eF-site ID 3vhx-EFGH PDB Code 3vhx Chain E, F, G, H click to enlarge Title The crystal structure of Arf6-MKLP1 (Mitotic kinesin-like protein 1) complex Classification CELL CYCLE/SIGNALING PROTEIN Compound ADP-ribosylation factor 6 Source Mus musculus (Mouse) (KIF23_HUMAN) Sequence E:  MEMRILMLGLDAAGKTTILYKLKLGQSVTTIPTVGFNVET VTYKNVKFNVWDVGGLDKIRPLWRHYYTGTQGLIFVVDCA DRDRIDEARQELHRIINDREMRDAIILIFANKQDLPDAMK PHEIQEKLGLTRIRDRNWYVQPSCATSGDGLYEGLTWLTS NY F:  PPIRLRHRRSRSAGDRWVDHKPASNMQTETVMQPHVPHAI TVSVANEKALAKCEKYMLTHQELASDGEIETKLIKGDIYK TRGGGQSVQFTDIETLKQESPN G:  MEMRILMLGLDAAGKTTILYKLKLGQSVTTIPTVGFNVET VTYKNVKFNVWDVGGLDKIRPLWRHYYTGTQGLIFVVDCA DRDRIDEARQELHRIINDREMRDAIILIFANKQDLPDAMK PHEIQEKLGLTRIRDRNWYVQPSCATSGDGLYEGLTWLTS NY H:  DRWVDHKPASNMQTETVMQPHVPHAITVSVANEKALAKCE KYMLTHQELASDGEIETKLIKGDIYKTRGGGQSVQFTDIE TLKQESPN Description Functional site 1) chain E residue 22 type sequence D description BINDING SITE FOR RESIDUE GTP E 184 source : AC5 2) chain E residue 23 type sequence A description BINDING SITE FOR RESIDUE GTP E 184 source : AC5 3) chain E residue 24 type sequence A description BINDING SITE FOR RESIDUE GTP E 184 source : AC5 4) chain E residue 25 type sequence G description BINDING SITE FOR RESIDUE GTP E 184 source : AC5 5) chain E residue 26 type sequence K description BINDING SITE FOR RESIDUE GTP E 184 source : AC5 6) chain E residue 27 type sequence T description BINDING SITE FOR RESIDUE GTP E 184 source : AC5 7) chain E residue 28 type sequence T description BINDING SITE FOR RESIDUE GTP E 184 source : AC5 8) chain E residue 41 type sequence T description BINDING SITE FOR RESIDUE GTP E 184 source : AC5 9) chain E residue 43 type sequence P description BINDING SITE FOR RESIDUE GTP E 184 source : AC5 10) chain E residue 44 type sequence T description BINDING SITE FOR RESIDUE GTP E 184 source : AC5 11) chain E residue 66 type sequence G description BINDING SITE FOR RESIDUE GTP E 184 source : AC5 12) chain E residue 67 type sequence L description BINDING SITE FOR RESIDUE GTP E 184 source : AC5 13) chain E residue 122 type sequence N description BINDING SITE FOR RESIDUE GTP E 184 source : AC5 14) chain E residue 123 type sequence K description BINDING SITE FOR RESIDUE GTP E 184 source : AC5 15) chain E residue 125 type sequence D description BINDING SITE FOR RESIDUE GTP E 184 source : AC5 16) chain E residue 126 type sequence L description BINDING SITE FOR RESIDUE GTP E 184 source : AC5 17) chain E residue 155 type sequence C description BINDING SITE FOR RESIDUE GTP E 184 source : AC5 18) chain E residue 156 type sequence A description BINDING SITE FOR RESIDUE GTP E 184 source : AC5 19) chain E residue 27 type sequence T description BINDING SITE FOR RESIDUE MG E 185 source : AC6 20) chain E residue 44 type sequence T description BINDING SITE FOR RESIDUE MG E 185 source : AC6 21) chain E residue 75 type sequence R description BINDING SITE FOR RESIDUE GOL F 1 source : AC7 22) chain E residue 76 type sequence H description BINDING SITE FOR RESIDUE GOL F 1 source : AC7 23) chain F residue 720 type sequence P description BINDING SITE FOR RESIDUE GOL F 1 source : AC7 24) chain F residue 721 type sequence A description BINDING SITE FOR RESIDUE GOL F 1 source : AC7 25) chain F residue 722 type sequence S description BINDING SITE FOR RESIDUE GOL F 1 source : AC7 26) chain G residue 22 type sequence D description BINDING SITE FOR RESIDUE GTP G 184 source : AC8 27) chain G residue 23 type sequence A description BINDING SITE FOR RESIDUE GTP G 184 source : AC8 28) chain G residue 25 type sequence G description BINDING SITE FOR RESIDUE GTP G 184 source : AC8 29) chain G residue 26 type sequence K description BINDING SITE FOR RESIDUE GTP G 184 source : AC8 30) chain G residue 27 type sequence T description BINDING SITE FOR RESIDUE GTP G 184 source : AC8 31) chain G residue 28 type sequence T description BINDING SITE FOR RESIDUE GTP G 184 source : AC8 32) chain G residue 41 type sequence T description BINDING SITE FOR RESIDUE GTP G 184 source : AC8 33) chain G residue 44 type sequence T description BINDING SITE FOR RESIDUE GTP G 184 source : AC8 34) chain G residue 66 type sequence G description BINDING SITE FOR RESIDUE GTP G 184 source : AC8 35) chain G residue 122 type sequence N description BINDING SITE FOR RESIDUE GTP G 184 source : AC8 36) chain G residue 123 type sequence K description BINDING SITE FOR RESIDUE GTP G 184 source : AC8 37) chain G residue 125 type sequence D description BINDING SITE FOR RESIDUE GTP G 184 source : AC8 38) chain G residue 126 type sequence L description BINDING SITE FOR RESIDUE GTP G 184 source : AC8 39) chain G residue 155 type sequence C description BINDING SITE FOR RESIDUE GTP G 184 source : AC8 40) chain G residue 156 type sequence A description BINDING SITE FOR RESIDUE GTP G 184 source : AC8 41) chain G residue 157 type sequence T description BINDING SITE FOR RESIDUE GTP G 184 source : AC8 42) chain G residue 27 type sequence T description BINDING SITE FOR RESIDUE MG G 185 source : AC9 43) chain G residue 44 type sequence T description BINDING SITE FOR RESIDUE MG G 185 source : AC9 44) chain G residue 23 type MOD_RES sequence A description Phosphoserine => ECO:0007744|PubMed:17081983 source Swiss-Prot : SWS_FT_FI1 45) chain G residue 63 type MOD_RES sequence D description Phosphoserine => ECO:0007744|PubMed:17081983 source Swiss-Prot : SWS_FT_FI1 46) chain G residue 122 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:17081983 source Swiss-Prot : SWS_FT_FI1 47) chain F residue 710 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17081983 source Swiss-Prot : SWS_FT_FI1 48) chain E residue 23 type MOD_RES sequence A description Phosphoserine => ECO:0007744|PubMed:17081983 source Swiss-Prot : SWS_FT_FI1 49) chain E residue 63 type MOD_RES sequence D description Phosphoserine => ECO:0007744|PubMed:17081983 source Swiss-Prot : SWS_FT_FI1 50) chain E residue 122 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:17081983 source Swiss-Prot : SWS_FT_FI1 51) chain F residue 763 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI2 52) chain H residue 763 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI2 53) chain E residue 41 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI2 54) chain E residue 155 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI2 55) chain G residue 41 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI2 56) chain G residue 155 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI2 57) chain F residue 798 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 58) chain H residue 798 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 59) chain F residue 719 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI5 60) chain F residue 750 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI5 61) chain F residue 770 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI5 62) chain F residue 795 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI5 63) chain H residue 719 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI5 64) chain H residue 750 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI5 65) chain H residue 770 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI5 66) chain H residue 795 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI5 67) chain F residue 773 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI6 68) chain H residue 773 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI6

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