eF-site ID 5xlz-B PDB Code 5xlz Chain B click to enlarge Title The crystal structure of tubulin complexed with a benzylidene derivative of 9(10H)-anthracenone Classification CELL CYCLE Compound Tubulin alpha-1B chain Source ORGANISM_COMMON: Bovine; ORGANISM_SCIENTIFIC: Bos taurus; Sequence B:  REIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSD LQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGPF GQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVR KESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPD RIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYC IDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLR FPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQY RALTVPELTQQMFDSKNMMAACDPRHGRYLTVAAIFRGRM SMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGL KMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGE GMDEMEFTEAESNMNDLVSEYQQYQDA Description Functional site 1) chain B residue 252 type sequence K description binding site for residue GTP A 501 source : AC1 2) chain B residue 10 type sequence G description binding site for residue GDP B 501 source : AC4 3) chain B residue 11 type sequence Q description binding site for residue GDP B 501 source : AC4 4) chain B residue 12 type sequence C description binding site for residue GDP B 501 source : AC4 5) chain B residue 15 type sequence Q description binding site for residue GDP B 501 source : AC4 6) chain B residue 138 type sequence S description binding site for residue GDP B 501 source : AC4 7) chain B residue 141 type sequence G description binding site for residue GDP B 501 source : AC4 8) chain B residue 142 type sequence G description binding site for residue GDP B 501 source : AC4 9) chain B residue 143 type sequence T description binding site for residue GDP B 501 source : AC4 10) chain B residue 144 type sequence G description binding site for residue GDP B 501 source : AC4 11) chain B residue 171 type sequence P description binding site for residue GDP B 501 source : AC4 12) chain B residue 175 type sequence V description binding site for residue GDP B 501 source : AC4 13) chain B residue 177 type sequence D description binding site for residue GDP B 501 source : AC4 14) chain B residue 181 type sequence E description binding site for residue GDP B 501 source : AC4 15) chain B residue 204 type sequence N description binding site for residue GDP B 501 source : AC4 16) chain B residue 222 type sequence Y description binding site for residue GDP B 501 source : AC4 17) chain B residue 226 type sequence N description binding site for residue GDP B 501 source : AC4 18) chain B residue 11 type sequence Q description binding site for residue MG B 502 source : AC5 19) chain B residue 156 type sequence R description binding site for residue MES B 503 source : AC6 20) chain B residue 160 type sequence P description binding site for residue MES B 503 source : AC6 21) chain B residue 161 type sequence D description binding site for residue MES B 503 source : AC6 22) chain B residue 162 type sequence R description binding site for residue MES B 503 source : AC6 23) chain B residue 195 type sequence N description binding site for residue MES B 503 source : AC6 24) chain B residue 196 type sequence T description binding site for residue MES B 503 source : AC6 25) chain B residue 197 type sequence D description binding site for residue MES B 503 source : AC6 26) chain B residue 251 type sequence R description binding site for residue MES B 503 source : AC6 27) chain B residue 239 type sequence C description binding site for residue 89U B 504 source : AC7 28) chain B residue 240 type sequence L description binding site for residue 89U B 504 source : AC7 29) chain B residue 246 type sequence L description binding site for residue 89U B 504 source : AC7 30) chain B residue 249 type sequence D description binding site for residue 89U B 504 source : AC7 31) chain B residue 256 type sequence N description binding site for residue 89U B 504 source : AC7 32) chain B residue 257 type sequence M description binding site for residue 89U B 504 source : AC7 33) chain B residue 313 type sequence V description binding site for residue 89U B 504 source : AC7 34) chain B residue 315 type sequence A description binding site for residue 89U B 504 source : AC7 35) chain B residue 348 type sequence N description binding site for residue 89U B 504 source : AC7 36) chain B residue 350 type sequence K description binding site for residue 89U B 504 source : AC7 37) chain B residue 294 type sequence F description binding site for residue MES B 505 source : AC8 38) chain B residue 295 type sequence D description binding site for residue MES B 505 source : AC8 39) chain B residue 296 type sequence S description binding site for residue MES B 505 source : AC8 40) chain B residue 304 type sequence D description binding site for residue MES B 505 source : AC8 41) chain B residue 305 type sequence P description binding site for residue MES B 505 source : AC8 42) chain B residue 306 type sequence R description binding site for residue MES B 505 source : AC8 43) chain B residue 333 type sequence V description binding site for residue MES B 505 source : AC8 44) chain B residue 337 type sequence N description binding site for residue MES B 505 source : AC8 45) chain B residue 58 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 46) chain B residue 324 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI11 47) chain B residue 140-146 type prosite sequence GGGTGSG description TUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG source prosite : PS00227 48) chain B residue 142 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 49) chain B residue 143 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 50) chain B residue 144 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 51) chain B residue 204 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 52) chain B residue 226 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 53) chain B residue 138 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 54) chain B residue 69 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 55) chain B residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 56) chain B residue 55 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q3KRE8 source Swiss-Prot : SWS_FT_FI4 57) chain B residue 58 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI5 58) chain B residue 172 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q9BVA1 source Swiss-Prot : SWS_FT_FI6 59) chain B residue 285 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 60) chain B residue 290 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 61) chain B residue 318 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI8

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