A residue 179 type sequence T description binding site for residue GTP A 502 source : AC2 17) chain A residue 183 type sequence E description binding site for residue GTP A 502 source : AC2 18) chain A residue 206 type sequence N description binding site for residue GTP A 502 source : AC2 19) chain A residue 224 type sequence Y description binding site for residue GTP A 502 source : AC2 20) chain A residue 228 type sequence N description binding site for residue GTP A 502 source : AC2 21) chain A residue 231 type sequence I description binding site for residue GTP A 502 source : AC2 22) chain A residue 39 type sequence D description binding site for residue CA A 503 source : AC3 23) chain A residue 41 type sequence T description binding site for residue CA A 503 source : AC3 24) chain A residue 44 type sequence G description binding site for residue CA A 503 source : AC3 25) chain A residue 45 type sequence G description binding site for residue CA A 503 source : AC3 26) chain A residue 55 type sequence E description binding site for residue CA A 503 source : AC3 27) chain A residue 179 type sequence T description binding site for residue 4EE B 503 source : AC6 28) chain A residue 181 type sequence V description binding site for residue 4EE B 503 source : AC6 29) chain A residue 407 type sequence W description binding site for residue MES B 505 source : AC8 30) chain A 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 31) chain A 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 32) chain A residue 140 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 33) chain A residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 34) chain A residue 145 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 35) chain A residue 179 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 36) chain A residue 206 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 37) chain A residue 228 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 38) chain A residue 142-148 type prosite sequence GGGTGSG description TUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG source prosite : PS00227

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