eF-site ID 3j6p-B PDB Code 3j6p Chain B 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 B:  REIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSD LQLERINVYYNEAAGNKYVPRAILVDLEPGTMDSVRSGPF GQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVR KESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPD RIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYC IDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLR FPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQY RALTVPELTQQMFDAKNMMAACDPRHGRYLTVAAVFRGRM SMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGL KMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGE GMDEMEFTEAESNMNDLVSEYQQYQD Description Functional site 1) chain B residue 248 type sequence L description BINDING SITE FOR RESIDUE GTP A 502 source : AC2 2) chain B residue 254 type sequence K description BINDING SITE FOR RESIDUE GTP A 502 source : AC2 3) chain B residue 10 type sequence G description BINDING SITE FOR RESIDUE GDP B 501 source : AC3 4) chain B residue 11 type sequence Q description BINDING SITE FOR RESIDUE GDP B 501 source : AC3 5) chain B residue 12 type sequence C description BINDING SITE FOR RESIDUE GDP B 501 source : AC3 6) chain B residue 15 type sequence Q description BINDING SITE FOR RESIDUE GDP B 501 source : AC3 7) chain B residue 140 type sequence S description BINDING SITE FOR RESIDUE GDP B 501 source : AC3 8) chain B residue 142 type sequence G description BINDING SITE FOR RESIDUE GDP B 501 source : AC3 9) chain B residue 143 type sequence G description BINDING SITE FOR RESIDUE GDP B 501 source : AC3 10) chain B residue 144 type sequence G description BINDING SITE FOR RESIDUE GDP B 501 source : AC3 11) chain B residue 145 type sequence T description BINDING SITE FOR RESIDUE GDP B 501 source : AC3 12) chain B residue 146 type sequence G description BINDING SITE FOR RESIDUE GDP B 501 source : AC3 13) chain B residue 179 type sequence D description BINDING SITE FOR RESIDUE GDP B 501 source : AC3 14) chain B residue 183 type sequence E description BINDING SITE FOR RESIDUE GDP B 501 source : AC3 15) chain B residue 206 type sequence N description BINDING SITE FOR RESIDUE GDP B 501 source : AC3 16) chain B residue 224 type sequence Y description BINDING SITE FOR RESIDUE GDP B 501 source : AC3 17) chain B residue 228 type sequence N description BINDING SITE FOR RESIDUE GDP B 501 source : AC3 18) chain B residue 23 type sequence V description BINDING SITE FOR RESIDUE TA1 B 502 source : AC4 19) chain B residue 26 type sequence D description BINDING SITE FOR RESIDUE TA1 B 502 source : AC4 20) chain B residue 27 type sequence E description BINDING SITE FOR RESIDUE TA1 B 502 source : AC4 21) chain B residue 226 type sequence D description BINDING SITE FOR RESIDUE TA1 B 502 source : AC4 22) chain B residue 229 type sequence H description BINDING SITE FOR RESIDUE TA1 B 502 source : AC4 23) chain B residue 230 type sequence L description BINDING SITE FOR RESIDUE TA1 B 502 source : AC4 24) chain B residue 233 type sequence A description BINDING SITE FOR RESIDUE TA1 B 502 source : AC4 25) chain B residue 236 type sequence S description BINDING SITE FOR RESIDUE TA1 B 502 source : AC4 26) chain B residue 272 type sequence F description BINDING SITE FOR RESIDUE TA1 B 502 source : AC4 27) chain B residue 275 type sequence L description BINDING SITE FOR RESIDUE TA1 B 502 source : AC4 28) chain B residue 276 type sequence T description BINDING SITE FOR RESIDUE TA1 B 502 source : AC4 29) chain B residue 278 type sequence R description BINDING SITE FOR RESIDUE TA1 B 502 source : AC4 30) chain B residue 360 type sequence P description BINDING SITE FOR RESIDUE TA1 B 502 source : AC4 31) chain B residue 369 type sequence R description BINDING SITE FOR RESIDUE TA1 B 502 source : AC4 32) chain B residue 370 type sequence G description BINDING SITE FOR RESIDUE TA1 B 502 source : AC4 33) chain B residue 371 type sequence L description BINDING SITE FOR RESIDUE TA1 B 502 source : AC4 34) 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 35) chain B residue 71 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 36) chain B residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 37) chain B residue 60 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI4 38) chain B residue 174 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885 source Swiss-Prot : SWS_FT_FI5 39) chain B residue 292 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 40) chain B residue 287 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 41) chain B residue 320 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 42) 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 43) chain B residue 142-148 type prosite sequence GGGTGSG description TUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG source prosite : PS00227 44) chain B residue 140 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 45) chain B residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 46) chain B residue 145 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 47) chain B residue 146 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 48) chain B residue 206 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 49) chain B residue 228 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 50) chain B residue 11 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1

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