eF-site ID 3jar-C PDB Code 3jar Chain C 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 C:  MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPDSF NTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHP EQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQC TGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEF SIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAI YDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALN VDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVA EITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVN AAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLA KVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYV GEGMEEGEFSEAREDMAALEKDYEEVGVDSVE Description Functional site 1) chain C residue 11 type sequence Q description BINDING SITE FOR RESIDUE GTP C 501 source : AC7 2) chain C residue 12 type sequence A description BINDING SITE FOR RESIDUE GTP C 501 source : AC7 3) chain C residue 15 type sequence Q description BINDING SITE FOR RESIDUE GTP C 501 source : AC7 4) chain C residue 99 type sequence A description BINDING SITE FOR RESIDUE GTP C 501 source : AC7 5) chain C residue 100 type sequence A description BINDING SITE FOR RESIDUE GTP C 501 source : AC7 6) chain C residue 101 type sequence N description BINDING SITE FOR RESIDUE GTP C 501 source : AC7 7) chain C residue 140 type sequence S description BINDING SITE FOR RESIDUE GTP C 501 source : AC7 8) chain C residue 143 type sequence G description BINDING SITE FOR RESIDUE GTP C 501 source : AC7 9) chain C residue 144 type sequence G description BINDING SITE FOR RESIDUE GTP C 501 source : AC7 10) chain C residue 145 type sequence T description BINDING SITE FOR RESIDUE GTP C 501 source : AC7 11) chain C residue 146 type sequence G description BINDING SITE FOR RESIDUE GTP C 501 source : AC7 12) chain C residue 171 type sequence I description BINDING SITE FOR RESIDUE GTP C 501 source : AC7 13) chain C residue 179 type sequence T description BINDING SITE FOR RESIDUE GTP C 501 source : AC7 14) chain C residue 183 type sequence E description BINDING SITE FOR RESIDUE GTP C 501 source : AC7 15) chain C residue 206 type sequence N description BINDING SITE FOR RESIDUE GTP C 501 source : AC7 16) chain C residue 224 type sequence Y description BINDING SITE FOR RESIDUE GTP C 501 source : AC7 17) chain C residue 228 type sequence N description BINDING SITE FOR RESIDUE GTP C 501 source : AC7 18) chain C residue 71 type sequence E description BINDING SITE FOR RESIDUE MG C 502 source : AC8 19) chain C residue 326 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI12 20) chain C residue 370 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI12 21) chain C residue 11 type MOD_RES sequence Q description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 22) chain C residue 71 type MOD_RES sequence E description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 23) chain C residue 140 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 24) chain C residue 144 type MOD_RES sequence G description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 25) chain C residue 145 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 26) chain C residue 179 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 27) chain C residue 206 type MOD_RES sequence N description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 28) chain C residue 228 type MOD_RES sequence N description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2

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