eF-site ID 3jar-D PDB Code 3jar Chain D 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 D:  MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDS DLQLERINVYYNEAAGNKYVPRAILVDLEPGTMDSVRSGP FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP DRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETY CIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQ YRALTVPELTQQMFDAKNMMAACDPRHGRYLTVAAVFRGR MSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG LKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG EGMDEMEFTEAESNMNDLVSEYQQYQDAT Description Functional site 1) chain D residue 11 type sequence Q description BINDING SITE FOR RESIDUE GDP D 501 source : AC9 2) chain D residue 12 type sequence C description BINDING SITE FOR RESIDUE GDP D 501 source : AC9 3) chain D residue 15 type sequence Q description BINDING SITE FOR RESIDUE GDP D 501 source : AC9 4) chain D residue 140 type sequence S description BINDING SITE FOR RESIDUE GDP D 501 source : AC9 5) chain D residue 143 type sequence G description BINDING SITE FOR RESIDUE GDP D 501 source : AC9 6) chain D residue 144 type sequence G description BINDING SITE FOR RESIDUE GDP D 501 source : AC9 7) chain D residue 145 type sequence T description BINDING SITE FOR RESIDUE GDP D 501 source : AC9 8) chain D residue 146 type sequence G description BINDING SITE FOR RESIDUE GDP D 501 source : AC9 9) chain D residue 179 type sequence D description BINDING SITE FOR RESIDUE GDP D 501 source : AC9 10) chain D residue 206 type sequence N description BINDING SITE FOR RESIDUE GDP D 501 source : AC9 11) chain D residue 224 type sequence Y description BINDING SITE FOR RESIDUE GDP D 501 source : AC9 12) chain D residue 228 type sequence N description BINDING SITE FOR RESIDUE GDP D 501 source : AC9 13) chain D residue 248 type sequence L description BINDING SITE FOR RESIDUE GTP L 501 source : BC1 14) chain D residue 254 type sequence K description BINDING SITE FOR RESIDUE GTP L 501 source : BC1 15) chain D residue 11 type MOD_RES sequence Q description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 16) chain D residue 140 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 17) chain D residue 144 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 18) chain D residue 145 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 19) chain D residue 146 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 20) chain D residue 206 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 21) chain D residue 228 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 22) chain D residue 71 type MOD_RES sequence E description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 23) chain D residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 24) chain D residue 60 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI4 25) chain D residue 174 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885 source Swiss-Prot : SWS_FT_FI5 26) chain D residue 287 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 27) chain D residue 292 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 28) chain D residue 320 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 29) chain D 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 D 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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