eF-site ID 3jat-G PDB Code 3jat Chain G 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 G:  MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDS DLQLERINVYYNEAAGNKYVPRAILVDLEPGTMDSVRSGP FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP DRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETY CIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQ YRALTVPELTQQMFDAKNMMAACDPRHGRYLTVAAVFRGR MSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG LKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG EGMDEMEFTEAESNMNDLVSEYQQYQ Description Functional site 1) chain G residue 254 type sequence K description BINDING SITE FOR RESIDUE GTP E 501 source : AC1 2) chain G residue 10 type sequence G description BINDING SITE FOR RESIDUE G2P G 501 source : AC7 3) chain G residue 11 type sequence Q description BINDING SITE FOR RESIDUE G2P G 501 source : AC7 4) chain G residue 12 type sequence C description BINDING SITE FOR RESIDUE G2P G 501 source : AC7 5) chain G residue 15 type sequence Q description BINDING SITE FOR RESIDUE G2P G 501 source : AC7 6) chain G residue 99 type sequence A description BINDING SITE FOR RESIDUE G2P G 501 source : AC7 7) chain G residue 101 type sequence N description BINDING SITE FOR RESIDUE G2P G 501 source : AC7 8) chain G residue 144 type sequence G description BINDING SITE FOR RESIDUE G2P G 501 source : AC7 9) chain G residue 145 type sequence T description BINDING SITE FOR RESIDUE G2P G 501 source : AC7 10) chain G residue 146 type sequence G description BINDING SITE FOR RESIDUE G2P G 501 source : AC7 11) chain G residue 183 type sequence E description BINDING SITE FOR RESIDUE G2P G 501 source : AC7 12) chain G residue 206 type sequence N description BINDING SITE FOR RESIDUE G2P G 501 source : AC7 13) chain G residue 224 type sequence Y description BINDING SITE FOR RESIDUE G2P G 501 source : AC7 14) chain G residue 228 type sequence N description BINDING SITE FOR RESIDUE G2P G 501 source : AC7 15) chain G residue 287 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 16) chain G residue 292 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 17) chain G residue 320 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 18) chain G 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 19) chain G 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 20) chain G residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 21) chain G residue 145 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 22) chain G residue 146 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 23) chain G residue 206 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 24) chain G residue 228 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 25) chain G residue 11 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 26) chain G residue 140 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 27) chain G residue 71 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 28) chain G residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 29) chain G residue 60 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI4 30) chain G 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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