eF-site ID 4o4i-C PDB Code 4o4i Chain C click to enlarge Title Tubulin-Laulimalide-Epothilone A complex Classification CELL CYCLE/INHIBITOR Compound Tubulin alpha-1B chain Source ORGANISM_COMMON: bovine,cow,domestic cattle,domestic cow; ORGANISM_SCIENTIFIC: Bos taurus; 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 : BC2 2) chain C residue 11 type sequence Q description BINDING SITE FOR RESIDUE GTP C 501 source : BC2 3) chain C residue 12 type sequence A description BINDING SITE FOR RESIDUE GTP C 501 source : BC2 4) chain C residue 15 type sequence Q description BINDING SITE FOR RESIDUE GTP C 501 source : BC2 5) chain C residue 98 type sequence D description BINDING SITE FOR RESIDUE GTP C 501 source : BC2 6) chain C residue 99 type sequence A description BINDING SITE FOR RESIDUE GTP C 501 source : BC2 7) chain C residue 100 type sequence A description BINDING SITE FOR RESIDUE GTP C 501 source : BC2 8) chain C residue 101 type sequence N description BINDING SITE FOR RESIDUE GTP C 501 source : BC2 9) chain C residue 140 type sequence S description BINDING SITE FOR RESIDUE GTP C 501 source : BC2 10) chain C residue 143 type sequence G description BINDING SITE FOR RESIDUE GTP C 501 source : BC2 11) chain C residue 144 type sequence G description BINDING SITE FOR RESIDUE GTP C 501 source : BC2 12) chain C residue 145 type sequence T description BINDING SITE FOR RESIDUE GTP C 501 source : BC2 13) chain C residue 146 type sequence G description BINDING SITE FOR RESIDUE GTP C 501 source : BC2 14) chain C residue 177 type sequence V description BINDING SITE FOR RESIDUE GTP C 501 source : BC2 15) chain C residue 183 type sequence E description BINDING SITE FOR RESIDUE GTP C 501 source : BC2 16) chain C residue 206 type sequence N description BINDING SITE FOR RESIDUE GTP C 501 source : BC2 17) chain C residue 224 type sequence Y description BINDING SITE FOR RESIDUE GTP C 501 source : BC2 18) chain C residue 228 type sequence N description BINDING SITE FOR RESIDUE GTP C 501 source : BC2 19) chain C residue 231 type sequence I description BINDING SITE FOR RESIDUE GTP C 501 source : BC2 20) chain C residue 39 type sequence D description BINDING SITE FOR RESIDUE CA C 503 source : BC4 21) chain C residue 41 type sequence T description BINDING SITE FOR RESIDUE CA C 503 source : BC4 22) chain C residue 44 type sequence G description BINDING SITE FOR RESIDUE CA C 503 source : BC4 23) chain C residue 45 type sequence G description BINDING SITE FOR RESIDUE CA C 503 source : BC4 24) chain C residue 55 type sequence E description BINDING SITE FOR RESIDUE CA C 503 source : BC4 25) 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 26) 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 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 N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI5 36) 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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