eF-site ID 3j6p-ABD PDB Code 3j6p Chain A, B, D click to enlarge Title Pseudo-atomic model of dynein microtubule binding domain-tubulin complex based on a cryoEM map Classification MOTOR PROTEIN/STRUCTURAL PROTEIN Compound Dynein heavy chain, cytoplasmic Source ORGANISM_COMMON: pig; ORGANISM_SCIENTIFIC: Sus scrofa; Sequence A:  RECISIHVGQAGVQIGNACWELYCLEHGIQPDGHVPRAVF VDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGH YTIGKEIIDLVLDRIRKLADQCTGLQGFSVFHSFGGGTGS GFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNS ILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNL NRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRGHF PLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDP RHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWC PTGFKVGINYEPPTVVPGGDLAKVQRAVCMLSNTTAIAEA WARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAA LEKDYEEVGVDS B:  REIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSD LQLERINVYYNEAAGNKYVPRAILVDLEPGTMDSVRSGPF GQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVR KESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPD RIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYC IDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLR FPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQY RALTVPELTQQMFDAKNMMAACDPRHGRYLTVAAVFRGRM SMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGL KMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGE GMDEMEFTEAESNMNDLVSEYQQYQD D:  TIKKKHLDEIKSLPKPPTPVKLAMEAVCLMLGGKKLEWAD IRKKIMEPNFITSIINYDTKKMMTPKIREAITKGYLEDPG FDYETVNRASKACGPLVKWATAQTYYSE Description Functional site 1) chain A residue 11 type sequence Q description BINDING SITE FOR RESIDUE MG A 501 source : AC1 2) chain A residue 71 type sequence E description BINDING SITE FOR RESIDUE MG A 501 source : AC1 3) chain A residue 10 type sequence G description BINDING SITE FOR RESIDUE GTP A 502 source : AC2 4) chain A residue 11 type sequence Q description BINDING SITE FOR RESIDUE GTP A 502 source : AC2 5) chain A residue 12 type sequence A description BINDING SITE FOR RESIDUE GTP A 502 source : AC2 6) chain A residue 15 type sequence Q description BINDING SITE FOR RESIDUE GTP A 502 source : AC2 7) chain A residue 99 type sequence A description BINDING SITE FOR RESIDUE GTP A 502 source : AC2 8) chain A residue 100 type sequence A description BINDING SITE FOR RESIDUE GTP A 502 source : AC2 9) chain A residue 101 type sequence N description BINDING SITE FOR RESIDUE GTP A 502 source : AC2 10) chain A residue 142 type sequence G description BINDING SITE FOR RESIDUE GTP A 502 source : AC2 11) chain A residue 143 type sequence G description BINDING SITE FOR RESIDUE GTP A 502 source : AC2 12) chain A residue 144 type sequence G description BINDING SITE FOR RESIDUE GTP A 502 source : AC2 13) chain A residue 145 type sequence T description BINDING SITE FOR RESIDUE GTP A 502 source : AC2 14) chain A residue 146 type sequence G description BINDING SITE FOR RESIDUE GTP A 502 source : AC2 15) chain A residue 179 type sequence T description BINDING SITE FOR RESIDUE GTP A 502 source : AC2 16) chain A residue 183 type sequence E description BINDING SITE FOR RESIDUE GTP A 502 source : AC2 17) chain A residue 206 type sequence N description BINDING SITE FOR RESIDUE GTP A 502 source : AC2 18) chain A residue 224 type sequence Y description BINDING SITE FOR RESIDUE GTP A 502 source : AC2 19) chain A residue 228 type sequence N description BINDING SITE FOR RESIDUE GTP A 502 source : AC2 20) chain B residue 248 type sequence L description BINDING SITE FOR RESIDUE GTP A 502 source : AC2 21) chain B residue 254 type sequence K description BINDING SITE FOR RESIDUE GTP A 502 source : AC2 22) chain B residue 10 type sequence G description BINDING SITE FOR RESIDUE GDP B 501 source : AC3 23) chain B residue 11 type sequence Q description BINDING SITE FOR RESIDUE GDP B 501 source : AC3 24) chain B residue 12 type sequence C description BINDING SITE FOR RESIDUE GDP B 501 source : AC3 25) chain B residue 15 type sequence Q description BINDING SITE FOR RESIDUE GDP B 501 source : AC3 26) chain B residue 140 type sequence S description BINDING SITE FOR RESIDUE GDP B 501 source : AC3 27) chain B residue 142 type sequence G description BINDING SITE FOR RESIDUE GDP B 501 source : AC3 28) chain B residue 143 type sequence G description BINDING SITE FOR RESIDUE GDP B 501 source : AC3 29) chain B residue 144 type sequence G description BINDING SITE FOR RESIDUE GDP B 501 source : AC3 30) chain B residue 145 type sequence T description BINDING SITE FOR RESIDUE GDP B 501 source : AC3 31) chain B residue 146 type sequence G description BINDING SITE FOR RESIDUE GDP B 501 source : AC3 32) chain B residue 179 type sequence D description BINDING SITE FOR RESIDUE GDP B 501 source : AC3 33) chain B residue 183 type sequence E description BINDING SITE FOR RESIDUE GDP B 501 source : AC3 34) chain B residue 206 type sequence N description BINDING SITE FOR RESIDUE GDP B 501 source : AC3 35) chain B residue 224 type sequence Y description BINDING SITE FOR RESIDUE GDP B 501 source : AC3 36) chain B residue 228 type sequence N description BINDING SITE FOR RESIDUE GDP B 501 source : AC3 37) chain B residue 23 type sequence V description BINDING SITE FOR RESIDUE TA1 B 502 source : AC4 38) chain B residue 26 type sequence D description BINDING SITE FOR RESIDUE TA1 B 502 source : AC4 39) chain B residue 27 type sequence E description BINDING SITE FOR RESIDUE TA1 B 502 source : AC4 40) chain B residue 226 type sequence D description BINDING SITE FOR RESIDUE TA1 B 502 source : AC4 41) chain B residue 229 type sequence H description BINDING SITE FOR RESIDUE TA1 B 502 source : AC4 42) chain B residue 230 type sequence L description BINDING SITE FOR RESIDUE TA1 B 502 source : AC4 43) chain B residue 233 type sequence A description BINDING SITE FOR RESIDUE TA1 B 502 source : AC4 44) chain B residue 236 type sequence S description BINDING SITE FOR RESIDUE TA1 B 502 source : AC4 45) chain B residue 272 type sequence F description BINDING SITE FOR RESIDUE TA1 B 502 source : AC4 46) chain B residue 275 type sequence L description BINDING SITE FOR RESIDUE TA1 B 502 source : AC4 47) chain B residue 276 type sequence T description BINDING SITE FOR RESIDUE TA1 B 502 source : AC4 48) chain B residue 278 type sequence R description BINDING SITE FOR RESIDUE TA1 B 502 source : AC4 49) chain B residue 360 type sequence P description BINDING SITE FOR RESIDUE TA1 B 502 source : AC4 50) chain B residue 369 type sequence R description BINDING SITE FOR RESIDUE TA1 B 502 source : AC4 51) chain B residue 370 type sequence G description BINDING SITE FOR RESIDUE TA1 B 502 source : AC4 52) chain B residue 371 type sequence L description BINDING SITE FOR RESIDUE TA1 B 502 source : AC4 53) 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 54) chain A residue 71 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 55) chain A residue 140 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 56) chain A residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 57) chain A residue 145 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 58) chain A residue 179 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 59) chain A residue 206 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 60) chain A residue 228 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 61) chain B residue 71 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 62) chain B residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 63) chain B residue 60 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI4 64) chain B residue 174 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885 source Swiss-Prot : SWS_FT_FI5 65) chain B residue 292 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 66) chain B residue 287 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 67) chain B residue 320 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 68) 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 69) chain B residue 142-148 type prosite sequence GGGTGSG description TUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG source prosite : PS00227 70) chain A residue 142-148 type prosite sequence GGGTGSG description TUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG source prosite : PS00227 71) chain B residue 140 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 72) chain B residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 73) chain B residue 145 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 74) chain B residue 146 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 75) chain B residue 206 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 76) chain B residue 228 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 77) chain B residue 11 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1

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