eF-site ID 3vhx-ABCD PDB Code 3vhx Chain A, B, C, D 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 null (KIF23_HUMAN) Sequence A:  MEMRILMLGLDAAGKTTILYKLKLGQSVTTIPTVGFNVET VTYKNVKFNVWDVGGLDKIRPLWRHYYTGTQGLIFVVDCA DRDRIDEARQELHRIINDREMRDAIILIFANKQDLPDAMK PHEIQEKLGLTRIRDRNWYVQPSCATSGDGLYEGLTWLTS NY B:  DQNAPPIRLRHRRSRSAGDRWVDHKPASNMQTETVMQPHV PHAITVSVANEKALAKCEKYMLTHQELASDGEIETKLIKG DIYKTRGGGQSVQFTDIETLKQESPN C:  MEMRILMLGLDAAGKTTILYKLKLGQSVTTIPTVGFNVET VTYKNVKFNVWDVGGLDKIRPLWRHYYTGTQGLIFVVDCA DRDRIDEARQELHRIINDREMRDAIILIFANKQDLPDAMK PHEIQEKLGLTRIRDRNWYVQPSCATSGDGLYEGLTWLTS NY D:  DQNAPPIRLRHRRSRSAGDRWVDHKPASNMQTETVMQPHV PHAITVSVANEKALAKCEKYMLTHQELASDGEIETKLIKG DIYKTRGGGQSVQFTDIETLKQESPN Description Functional site 1) chain A residue 22 type sequence D description BINDING SITE FOR RESIDUE GTP A 184 source : AC1 2) chain A residue 23 type sequence A description BINDING SITE FOR RESIDUE GTP A 184 source : AC1 3) chain A residue 24 type sequence A description BINDING SITE FOR RESIDUE GTP A 184 source : AC1 4) chain A residue 25 type sequence G description BINDING SITE FOR RESIDUE GTP A 184 source : AC1 5) chain A residue 26 type sequence K description BINDING SITE FOR RESIDUE GTP A 184 source : AC1 6) chain A residue 27 type sequence T description BINDING SITE FOR RESIDUE GTP A 184 source : AC1 7) chain A residue 28 type sequence T description BINDING SITE FOR RESIDUE GTP A 184 source : AC1 8) chain A residue 41 type sequence T description BINDING SITE FOR RESIDUE GTP A 184 source : AC1 9) chain A residue 44 type sequence T description BINDING SITE FOR RESIDUE GTP A 184 source : AC1 10) chain A residue 66 type sequence G description BINDING SITE FOR RESIDUE GTP A 184 source : AC1 11) chain A residue 122 type sequence N description BINDING SITE FOR RESIDUE GTP A 184 source : AC1 12) chain A residue 123 type sequence K description BINDING SITE FOR RESIDUE GTP A 184 source : AC1 13) chain A residue 125 type sequence D description BINDING SITE FOR RESIDUE GTP A 184 source : AC1 14) chain A residue 126 type sequence L description BINDING SITE FOR RESIDUE GTP A 184 source : AC1 15) chain A residue 155 type sequence C description BINDING SITE FOR RESIDUE GTP A 184 source : AC1 16) chain A residue 156 type sequence A description BINDING SITE FOR RESIDUE GTP A 184 source : AC1 17) chain A residue 157 type sequence T description BINDING SITE FOR RESIDUE GTP A 184 source : AC1 18) chain A residue 27 type sequence T description BINDING SITE FOR RESIDUE MG A 185 source : AC2 19) chain A residue 44 type sequence T description BINDING SITE FOR RESIDUE MG A 185 source : AC2 20) chain C residue 22 type sequence D description BINDING SITE FOR RESIDUE GTP C 184 source : AC3 21) chain C residue 23 type sequence A description BINDING SITE FOR RESIDUE GTP C 184 source : AC3 22) chain C residue 24 type sequence A description BINDING SITE FOR RESIDUE GTP C 184 source : AC3 23) chain C residue 25 type sequence G description BINDING SITE FOR RESIDUE GTP C 184 source : AC3 24) chain C residue 26 type sequence K description BINDING SITE FOR RESIDUE GTP C 184 source : AC3 25) chain C residue 27 type sequence T description BINDING SITE FOR RESIDUE GTP C 184 source : AC3 26) chain C residue 28 type sequence T description BINDING SITE FOR RESIDUE GTP C 184 source : AC3 27) chain C residue 41 type sequence T description BINDING SITE FOR RESIDUE GTP C 184 source : AC3 28) chain C residue 43 type sequence P description BINDING SITE FOR RESIDUE GTP C 184 source : AC3 29) chain C residue 44 type sequence T description BINDING SITE FOR RESIDUE GTP C 184 source : AC3 30) chain C residue 65 type sequence G description BINDING SITE FOR RESIDUE GTP C 184 source : AC3 31) chain C residue 66 type sequence G description BINDING SITE FOR RESIDUE GTP C 184 source : AC3 32) chain C residue 122 type sequence N description BINDING SITE FOR RESIDUE GTP C 184 source : AC3 33) chain C residue 123 type sequence K description BINDING SITE FOR RESIDUE GTP C 184 source : AC3 34) chain C residue 125 type sequence D description BINDING SITE FOR RESIDUE GTP C 184 source : AC3 35) chain C residue 126 type sequence L description BINDING SITE FOR RESIDUE GTP C 184 source : AC3 36) chain C residue 155 type sequence C description BINDING SITE FOR RESIDUE GTP C 184 source : AC3 37) chain C residue 156 type sequence A description BINDING SITE FOR RESIDUE GTP C 184 source : AC3 38) chain C residue 27 type sequence T description BINDING SITE FOR RESIDUE MG C 185 source : AC4 39) chain C residue 44 type sequence T description BINDING SITE FOR RESIDUE MG C 185 source : AC4 40) chain B 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 41) chain D 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 42) chain B 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 43) chain B 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 44) chain B 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 45) chain B 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 46) chain D 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 47) chain D 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 48) chain D 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 49) chain D 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 50) chain B 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 51) chain D 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 52) chain B residue 710 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17081983 source Swiss-Prot : SWS_FT_FI1 53) chain D residue 710 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17081983 source Swiss-Prot : SWS_FT_FI1 54) chain C residue 63 type MOD_RES sequence D description Phosphoserine => ECO:0007744|PubMed:17081983 source Swiss-Prot : SWS_FT_FI1 55) chain C residue 122 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:17081983 source Swiss-Prot : SWS_FT_FI1 56) chain B 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 57) chain D 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

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