eF-site ID 5xag-C PDB Code 5xag Chain C click to enlarge Title Crystal structure of tubulin-stathmin-TTL-Compound Z2 complex Classification STRUCTURAL PROTEIN Compound Tubulin alpha-1B chain Source Bos taurus (Bovine) (E1BQ43_CHICK) Sequence C:  MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDK TIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT GTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD RIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVD YGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDC AFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEK AYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR GDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPP TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYA KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSV Description Functional site 1) chain C residue 253 type sequence T description binding site for residue GOL C 501 source : AD6 2) chain C residue 257 type sequence T description binding site for residue GOL C 501 source : AD6 3) chain C residue 10 type sequence G description binding site for residue GTP C 502 source : AD7 4) chain C residue 11 type sequence Q description binding site for residue GTP C 502 source : AD7 5) chain C residue 12 type sequence A description binding site for residue GTP C 502 source : AD7 6) chain C residue 15 type sequence Q description binding site for residue GTP C 502 source : AD7 7) chain C residue 98 type sequence D description binding site for residue GTP C 502 source : AD7 8) chain C residue 99 type sequence A description binding site for residue GTP C 502 source : AD7 9) chain C residue 101 type sequence N description binding site for residue GTP C 502 source : AD7 10) chain C residue 140 type sequence S description binding site for residue GTP C 502 source : AD7 11) chain C residue 143 type sequence G description binding site for residue GTP C 502 source : AD7 12) chain C residue 144 type sequence G description binding site for residue GTP C 502 source : AD7 13) chain C residue 145 type sequence T description binding site for residue GTP C 502 source : AD7 14) chain C residue 146 type sequence G description binding site for residue GTP C 502 source : AD7 15) chain C residue 177 type sequence V description binding site for residue GTP C 502 source : AD7 16) chain C residue 179 type sequence T description binding site for residue GTP C 502 source : AD7 17) chain C residue 183 type sequence E description binding site for residue GTP C 502 source : AD7 18) chain C residue 206 type sequence N description binding site for residue GTP C 502 source : AD7 19) chain C residue 224 type sequence Y description binding site for residue GTP C 502 source : AD7 20) chain C residue 228 type sequence N description binding site for residue GTP C 502 source : AD7 21) chain C residue 231 type sequence I description binding site for residue GTP C 502 source : AD7 22) chain C residue 71 type sequence E description binding site for residue MG C 503 source : AD8 23) chain C residue 221 type sequence R description binding site for residue GOL C 504 source : AD9 24) chain C residue 222 type sequence P description binding site for residue GOL C 504 source : AD9 25) chain C residue 223 type sequence T description binding site for residue GOL C 504 source : AD9 26) chain C residue 224 type sequence Y description binding site for residue GOL C 504 source : AD9 27) chain C residue 288 type sequence V description binding site for residue GOL C 505 source : AE1 28) chain C residue 322 type sequence D description binding site for residue GOL C 505 source : AE1 29) chain C residue 327 type sequence D description binding site for residue GOL C 505 source : AE1 30) chain C residue 373 type sequence R description binding site for residue GOL C 505 source : AE1 31) chain C residue 163 type sequence K description binding site for residue GOL C 506 source : AE2 32) chain C residue 164 type sequence K description binding site for residue GOL C 506 source : AE2 33) chain C residue 166 type sequence K description binding site for residue GOL C 506 source : AE2 34) chain C residue 196 type sequence E description binding site for residue GOL C 506 source : AE2 35) chain C residue 197 type sequence H description binding site for residue GOL C 506 source : AE2 36) chain C residue 199 type sequence D description binding site for residue GOL C 506 source : AE2 37) chain C residue 282 type sequence Y description binding site for residue CA C 507 source : AE3 38) chain C residue 262 type sequence Y description binding site for residue IMD C 508 source : AE4 39) chain C residue 431 type sequence D description binding site for residue IMD C 508 source : AE4 40) chain C residue 4 type sequence C description binding site for residue IMD C 509 source : AE5 41) chain C residue 133 type sequence Q description binding site for residue IMD C 509 source : AE5 42) chain C residue 165 type sequence S description binding site for residue IMD C 509 source : AE5 43) chain C residue 242 type sequence L description binding site for residue IMD C 509 source : AE5 44) chain C residue 253 type sequence T description binding site for residue IMD C 509 source : AE5 45) chain C residue 179 type sequence T description binding site for residue 93X D 505 source : AE9 46) chain C residue 180 type sequence A description binding site for residue 93X D 505 source : AE9 47) chain C residue 181 type sequence V description binding site for residue 93X D 505 source : AE9 48) chain C residue 407 type sequence W description binding site for residues GOL D 504 and IMD E 201 source : AF3 49) chain C residue 410 type sequence G description binding site for residues GOL D 504 and IMD E 201 source : AF3 50) chain C residue 411 type sequence E description binding site for residues GOL D 504 and IMD E 201 source : AF3 51) 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 52) 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 53) chain C residue 71 type LIPID sequence E description S-palmitoyl cysteine => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 54) chain C residue 140 type LIPID sequence S description S-palmitoyl cysteine => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 55) chain C residue 144 type LIPID sequence G description S-palmitoyl cysteine => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 56) chain C residue 145 type LIPID sequence T description S-palmitoyl cysteine => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 57) chain C residue 179 type LIPID sequence T description S-palmitoyl cysteine => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 58) chain C residue 206 type LIPID sequence N description S-palmitoyl cysteine => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 59) chain C residue 228 type LIPID sequence N description S-palmitoyl cysteine => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 60) chain C residue 11 type LIPID sequence Q description S-palmitoyl cysteine => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 61) chain C residue 48 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI5 62) 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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