eF-site ID 3jar-I PDB Code 3jar Chain I click to enlarge Title Cryo-EM structure of GDP-microtubule co-polymerized with EB3 Classification STRUCTURAL PROTEIN Compound Tubulin alpha-1B chain Source ORGANISM_COMMON: pig; ORGANISM_SCIENTIFIC: Sus scrofa; Sequence I:  MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDS DLQLERINVYYNEAAGNKYVPRAILVDLEPGTMDSVRSGP FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP DRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETY CIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQ YRALTVPELTQQMFDAKNMMAACDPRHGRYLTVAAVFRGR MSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG LKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG EGMDEMEFTEAESNMNDLVSEYQQYQDAT Description Functional site 1) chain I residue 248 type sequence L description BINDING SITE FOR RESIDUE GTP C 501 source : AC7 2) chain I residue 254 type sequence K description BINDING SITE FOR RESIDUE GTP C 501 source : AC7 3) chain I residue 11 type sequence Q description BINDING SITE FOR RESIDUE GDP I 501 source : BC3 4) chain I residue 12 type sequence C description BINDING SITE FOR RESIDUE GDP I 501 source : BC3 5) chain I residue 15 type sequence Q description BINDING SITE FOR RESIDUE GDP I 501 source : BC3 6) chain I residue 140 type sequence S description BINDING SITE FOR RESIDUE GDP I 501 source : BC3 7) chain I residue 143 type sequence G description BINDING SITE FOR RESIDUE GDP I 501 source : BC3 8) chain I residue 144 type sequence G description BINDING SITE FOR RESIDUE GDP I 501 source : BC3 9) chain I residue 145 type sequence T description BINDING SITE FOR RESIDUE GDP I 501 source : BC3 10) chain I residue 146 type sequence G description BINDING SITE FOR RESIDUE GDP I 501 source : BC3 11) chain I residue 179 type sequence D description BINDING SITE FOR RESIDUE GDP I 501 source : BC3 12) chain I residue 206 type sequence N description BINDING SITE FOR RESIDUE GDP I 501 source : BC3 13) chain I residue 224 type sequence Y description BINDING SITE FOR RESIDUE GDP I 501 source : BC3 14) chain I residue 228 type sequence N description BINDING SITE FOR RESIDUE GDP I 501 source : BC3 15) chain I residue 11 type MOD_RES sequence Q description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 16) chain I residue 140 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 17) chain I residue 144 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 18) chain I residue 145 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 19) chain I residue 146 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 20) chain I residue 206 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 21) chain I residue 228 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 22) chain I residue 71 type MOD_RES sequence E description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 23) chain I residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 24) chain I residue 60 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI4 25) chain I residue 174 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885 source Swiss-Prot : SWS_FT_FI5 26) chain I residue 287 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 27) chain I residue 292 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 28) chain I residue 320 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 29) chain I 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 30) chain I 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

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