eF-site ID 3jat-H PDB Code 3jat Chain H 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 H:  MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDS DLQLERINVYYNEAAGNKYVPRAILVDLEPGTMDSVRSGP FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP DRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETY CIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQ YRALTVPELTQQMFDAKNMMAACDPRHGRYLTVAAVFRGR MSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG LKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG EGMDEMEFTEAESNMNDLVSEYQQYQ Description Functional site 1) chain H residue 254 type sequence K description BINDING SITE FOR RESIDUE GTP A 501 source : BC8 2) chain H residue 10 type sequence G description BINDING SITE FOR RESIDUE G2P H 501 source : CC5 3) chain H residue 11 type sequence Q description BINDING SITE FOR RESIDUE G2P H 501 source : CC5 4) chain H residue 12 type sequence C description BINDING SITE FOR RESIDUE G2P H 501 source : CC5 5) chain H residue 15 type sequence Q description BINDING SITE FOR RESIDUE G2P H 501 source : CC5 6) chain H residue 99 type sequence A description BINDING SITE FOR RESIDUE G2P H 501 source : CC5 7) chain H residue 101 type sequence N description BINDING SITE FOR RESIDUE G2P H 501 source : CC5 8) chain H residue 144 type sequence G description BINDING SITE FOR RESIDUE G2P H 501 source : CC5 9) chain H residue 145 type sequence T description BINDING SITE FOR RESIDUE G2P H 501 source : CC5 10) chain H residue 146 type sequence G description BINDING SITE FOR RESIDUE G2P H 501 source : CC5 11) chain H residue 183 type sequence E description BINDING SITE FOR RESIDUE G2P H 501 source : CC5 12) chain H residue 206 type sequence N description BINDING SITE FOR RESIDUE G2P H 501 source : CC5 13) chain H residue 224 type sequence Y description BINDING SITE FOR RESIDUE G2P H 501 source : CC5 14) chain H residue 228 type sequence N description BINDING SITE FOR RESIDUE G2P H 501 source : CC5 15) chain H 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 16) chain H 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 17) chain H residue 11 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 18) chain H residue 140 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 19) chain H residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 20) chain H residue 145 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 21) chain H residue 146 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 22) chain H residue 206 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 23) chain H residue 228 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 24) chain H residue 71 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 25) chain H residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 26) chain H residue 60 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI4 27) chain H residue 174 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885 source Swiss-Prot : SWS_FT_FI5 28) chain H residue 287 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 29) chain H residue 292 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 30) chain H residue 320 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7

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