eF-site ID 3jar-B PDB Code 3jar Chain B 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 B:  MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDS DLQLERINVYYNEAAGNKYVPRAILVDLEPGTMDSVRSGP FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP DRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETY CIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQ YRALTVPELTQQMFDAKNMMAACDPRHGRYLTVAAVFRGR MSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG LKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG EGMDEMEFTEAESNMNDLVSEYQQYQDAT Description Functional site 1) chain B residue 11 type sequence Q description BINDING SITE FOR RESIDUE GDP B 501 source : BC6 2) chain B residue 12 type sequence C description BINDING SITE FOR RESIDUE GDP B 501 source : BC6 3) chain B residue 15 type sequence Q description BINDING SITE FOR RESIDUE GDP B 501 source : BC6 4) chain B residue 140 type sequence S description BINDING SITE FOR RESIDUE GDP B 501 source : BC6 5) chain B residue 143 type sequence G description BINDING SITE FOR RESIDUE GDP B 501 source : BC6 6) chain B residue 144 type sequence G description BINDING SITE FOR RESIDUE GDP B 501 source : BC6 7) chain B residue 145 type sequence T description BINDING SITE FOR RESIDUE GDP B 501 source : BC6 8) chain B residue 146 type sequence G description BINDING SITE FOR RESIDUE GDP B 501 source : BC6 9) chain B residue 179 type sequence D description BINDING SITE FOR RESIDUE GDP B 501 source : BC6 10) chain B residue 206 type sequence N description BINDING SITE FOR RESIDUE GDP B 501 source : BC6 11) chain B residue 224 type sequence Y description BINDING SITE FOR RESIDUE GDP B 501 source : BC6 12) chain B residue 228 type sequence N description BINDING SITE FOR RESIDUE GDP B 501 source : BC6 13) chain B residue 248 type sequence L description BINDING SITE FOR RESIDUE GTP K 501 source : BC7 14) chain B residue 254 type sequence K description BINDING SITE FOR RESIDUE GTP K 501 source : BC7 15) chain B residue 11 type MOD_RES sequence Q description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 16) chain B residue 140 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 17) chain B residue 144 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 18) chain B residue 145 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 19) chain B residue 146 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 20) chain B residue 206 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 21) chain B residue 228 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 22) chain B residue 71 type MOD_RES sequence E description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 23) chain B residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 24) chain B residue 60 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI4 25) chain B residue 174 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885 source Swiss-Prot : SWS_FT_FI5 26) chain B residue 292 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 27) chain B residue 287 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 28) chain B residue 320 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 29) chain B 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 B 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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