eF-site ID 3du7-B PDB Code 3du7 Chain B click to enlarge Title Tubulin-colchicine-phomopsin A: Stathmin-like domain complex Classification CELL CYCLE Compound Tubulin alpha-1C chain Source ORGANISM_COMMON: bovine; ORGANISM_SCIENTIFIC: Bos taurus; Sequence B:  REIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSD LQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGPF GQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVR KESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPD RIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYS IDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLR FPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQY RALTVPELTQQMFDSKNMMAACDPRHGRYLTVAAVFRGRM SMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGL KMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGE GMDEMEFTEAESNMNDLVSEYQQYQD Description Functional site 1) chain B residue 11 type sequence Q description BINDING SITE FOR RESIDUE GDP D 602 source : AC5 2) chain B residue 12 type sequence C description BINDING SITE FOR RESIDUE GDP D 602 source : AC5 3) chain B residue 140 type sequence S description BINDING SITE FOR RESIDUE GDP D 602 source : AC5 4) chain B residue 142 type sequence G description BINDING SITE FOR RESIDUE GDP D 602 source : AC5 5) chain B residue 144 type sequence G description BINDING SITE FOR RESIDUE GDP D 602 source : AC5 6) chain B residue 145 type sequence T description BINDING SITE FOR RESIDUE GDP D 602 source : AC5 7) chain B residue 173 type sequence P description BINDING SITE FOR RESIDUE GDP D 602 source : AC5 8) chain B residue 178 type sequence S description BINDING SITE FOR RESIDUE GDP D 602 source : AC5 9) chain B residue 183 type sequence E description BINDING SITE FOR RESIDUE GDP D 602 source : AC5 10) chain B residue 206 type sequence N description BINDING SITE FOR RESIDUE GDP D 602 source : AC5 11) chain B residue 224 type sequence Y description BINDING SITE FOR RESIDUE GDP D 602 source : AC5 12) chain B residue 228 type sequence N description BINDING SITE FOR RESIDUE GDP D 602 source : AC5 13) chain B residue 241 type sequence C description BINDING SITE FOR RESIDUE CN2 B 700 source : AC7 14) chain B residue 242 type sequence L description BINDING SITE FOR RESIDUE CN2 B 700 source : AC7 15) chain B residue 250 type sequence A description BINDING SITE FOR RESIDUE CN2 B 700 source : AC7 16) chain B residue 254 type sequence K description BINDING SITE FOR RESIDUE CN2 B 700 source : AC7 17) chain B residue 255 type sequence L description BINDING SITE FOR RESIDUE CN2 B 700 source : AC7 18) chain B residue 258 type sequence N description BINDING SITE FOR RESIDUE CN2 B 700 source : AC7 19) chain B residue 259 type sequence M description BINDING SITE FOR RESIDUE CN2 B 700 source : AC7 20) chain B residue 316 type sequence A description BINDING SITE FOR RESIDUE CN2 B 700 source : AC7 21) chain B residue 352 type sequence K description BINDING SITE FOR RESIDUE CN2 B 700 source : AC7 22) chain B residue 178 type sequence S description BINDING SITE FOR RESIDUE HOS B 800 source : AC9 23) chain B residue 221 type sequence T description BINDING SITE FOR RESIDUE HOS B 800 source : AC9 24) chain B residue 222 type sequence P description BINDING SITE FOR RESIDUE HOS B 800 source : AC9 25) chain B residue 223 type sequence T description BINDING SITE FOR RESIDUE HOS B 800 source : AC9 26) chain B residue 224 type sequence Y description BINDING SITE FOR RESIDUE HOS B 800 source : AC9 27) chain B residue 60 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 28) chain B residue 326 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 29) chain B residue 71 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 30) chain B residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 31) chain B residue 57 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q3KRE8 source Swiss-Prot : SWS_FT_FI4 32) chain B residue 60 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI5 33) chain B residue 174 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q9BVA1 source Swiss-Prot : SWS_FT_FI6 34) chain B residue 287 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 35) chain B residue 292 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 36) chain B residue 320 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI8 37) chain B residue 142-148 type prosite sequence GGGTGSG description TUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG source prosite : PS00227 38) chain B residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 39) chain B residue 145 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 40) chain B residue 146 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 41) chain B residue 206 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 42) chain B residue 228 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 43) chain B residue 140 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 44) chain B residue 11 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1

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