eF-site ID 3jat-F PDB Code 3jat Chain F click to enlarge Title Cryo-EM structure of GMPCPP-microtubule (14 protofilaments) decorated with kinesin Classification STRUCTURAL PROTEIN Compound Tubulin alpha-1B chain Source ORGANISM_COMMON: pig; ORGANISM_SCIENTIFIC: Sus scrofa; Sequence F:  MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDS DLQLERINVYYNEAAGNKYVPRAILVDLEPGTMDSVRSGP FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP DRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETY CIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQ YRALTVPELTQQMFDAKNMMAACDPRHGRYLTVAAVFRGR MSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG LKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG EGMDEMEFTEAESNMNDLVSEYQQYQ Description Functional site 1) chain F residue 10 type sequence G description BINDING SITE FOR RESIDUE G2P F 501 source : AC3 2) chain F residue 11 type sequence Q description BINDING SITE FOR RESIDUE G2P F 501 source : AC3 3) chain F residue 12 type sequence C description BINDING SITE FOR RESIDUE G2P F 501 source : AC3 4) chain F residue 15 type sequence Q description BINDING SITE FOR RESIDUE G2P F 501 source : AC3 5) chain F residue 99 type sequence A description BINDING SITE FOR RESIDUE G2P F 501 source : AC3 6) chain F residue 101 type sequence N description BINDING SITE FOR RESIDUE G2P F 501 source : AC3 7) chain F residue 144 type sequence G description BINDING SITE FOR RESIDUE G2P F 501 source : AC3 8) chain F residue 145 type sequence T description BINDING SITE FOR RESIDUE G2P F 501 source : AC3 9) chain F residue 146 type sequence G description BINDING SITE FOR RESIDUE G2P F 501 source : AC3 10) chain F residue 206 type sequence N description BINDING SITE FOR RESIDUE G2P F 501 source : AC3 11) chain F residue 224 type sequence Y description BINDING SITE FOR RESIDUE G2P F 501 source : AC3 12) chain F residue 228 type sequence N description BINDING SITE FOR RESIDUE G2P F 501 source : AC3 13) chain F residue 254 type sequence K description BINDING SITE FOR RESIDUE GTP J 501 source : AC5 14) chain F residue 287 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 15) chain F residue 292 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 16) chain F residue 320 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 17) chain F 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_FI9 18) chain F 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_FI10 19) chain F residue 142-148 type prosite sequence GGGTGSG description TUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG source prosite : PS00227 20) chain F residue 1-4 type prosite sequence MREI description TUBULIN_B_AUTOREG Tubulin-beta mRNA autoregulation signal. MREI source prosite : PS00228 21) chain F residue 11 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 22) chain F residue 140 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 23) chain F residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 24) chain F residue 145 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 25) chain F residue 146 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 26) chain F residue 206 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 27) chain F residue 228 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 28) chain F residue 71 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 29) chain F residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 30) chain F residue 60 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI4 31) chain F residue 174 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885 source Swiss-Prot : SWS_FT_FI5

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