eF-site ID 6bw5-ABCD PDB Code 6bw5 Chain A, B, C, D click to enlarge Title Human GPT (DPAGT1) in complex with tunicamycin Classification TRANSFERASE/ANTIBIOTIC Compound UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase Source (GPT_HUMAN) Sequence A:  PMPLLINLIVSLLGFVATVTLIPAFRGHFIAARLCGQDLN KTSRQQIPESQGVISGAVFLIILFCFIPFPFLNCAFPHHE FVALIGALLAICCMIFLGFADDVLNLRWRHKLLLPTAASL PLLMVYFTNFGNTTIHLDLGILYYVYMGLLAVFCTNAINI LAGINGLEAGQSLVISASIIVFNLVELEGDCRDDHVFSLY FMIPFFFTTLGLLYHNWYPSRVFVGDTFCYFAGMTFAVVG ILGHFSKTMLLFFMPQVFNFLYSLPQLLHIIPCPRHRIPR LNIKTGKLEMSYSKFKTKSLSFLGTFILKVAESLQLVTVH QSETEDGEFTECNNMTLINLLLKVLGPIHERNLTLLLLLL QILGSAITFSIRYQLVRL B:  MPLLINLIVSLLGFVATVTLIPAFRGHFIAARLCGQDLNK TSRQQIPESQGVISGAVFLIILFCFIPFPFLNCAFPHHEF VALIGALLAICCMIFLGFADDVLNLRWRHKLLLPTAASLP LLMVYFTNFGNTTIVVHLDLGILYYVYMGLLAVFCTNAIN ILAGINGLEAGQSLVISASIIVFNLVELEGDCRDDHVFSL YFMIPFFFTTLGLLYHNWYPSRVFVGDTFCYFAGMTFAVV GILGHFSKTMLLFFMPQVFNFLYSLPQLLHIIPCPRHRIP RLNIKTGKLEMSYSKFKTKFLGTFILKVAESLQLVTVHQE DGEFTECNNMTLINLLLKVLGPIHERNLTLLLLLLQILGS AITFSIRYQ C:  PMPLLINLIVSLLGFVATVTLIPAFRGHFIAARLCGQDLN KTSRQQIPESQGVISGAVFLIILFCFIPFPFLNCAFPHHE FVALIGALLAICCMIFLGFADDVLNLRWRHKLLLPTAASL PLLMVYFTNFGNTTIHLDLGILYYVYMGLLAVFCTNAINI LAGINGLEAGQSLVISASIIVFNLVELEGDCRDDHVFSLY FMIPFFFTTLGLLYHNWYPSRVFVGDTFCYFAGMTFAVVG ILGHFSKTMLLFFMPQVFNFLYSLPQLLHIIPCPRHRIPR LNIKTGKLEMSYSKFKTKSLSFLGTFILKVAESLQLVTVH QSETEDGEFTECNNMTLINLLLKVLGPIHERNLTLLLLLL QILGSAITFSIRYQL D:  MPLLINLIVSLLGFVATVTLIPAFRGHFIAARLCGQDLNK TSRQQIPESQGVISGAVFLIILFCFIPFPFLNCAFPHHEF VALIGALLAICCMIFLGFADDVLNLRWRHKLLLPTAASLP LLMVYFTNFGNTTILDLGILYYVYMGLLAVFCTNAINILA GINGLEAGQSLVISASIIVFNLVELEGDCRDDHVFSLYFM IPFFFTTLGLLYHNWYPSRVFVGDTFCYFAGMTFAVVGIL GHFSKTMLLFFMPQVFNFLYSLPQLLHIIPCPRHRIPRLN IKTGKLEMSYSKFKTKLSFLGTFILKVAESLVTVHQFTEC NNMTLINLLLKVLGPIHERNLTLLLLLLQILGSAITFSIR YQ Description Functional site 1) chain A residue 44 type sequence Q description binding site for residue TUM A 501 source : AC1 2) chain A residue 45 type sequence D description binding site for residue TUM A 501 source : AC1 3) chain A residue 46 type sequence L description binding site for residue TUM A 501 source : AC1 4) chain A residue 56 type sequence E description binding site for residue TUM A 501 source : AC1 5) chain A residue 119 type sequence N description binding site for residue TUM A 501 source : AC1 6) chain A residue 122 type sequence W description binding site for residue TUM A 501 source : AC1 7) chain A residue 125 type sequence K description binding site for residue TUM A 501 source : AC1 8) chain A residue 126 type sequence L description binding site for residue TUM A 501 source : AC1 9) chain A residue 182 type sequence N description binding site for residue TUM A 501 source : AC1 10) chain A residue 185 type sequence N description binding site for residue TUM A 501 source : AC1 11) chain A residue 186 type sequence I description binding site for residue TUM A 501 source : AC1 12) chain A residue 188 type sequence A description binding site for residue TUM A 501 source : AC1 13) chain A residue 189 type sequence G description binding site for residue TUM A 501 source : AC1 14) chain A residue 190 type sequence I description binding site for residue TUM A 501 source : AC1 15) chain A residue 191 type sequence N description binding site for residue TUM A 501 source : AC1 16) chain A residue 252 type sequence D description binding site for residue TUM A 501 source : AC1 17) chain A residue 286 type sequence F description binding site for residue TUM A 501 source : AC1 18) chain A residue 302 type sequence H description binding site for residue TUM A 501 source : AC1 19) chain A residue 303 type sequence R description binding site for residue TUM A 501 source : AC1 20) chain A residue 304 type sequence I description binding site for residue TUM A 501 source : AC1 21) chain A residue 107 type sequence C description binding site for residue PGW A 502 source : AC2 22) chain A residue 110 type sequence F description binding site for residue PGW A 502 source : AC2 23) chain A residue 111 type sequence L description binding site for residue PGW A 502 source : AC2 24) chain A residue 114 type sequence A description binding site for residue PGW A 502 source : AC2 25) chain A residue 124 type sequence H description binding site for residue PGW A 502 source : AC2 26) chain B residue 64 type sequence A description binding site for residue PGW A 502 source : AC2 27) chain B residue 68 type sequence I description binding site for residue PGW A 502 source : AC2 28) chain B residue 71 type sequence F description binding site for residue PGW A 502 source : AC2 29) chain B residue 44 type sequence Q description binding site for residue TUM B 501 source : AC3 30) chain B residue 45 type sequence D description binding site for residue TUM B 501 source : AC3 31) chain B residue 46 type sequence L description binding site for residue TUM B 501 source : AC3 32) chain B residue 119 type sequence N description binding site for residue TUM B 501 source : AC3 33) chain B residue 122 type sequence W description binding site for residue TUM B 501 source : AC3 34) chain B residue 125 type sequence K description binding site for residue TUM B 501 source : AC3 35) chain B residue 126 type sequence L description binding site for residue TUM B 501 source : AC3 36) chain B residue 179 type sequence F description binding site for residue TUM B 501 source : AC3 37) chain B residue 185 type sequence N description binding site for residue TUM B 501 source : AC3 38) chain B residue 186 type sequence I description binding site for residue TUM B 501 source : AC3 39) chain B residue 188 type sequence A description binding site for residue TUM B 501 source : AC3 40) chain B residue 189 type sequence G description binding site for residue TUM B 501 source : AC3 41) chain B residue 190 type sequence I description binding site for residue TUM B 501 source : AC3 42) chain B residue 191 type sequence N description binding site for residue TUM B 501 source : AC3 43) chain B residue 249 type sequence F description binding site for residue TUM B 501 source : AC3 44) chain B residue 252 type sequence D description binding site for residue TUM B 501 source : AC3 45) chain B residue 286 type sequence F description binding site for residue TUM B 501 source : AC3 46) chain B residue 293 type sequence L description binding site for residue TUM B 501 source : AC3 47) chain B residue 301 type sequence R description binding site for residue TUM B 501 source : AC3 48) chain B residue 303 type sequence R description binding site for residue TUM B 501 source : AC3 49) chain B residue 304 type sequence I description binding site for residue TUM B 501 source : AC3 50) chain A residue 31 type sequence A description binding site for residue PGW B 502 source : AC4 51) chain A residue 35 type sequence H description binding site for residue PGW B 502 source : AC4 52) chain A residue 68 type sequence I description binding site for residue PGW B 502 source : AC4 53) chain B residue 110 type sequence F description binding site for residue PGW B 502 source : AC4 54) chain B residue 114 type sequence A description binding site for residue PGW B 502 source : AC4 55) chain B residue 124 type sequence H description binding site for residue PGW B 502 source : AC4 56) chain C residue 44 type sequence Q description binding site for residue TUM C 501 source : AC5 57) chain C residue 45 type sequence D description binding site for residue TUM C 501 source : AC5 58) chain C residue 46 type sequence L description binding site for residue TUM C 501 source : AC5 59) chain C residue 56 type sequence E description binding site for residue TUM C 501 source : AC5 60) chain C residue 119 type sequence N description binding site for residue TUM C 501 source : AC5 61) chain C residue 122 type sequence W description binding site for residue TUM C 501 source : AC5 62) chain C residue 125 type sequence K description binding site for residue TUM C 501 source : AC5 63) chain C residue 126 type sequence L description binding site for residue TUM C 501 source : AC5 64) chain C residue 185 type sequence N description binding site for residue TUM C 501 source : AC5 65) chain C residue 186 type sequence I description binding site for residue TUM C 501 source : AC5 66) chain C residue 188 type sequence A description binding site for residue TUM C 501 source : AC5 67) chain C residue 189 type sequence G description binding site for residue TUM C 501 source : AC5 68) chain C residue 190 type sequence I description binding site for residue TUM C 501 source : AC5 69) chain C residue 191 type sequence N description binding site for residue TUM C 501 source : AC5 70) chain C residue 249 type sequence F description binding site for residue TUM C 501 source : AC5 71) chain C residue 252 type sequence D description binding site for residue TUM C 501 source : AC5 72) chain C residue 286 type sequence F description binding site for residue TUM C 501 source : AC5 73) chain C residue 293 type sequence L description binding site for residue TUM C 501 source : AC5 74) chain C residue 301 type sequence R description binding site for residue TUM C 501 source : AC5 75) chain C residue 302 type sequence H description binding site for residue TUM C 501 source : AC5 76) chain C residue 303 type sequence R description binding site for residue TUM C 501 source : AC5 77) chain C residue 304 type sequence I description binding site for residue TUM C 501 source : AC5 78) chain C residue 110 type sequence F description binding site for residue PGW C 502 source : AC6 79) chain C residue 111 type sequence L description binding site for residue PGW C 502 source : AC6 80) chain C residue 114 type sequence A description binding site for residue PGW C 502 source : AC6 81) chain C residue 124 type sequence H description binding site for residue PGW C 502 source : AC6 82) chain D residue 28 type sequence L description binding site for residue PGW C 502 source : AC6 83) chain D residue 31 type sequence A description binding site for residue PGW C 502 source : AC6 84) chain D residue 32 type sequence F description binding site for residue PGW C 502 source : AC6 85) chain D residue 35 type sequence H description binding site for residue PGW C 502 source : AC6 86) chain D residue 68 type sequence I description binding site for residue PGW C 502 source : AC6 87) chain D residue 71 type sequence F description binding site for residue PGW C 502 source : AC6 88) chain D residue 44 type sequence Q description binding site for residue TUM D 501 source : AC7 89) chain D residue 45 type sequence D description binding site for residue TUM D 501 source : AC7 90) chain D residue 46 type sequence L description binding site for residue TUM D 501 source : AC7 91) chain D residue 119 type sequence N description binding site for residue TUM D 501 source : AC7 92) chain D residue 122 type sequence W description binding site for residue TUM D 501 source : AC7 93) chain D residue 125 type sequence K description binding site for residue TUM D 501 source : AC7 94) chain D residue 126 type sequence L description binding site for residue TUM D 501 source : AC7 95) chain D residue 179 type sequence F description binding site for residue TUM D 501 source : AC7 96) chain D residue 185 type sequence N description binding site for residue TUM D 501 source : AC7 97) chain D residue 188 type sequence A description binding site for residue TUM D 501 source : AC7 98) chain D residue 189 type sequence G description binding site for residue TUM D 501 source : AC7 99) chain D residue 191 type sequence N description binding site for residue TUM D 501 source : AC7 100) chain D residue 249 type sequence F description binding site for residue TUM D 501 source : AC7 101) chain D residue 252 type sequence D description binding site for residue TUM D 501 source : AC7 102) chain D residue 293 type sequence L description binding site for residue TUM D 501 source : AC7 103) chain D residue 303 type sequence R description binding site for residue TUM D 501 source : AC7 104) chain D residue 304 type sequence I description binding site for residue TUM D 501 source : AC7 105) chain C residue 31 type sequence A description binding site for residue PGW D 502 source : AC8 106) chain C residue 35 type sequence H description binding site for residue PGW D 502 source : AC8 107) chain C residue 68 type sequence I description binding site for residue PGW D 502 source : AC8 108) chain D residue 107 type sequence C description binding site for residue PGW D 502 source : AC8 109) chain D residue 111 type sequence L description binding site for residue PGW D 502 source : AC8 110) chain D residue 114 type sequence A description binding site for residue PGW D 502 source : AC8 111) chain D residue 124 type sequence H description binding site for residue PGW D 502 source : AC8 112) chain C residue 46 type BINDING sequence L description BINDING => ECO:0000269|PubMed:29459785, ECO:0007744|PDB:6BW5, ECO:0007744|PDB:6BW6 source Swiss-Prot : SWS_FT_FI14 113) chain C residue 303 type BINDING sequence R description BINDING => ECO:0000269|PubMed:29459785, ECO:0007744|PDB:6BW5, ECO:0007744|PDB:6BW6 source Swiss-Prot : SWS_FT_FI14 114) chain D residue 46 type BINDING sequence L description BINDING => ECO:0000269|PubMed:29459785, ECO:0007744|PDB:6BW5, ECO:0007744|PDB:6BW6 source Swiss-Prot : SWS_FT_FI14 115) chain D residue 303 type BINDING sequence R description BINDING => ECO:0000269|PubMed:29459785, ECO:0007744|PDB:6BW5, ECO:0007744|PDB:6BW6 source Swiss-Prot : SWS_FT_FI14 116) chain A residue 303 type BINDING sequence R description BINDING => ECO:0000269|PubMed:29459785, ECO:0007744|PDB:6BW5, ECO:0007744|PDB:6BW6 source Swiss-Prot : SWS_FT_FI14 117) chain B residue 46 type BINDING sequence L description BINDING => ECO:0000269|PubMed:29459785, ECO:0007744|PDB:6BW5, ECO:0007744|PDB:6BW6 source Swiss-Prot : SWS_FT_FI14 118) chain B residue 303 type BINDING sequence R description BINDING => ECO:0000269|PubMed:29459785, ECO:0007744|PDB:6BW5, ECO:0007744|PDB:6BW6 source Swiss-Prot : SWS_FT_FI14 119) chain A residue 46 type BINDING sequence L description BINDING => ECO:0000269|PubMed:29459785, ECO:0007744|PDB:6BW5, ECO:0007744|PDB:6BW6 source Swiss-Prot : SWS_FT_FI14 120) chain A residue 125 type BINDING sequence K description BINDING => ECO:0000305|PubMed:30388443 source Swiss-Prot : SWS_FT_FI16 121) chain A residue 178 type BINDING sequence V description BINDING => ECO:0000305|PubMed:30388443 source Swiss-Prot : SWS_FT_FI16 122) chain B residue 125 type BINDING sequence K description BINDING => ECO:0000305|PubMed:30388443 source Swiss-Prot : SWS_FT_FI16 123) chain B residue 178 type BINDING sequence V description BINDING => ECO:0000305|PubMed:30388443 source Swiss-Prot : SWS_FT_FI16 124) chain C residue 125 type BINDING sequence K description BINDING => ECO:0000305|PubMed:30388443 source Swiss-Prot : SWS_FT_FI16 125) chain C residue 178 type BINDING sequence V description BINDING => ECO:0000305|PubMed:30388443 source Swiss-Prot : SWS_FT_FI16 126) chain D residue 125 type BINDING sequence K description BINDING => ECO:0000305|PubMed:30388443 source Swiss-Prot : SWS_FT_FI16 127) chain D residue 178 type BINDING sequence V description BINDING => ECO:0000305|PubMed:30388443 source Swiss-Prot : SWS_FT_FI16 128) chain B residue 146 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI18 129) chain C residue 146 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI18 130) chain D residue 146 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI18 131) chain A residue 146 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI18 132) chain A residue 79-91 type TOPO_DOM sequence LNCAFP description Lumenal => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI1 133) chain A residue 144-166 type TOPO_DOM sequence FGNTTIHLDLG description Lumenal => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI1 134) chain A residue 214-218 type TOPO_DOM sequence EGDCR description Lumenal => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI1 135) chain A residue 270-271 type TOPO_DOM sequence HF description Lumenal => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI1 136) chain B residue 79-91 type TOPO_DOM sequence LNCAFP description Lumenal => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI1 137) chain B residue 144-166 type TOPO_DOM sequence FGNTTIVVHLDLG description Lumenal => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI1 138) chain B residue 214-218 type TOPO_DOM sequence EGDCR description Lumenal => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI1 139) chain B residue 270-271 type TOPO_DOM sequence HF description Lumenal => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI1 140) chain C residue 79-91 type TOPO_DOM sequence LNCAFP description Lumenal => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI1 141) chain C residue 144-166 type TOPO_DOM sequence FGNTTIHLDLG description Lumenal => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI1 142) chain C residue 214-218 type TOPO_DOM sequence EGDCR description Lumenal => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI1 143) chain C residue 270-271 type TOPO_DOM sequence HF description Lumenal => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI1 144) chain D residue 79-91 type TOPO_DOM sequence LNCAFP description Lumenal => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI1 145) chain D residue 144-166 type TOPO_DOM sequence FGNTTILDLG description Lumenal => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI1 146) chain D residue 214-218 type TOPO_DOM sequence EGDCR description Lumenal => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI1 147) chain D residue 270-271 type TOPO_DOM sequence HF description Lumenal => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI1 148) chain A residue 11-38 type TRANSMEM sequence LLINLIVSLLGFVATVTLIPAFRGHFIA description Helical; Name=Helix 1 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI2 149) chain B residue 11-38 type TRANSMEM sequence LLINLIVSLLGFVATVTLIPAFRGHFIA description Helical; Name=Helix 1 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI2 150) chain C residue 11-38 type TRANSMEM sequence LLINLIVSLLGFVATVTLIPAFRGHFIA description Helical; Name=Helix 1 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI2 151) chain D residue 11-38 type TRANSMEM sequence LLINLIVSLLGFVATVTLIPAFRGHFIA description Helical; Name=Helix 1 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI2 152) chain A residue 39-58 type TOPO_DOM sequence ARLCGQDLNKTSRQQIPESQ description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 153) chain A residue 119-121 type TOPO_DOM sequence NLR description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 154) chain A residue 187-192 type TOPO_DOM sequence LAGING description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 155) chain A residue 243-250 type TOPO_DOM sequence WYPSRVFV description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 156) chain A residue 294-375 type TOPO_DOM sequence LHIIPCPRHRIPRLNIKTGKLEMSYSKFKTKSLSFLGTFI LKVAESLQLVTVHQSETEDGEFTECNNMTLINLLLKVLGP IH description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 157) chain B residue 39-58 type TOPO_DOM sequence ARLCGQDLNKTSRQQIPESQ description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 158) chain B residue 119-121 type TOPO_DOM sequence NLR description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 159) chain B residue 187-192 type TOPO_DOM sequence LAGING description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 160) chain B residue 243-250 type TOPO_DOM sequence WYPSRVFV description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 161) chain B residue 294-375 type TOPO_DOM sequence LHIIPCPRHRIPRLNIKTGKLEMSYSKFKTKFLGTFILKV AESLQLVTVHQEDGEFTECNNMTLINLLLKVLGPIH description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 162) chain C residue 39-58 type TOPO_DOM sequence ARLCGQDLNKTSRQQIPESQ description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 163) chain C residue 119-121 type TOPO_DOM sequence NLR description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 164) chain C residue 187-192 type TOPO_DOM sequence LAGING description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 165) chain C residue 243-250 type TOPO_DOM sequence WYPSRVFV description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 166) chain C residue 294-375 type TOPO_DOM sequence LHIIPCPRHRIPRLNIKTGKLEMSYSKFKTKSLSFLGTFI LKVAESLQLVTVHQSETEDGEFTECNNMTLINLLLKVLGP IH description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 167) chain D residue 39-58 type TOPO_DOM sequence ARLCGQDLNKTSRQQIPESQ description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 168) chain D residue 119-121 type TOPO_DOM sequence NLR description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 169) chain D residue 187-192 type TOPO_DOM sequence LAGING description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 170) chain D residue 243-250 type TOPO_DOM sequence WYPSRVFV description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 171) chain D residue 294-375 type TOPO_DOM sequence LHIIPCPRHRIPRLNIKTGKLEMSYSKFKTKLSFLGTFIL KVAESLVTVHQFTECNNMTLINLLLKVLGPIH description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 172) chain A residue 59-78 type TRANSMEM sequence GVISGAVFLIILFCFIPFPF description Helical; Name=Helix 2 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI4 173) chain B residue 59-78 type TRANSMEM sequence GVISGAVFLIILFCFIPFPF description Helical; Name=Helix 2 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI4 174) chain C residue 59-78 type TRANSMEM sequence GVISGAVFLIILFCFIPFPF description Helical; Name=Helix 2 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI4 175) chain D residue 59-78 type TRANSMEM sequence GVISGAVFLIILFCFIPFPF description Helical; Name=Helix 2 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI4 176) chain A residue 92-118 type TRANSMEM sequence HHEFVALIGALLAICCMIFLGFADDVL description Helical; Name=Helix 3 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI5 177) chain B residue 92-118 type TRANSMEM sequence HHEFVALIGALLAICCMIFLGFADDVL description Helical; Name=Helix 3 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI5 178) chain C residue 92-118 type TRANSMEM sequence HHEFVALIGALLAICCMIFLGFADDVL description Helical; Name=Helix 3 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI5 179) chain D residue 92-118 type TRANSMEM sequence HHEFVALIGALLAICCMIFLGFADDVL description Helical; Name=Helix 3 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI5 180) chain A residue 122-143 type TRANSMEM sequence WRHKLLLPTAASLPLLMVYFTN description Helical; Name=Helix 4 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI6 181) chain B residue 122-143 type TRANSMEM sequence WRHKLLLPTAASLPLLMVYFTN description Helical; Name=Helix 4 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI6 182) chain C residue 122-143 type TRANSMEM sequence WRHKLLLPTAASLPLLMVYFTN description Helical; Name=Helix 4 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI6 183) chain D residue 122-143 type TRANSMEM sequence WRHKLLLPTAASLPLLMVYFTN description Helical; Name=Helix 4 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI6 184) chain A residue 167-186 type TRANSMEM sequence ILYYVYMGLLAVFCTNAINI description Helical; Name=Helix 5 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI7 185) chain B residue 167-186 type TRANSMEM sequence ILYYVYMGLLAVFCTNAINI description Helical; Name=Helix 5 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI7 186) chain C residue 167-186 type TRANSMEM sequence ILYYVYMGLLAVFCTNAINI description Helical; Name=Helix 5 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI7 187) chain D residue 167-186 type TRANSMEM sequence ILYYVYMGLLAVFCTNAINI description Helical; Name=Helix 5 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI7 188) chain A residue 193-213 type TRANSMEM sequence LEAGQSLVISASIIVFNLVEL description Helical; Name=Helix 6 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI8 189) chain B residue 193-213 type TRANSMEM sequence LEAGQSLVISASIIVFNLVEL description Helical; Name=Helix 6 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI8 190) chain C residue 193-213 type TRANSMEM sequence LEAGQSLVISASIIVFNLVEL description Helical; Name=Helix 6 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI8 191) chain D residue 193-213 type TRANSMEM sequence LEAGQSLVISASIIVFNLVEL description Helical; Name=Helix 6 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI8 192) chain A residue 219-242 type TRANSMEM sequence DDHVFSLYFMIPFFFTTLGLLYHN description Helical; Name=Helix 7 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI9 193) chain B residue 219-242 type TRANSMEM sequence DDHVFSLYFMIPFFFTTLGLLYHN description Helical; Name=Helix 7 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI9 194) chain C residue 219-242 type TRANSMEM sequence DDHVFSLYFMIPFFFTTLGLLYHN description Helical; Name=Helix 7 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI9 195) chain D residue 219-242 type TRANSMEM sequence DDHVFSLYFMIPFFFTTLGLLYHN description Helical; Name=Helix 7 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI9 196) chain A residue 251-269 type TRANSMEM sequence GDTFCYFAGMTFAVVGILG description Helical; Name=Helix 8 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI10 197) chain B residue 251-269 type TRANSMEM sequence GDTFCYFAGMTFAVVGILG description Helical; Name=Helix 8 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI10 198) chain C residue 251-269 type TRANSMEM sequence GDTFCYFAGMTFAVVGILG description Helical; Name=Helix 8 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI10 199) chain D residue 251-269 type TRANSMEM sequence GDTFCYFAGMTFAVVGILG description Helical; Name=Helix 8 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI10 200) chain A residue 272-293 type TRANSMEM sequence SKTMLLFFMPQVFNFLYSLPQL description Helical; Name=Helix 9 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI11 201) chain B residue 272-293 type TRANSMEM sequence SKTMLLFFMPQVFNFLYSLPQL description Helical; Name=Helix 9 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI11 202) chain C residue 272-293 type TRANSMEM sequence SKTMLLFFMPQVFNFLYSLPQL description Helical; Name=Helix 9 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI11 203) chain D residue 272-293 type TRANSMEM sequence SKTMLLFFMPQVFNFLYSLPQL description Helical; Name=Helix 9 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI11 204) chain A residue 376-400 type TRANSMEM sequence ERNLTLLLLLLQILGSAITFSIRYQ description Helical; Name=Helix 10 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI12 205) chain B residue 376-400 type TRANSMEM sequence ERNLTLLLLLLQILGSAITFSIRYQ description Helical; Name=Helix 10 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI12 206) chain C residue 376-400 type TRANSMEM sequence ERNLTLLLLLLQILGSAITFSIRYQ description Helical; Name=Helix 10 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI12 207) chain D residue 376-400 type TRANSMEM sequence ERNLTLLLLLLQILGSAITFSIRYQ description Helical; Name=Helix 10 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI12 208) chain C residue 56 type BINDING sequence E description BINDING => ECO:0000269|PubMed:30388443 source Swiss-Prot : SWS_FT_FI13 209) chain C residue 191 type BINDING sequence N description BINDING => ECO:0000269|PubMed:30388443 source Swiss-Prot : SWS_FT_FI13 210) chain C residue 301 type BINDING sequence R description BINDING => ECO:0000269|PubMed:30388443 source Swiss-Prot : SWS_FT_FI13 211) chain D residue 44 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:30388443 source Swiss-Prot : SWS_FT_FI13 212) chain D residue 56 type BINDING sequence E description BINDING => ECO:0000269|PubMed:30388443 source Swiss-Prot : SWS_FT_FI13 213) chain D residue 191 type BINDING sequence N description BINDING => ECO:0000269|PubMed:30388443 source Swiss-Prot : SWS_FT_FI13 214) chain D residue 301 type BINDING sequence R description BINDING => ECO:0000269|PubMed:30388443 source Swiss-Prot : SWS_FT_FI13 215) chain C residue 44 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:30388443 source Swiss-Prot : SWS_FT_FI13 216) chain A residue 56 type BINDING sequence E description BINDING => ECO:0000269|PubMed:30388443 source Swiss-Prot : SWS_FT_FI13 217) chain A residue 191 type BINDING sequence N description BINDING => ECO:0000269|PubMed:30388443 source Swiss-Prot : SWS_FT_FI13 218) chain A residue 301 type BINDING sequence R description BINDING => ECO:0000269|PubMed:30388443 source Swiss-Prot : SWS_FT_FI13 219) chain B residue 44 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:30388443 source Swiss-Prot : SWS_FT_FI13 220) chain B residue 56 type BINDING sequence E description BINDING => ECO:0000269|PubMed:30388443 source Swiss-Prot : SWS_FT_FI13 221) chain B residue 191 type BINDING sequence N description BINDING => ECO:0000269|PubMed:30388443 source Swiss-Prot : SWS_FT_FI13 222) chain B residue 301 type BINDING sequence R description BINDING => ECO:0000269|PubMed:30388443 source Swiss-Prot : SWS_FT_FI13 223) chain A residue 44 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:30388443 source Swiss-Prot : SWS_FT_FI13 224) chain A residue 119 type BINDING sequence N description BINDING => ECO:0000269|PubMed:29459785, ECO:0007744|PDB:6BW5 source Swiss-Prot : SWS_FT_FI15 225) chain A residue 252 type BINDING sequence D description BINDING => ECO:0000269|PubMed:29459785, ECO:0007744|PDB:6BW5 source Swiss-Prot : SWS_FT_FI15 226) chain B residue 119 type BINDING sequence N description BINDING => ECO:0000269|PubMed:29459785, ECO:0007744|PDB:6BW5 source Swiss-Prot : SWS_FT_FI15 227) chain B residue 252 type BINDING sequence D description BINDING => ECO:0000269|PubMed:29459785, ECO:0007744|PDB:6BW5 source Swiss-Prot : SWS_FT_FI15 228) chain C residue 119 type BINDING sequence N description BINDING => ECO:0000269|PubMed:29459785, ECO:0007744|PDB:6BW5 source Swiss-Prot : SWS_FT_FI15 229) chain C residue 252 type BINDING sequence D description BINDING => ECO:0000269|PubMed:29459785, ECO:0007744|PDB:6BW5 source Swiss-Prot : SWS_FT_FI15 230) chain D residue 119 type BINDING sequence N description BINDING => ECO:0000269|PubMed:29459785, ECO:0007744|PDB:6BW5 source Swiss-Prot : SWS_FT_FI15 231) chain D residue 252 type BINDING sequence D description BINDING => ECO:0000269|PubMed:29459785, ECO:0007744|PDB:6BW5 source Swiss-Prot : SWS_FT_FI15 232) chain A residue 185 type BINDING sequence N description BINDING => ECO:0000269|PubMed:29459785, ECO:0007744|PDB:6BW6 source Swiss-Prot : SWS_FT_FI17 233) chain B residue 185 type BINDING sequence N description BINDING => ECO:0000269|PubMed:29459785, ECO:0007744|PDB:6BW6 source Swiss-Prot : SWS_FT_FI17 234) chain C residue 185 type BINDING sequence N description BINDING => ECO:0000269|PubMed:29459785, ECO:0007744|PDB:6BW6 source Swiss-Prot : SWS_FT_FI17 235) chain D residue 185 type BINDING sequence N description BINDING => ECO:0000269|PubMed:29459785, ECO:0007744|PDB:6BW6 source Swiss-Prot : SWS_FT_FI17

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