eF-site ID 6bw6-ABCD PDB Code 6bw6 Chain A, B, C, D click to enlarge Title Human GPT (DPAGT1) H129 variant in complex with tunicamycin Classification TRANSFERASE/ANTIBIOTIC Compound UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase Source (GPT_HUMAN) Sequence A:  PMPLLINLIVSLLGFVATVTLIPAFRGHFIAARLCGQDLN KTSRQQIPESQGVISGAVFLIILFCFIPFPFLNCAFPHHE FVALIGALLAICCMIFLGFADDVLNLRWRHKLLLHTAASL PLLMVYFTNFGNTTIVVHLDLGILYYVYMGLLAVFCTNAI NILAGINGLEAGQSLVISASIIVFNLVELEGDCRDDHVFS LYFMIPFFFTTLGLLYHNWYPSRVFVGDTFCYFAGMTFAV VGILGHFSKTMLLFFMPQVFNFLYSLPQLLHIIPCPRHRI PRLNIKTGKLEMSYSKFKTKSLSFLGTFILKVAESLQLVT VHQFTECNNMTLINLLLKVLGPIHERNLTLLLLLLQILGS AITFSIRY B:  PMPLLINLIVSLLGFVATVTLIPAFRGHFIAARLCGQDLN KTSRQQIPESQGVISGAVFLIILFCFIPFPFLNCCKAFPH HEFVALIGALLAICCMIFLGFADDVLNLRWRHKLLLHTAA SLPLLMVYFTNFGNTTIVVHLDLGILYYVYMGLLAVFCTN AINILAGINGLEAGQSLVISASIIVFNLVELEGDCRDDHV FSLYFMIPFFFTTLGLLYHNWYPSRVFVGDTFCYFAGMTF AVVGILGHFSKTMLLFFMPQVFNFLYSLPQLLHIIPCPRH RIPRLNIKTGKLEMSYSKFKTKSLSFLGTFILKVAESLQL VTVHQFTECNNMTLINLLLKVLGPIHERNLTLLLLLLQIL GSAITFSIRYQLVR C:  PMPLLINLIVSLLGFVATVTLIPAFRGHFIAARLCGQDLN KTSRQQIPESQGVISGAVFLIILFCFIPFPFLNCAFPHHE FVALIGALLAICCMIFLGFADDVLNLRWRHKLLLHTAASL PLLMVYFTNFGNTTIVHLDLGILYYVYMGLLAVFCTNAIN ILAGINGLEAGQSLVISASIIVFNLVELEGDCRDDHVFSL YFMIPFFFTTLGLLYHNWYPSRVFVGDTFCYFAGMTFAVV GILGHFSKTMLLFFMPQVFNFLYSLPQLLHIIPCPRHRIP RLNIKTGKLEMSYSKFKTKSLSFLGTFILKVAESLQLVTV HQCNNMTLINLLLKVLGPIHERNLTLLLLLLQILGSAITF SIRYQ D:  PMPLLINLIVSLLGFVATVTLIPAFRGHFIAARLCGQDLN KTSRQQIPESQGVISGAVFLIILFCFIPFPFLNCAFPHHE FVALIGALLAICCMIFLGFADDVLNLRWRHKLLLHTAASL PLLMVYFTNFGNTTIVVHLDLGILYYVYMGLLAVFCTNAI NILAGINGLEAGQSLVISASIIVFNLVELEGDCRDDHVFS LYFMIPFFFTTLGLLYHNWYPSRVFVGDTFCYFAGMTFAV VGILGHFSKTMLLFFMPQVFNFLYSLPQLLHIIPCPRHRI PRLNIKTGKLEMSYSKFKTKSLSFLGTFILKVAESLQLVT VHQTECNNMTLINLLLKVLGPIHERNLTLLLLLLQILGSA ITFSIRYQL 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 46 type sequence L description binding site for residue TUM A 501 source : AC1 3) chain A residue 122 type sequence W description binding site for residue TUM A 501 source : AC1 4) chain A residue 182 type sequence N description binding site for residue TUM A 501 source : AC1 5) chain A residue 185 type sequence N description binding site for residue TUM A 501 source : AC1 6) chain A residue 186 type sequence I description binding site for residue TUM A 501 source : AC1 7) chain A residue 188 type sequence A description binding site for residue TUM A 501 source : AC1 8) chain A residue 189 type sequence G description binding site for residue TUM A 501 source : AC1 9) chain A residue 191 type sequence N description binding site for residue TUM A 501 source : AC1 10) chain A residue 249 type sequence F description binding site for residue TUM A 501 source : AC1 11) chain A residue 252 type sequence D description binding site for residue TUM A 501 source : AC1 12) chain A residue 301 type sequence R description binding site for residue TUM A 501 source : AC1 13) chain A residue 303 type sequence R description binding site for residue TUM A 501 source : AC1 14) chain A residue 304 type sequence I description binding site for residue TUM A 501 source : AC1 15) chain A residue 31 type sequence A description binding site for residue PGW A 502 source : AC2 16) chain A residue 32 type sequence F description binding site for residue PGW A 502 source : AC2 17) chain A residue 35 type sequence H description binding site for residue PGW A 502 source : AC2 18) chain A residue 68 type sequence I description binding site for residue PGW A 502 source : AC2 19) chain B residue 107 type sequence C description binding site for residue PGW A 502 source : AC2 20) chain B residue 110 type sequence F description binding site for residue PGW A 502 source : AC2 21) chain B residue 111 type sequence L description binding site for residue PGW A 502 source : AC2 22) chain B residue 114 type sequence A description binding site for residue PGW A 502 source : AC2 23) chain B residue 124 type sequence H description binding site for residue PGW A 502 source : AC2 24) chain B residue 128 type sequence L description binding site for residue PGW A 502 source : AC2 25) chain A residue 107 type sequence C description binding site for residue PGW B 501 source : AC3 26) chain A residue 110 type sequence F description binding site for residue PGW B 501 source : AC3 27) chain A residue 114 type sequence A description binding site for residue PGW B 501 source : AC3 28) chain A residue 118 type sequence L description binding site for residue PGW B 501 source : AC3 29) chain A residue 124 type sequence H description binding site for residue PGW B 501 source : AC3 30) chain B residue 28 type sequence L description binding site for residue PGW B 501 source : AC3 31) chain B residue 31 type sequence A description binding site for residue PGW B 501 source : AC3 32) chain B residue 32 type sequence F description binding site for residue PGW B 501 source : AC3 33) chain B residue 35 type sequence H description binding site for residue PGW B 501 source : AC3 34) chain B residue 68 type sequence I description binding site for residue PGW B 501 source : AC3 35) chain B residue 71 type sequence F description binding site for residue PGW B 501 source : AC3 36) chain B residue 44 type sequence Q description binding site for residue TUM B 502 source : AC4 37) chain B residue 45 type sequence D description binding site for residue TUM B 502 source : AC4 38) chain B residue 46 type sequence L description binding site for residue TUM B 502 source : AC4 39) chain B residue 122 type sequence W description binding site for residue TUM B 502 source : AC4 40) chain B residue 125 type sequence K description binding site for residue TUM B 502 source : AC4 41) chain B residue 185 type sequence N description binding site for residue TUM B 502 source : AC4 42) chain B residue 186 type sequence I description binding site for residue TUM B 502 source : AC4 43) chain B residue 188 type sequence A description binding site for residue TUM B 502 source : AC4 44) chain B residue 189 type sequence G description binding site for residue TUM B 502 source : AC4 45) chain B residue 190 type sequence I description binding site for residue TUM B 502 source : AC4 46) chain B residue 191 type sequence N description binding site for residue TUM B 502 source : AC4 47) chain B residue 249 type sequence F description binding site for residue TUM B 502 source : AC4 48) chain B residue 252 type sequence D description binding site for residue TUM B 502 source : AC4 49) chain B residue 293 type sequence L description binding site for residue TUM B 502 source : AC4 50) chain B residue 302 type sequence H description binding site for residue TUM B 502 source : AC4 51) chain B residue 303 type sequence R description binding site for residue TUM B 502 source : AC4 52) chain B residue 304 type sequence I description binding site for residue TUM B 502 source : AC4 53) chain C residue 44 type sequence Q description binding site for residue TUM C 501 source : AC5 54) chain C residue 45 type sequence D description binding site for residue TUM C 501 source : AC5 55) chain C residue 46 type sequence L description binding site for residue TUM C 501 source : AC5 56) chain C residue 122 type sequence W description binding site for residue TUM C 501 source : AC5 57) chain C residue 185 type sequence N description binding site for residue TUM C 501 source : AC5 58) chain C residue 186 type sequence I description binding site for residue TUM C 501 source : AC5 59) chain C residue 188 type sequence A description binding site for residue TUM C 501 source : AC5 60) chain C residue 189 type sequence G description binding site for residue TUM C 501 source : AC5 61) chain C residue 190 type sequence I description binding site for residue TUM C 501 source : AC5 62) chain C residue 191 type sequence N description binding site for residue TUM C 501 source : AC5 63) chain C residue 249 type sequence F description binding site for residue TUM C 501 source : AC5 64) chain C residue 252 type sequence D description binding site for residue TUM C 501 source : AC5 65) chain C residue 293 type sequence L description binding site for residue TUM C 501 source : AC5 66) chain C residue 301 type sequence R description binding site for residue TUM C 501 source : AC5 67) chain C residue 302 type sequence H description binding site for residue TUM C 501 source : AC5 68) chain C residue 303 type sequence R description binding site for residue TUM C 501 source : AC5 69) chain C residue 304 type sequence I description binding site for residue TUM C 501 source : AC5 70) chain C residue 107 type sequence C description binding site for residue PGW C 502 source : AC6 71) chain C residue 110 type sequence F description binding site for residue PGW C 502 source : AC6 72) chain C residue 114 type sequence A description binding site for residue PGW C 502 source : AC6 73) chain C residue 118 type sequence L description binding site for residue PGW C 502 source : AC6 74) chain C residue 124 type sequence H description binding site for residue PGW C 502 source : AC6 75) chain D residue 28 type sequence L description binding site for residue PGW C 502 source : AC6 76) chain D residue 31 type sequence A description binding site for residue PGW C 502 source : AC6 77) chain D residue 32 type sequence F description binding site for residue PGW C 502 source : AC6 78) chain D residue 35 type sequence H description binding site for residue PGW C 502 source : AC6 79) chain D residue 64 type sequence A description binding site for residue PGW C 502 source : AC6 80) chain D residue 68 type sequence I description binding site for residue PGW C 502 source : AC6 81) chain D residue 71 type sequence F description binding site for residue PGW C 502 source : AC6 82) chain C residue 28 type sequence L description binding site for residue PGW C 503 source : AC7 83) chain C residue 31 type sequence A description binding site for residue PGW C 503 source : AC7 84) chain C residue 32 type sequence F description binding site for residue PGW C 503 source : AC7 85) chain C residue 35 type sequence H description binding site for residue PGW C 503 source : AC7 86) chain C residue 68 type sequence I description binding site for residue PGW C 503 source : AC7 87) chain C residue 71 type sequence F description binding site for residue PGW C 503 source : AC7 88) chain D residue 107 type sequence C description binding site for residue PGW C 503 source : AC7 89) chain D residue 110 type sequence F description binding site for residue PGW C 503 source : AC7 90) chain D residue 111 type sequence L description binding site for residue PGW C 503 source : AC7 91) chain D residue 114 type sequence A description binding site for residue PGW C 503 source : AC7 92) chain D residue 118 type sequence L description binding site for residue PGW C 503 source : AC7 93) chain D residue 124 type sequence H description binding site for residue PGW C 503 source : AC7 94) chain D residue 127 type sequence L description binding site for residue PGW C 503 source : AC7 95) chain D residue 44 type sequence Q description binding site for residue TUM D 501 source : AC8 96) chain D residue 45 type sequence D description binding site for residue TUM D 501 source : AC8 97) chain D residue 46 type sequence L description binding site for residue TUM D 501 source : AC8 98) chain D residue 122 type sequence W description binding site for residue TUM D 501 source : AC8 99) chain D residue 125 type sequence K description binding site for residue TUM D 501 source : AC8 100) chain D residue 185 type sequence N description binding site for residue TUM D 501 source : AC8 101) chain D residue 186 type sequence I description binding site for residue TUM D 501 source : AC8 102) chain D residue 188 type sequence A description binding site for residue TUM D 501 source : AC8 103) chain D residue 189 type sequence G description binding site for residue TUM D 501 source : AC8 104) chain D residue 190 type sequence I description binding site for residue TUM D 501 source : AC8 105) chain D residue 191 type sequence N description binding site for residue TUM D 501 source : AC8 106) chain D residue 249 type sequence F description binding site for residue TUM D 501 source : AC8 107) chain D residue 252 type sequence D description binding site for residue TUM D 501 source : AC8 108) chain D residue 293 type sequence L description binding site for residue TUM D 501 source : AC8 109) chain D residue 301 type sequence R description binding site for residue TUM D 501 source : AC8 110) chain D residue 302 type sequence H description binding site for residue TUM D 501 source : AC8 111) chain D residue 303 type sequence R description binding site for residue TUM D 501 source : AC8 112) chain D residue 304 type sequence I description binding site for residue TUM D 501 source : AC8 113) chain A residue 44 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:30388443 source Swiss-Prot : SWS_FT_FI13 114) chain C residue 56 type BINDING sequence E description BINDING => ECO:0000269|PubMed:30388443 source Swiss-Prot : SWS_FT_FI13 115) chain C residue 191 type BINDING sequence N description BINDING => ECO:0000269|PubMed:30388443 source Swiss-Prot : SWS_FT_FI13 116) chain C residue 301 type BINDING sequence R description BINDING => ECO:0000269|PubMed:30388443 source Swiss-Prot : SWS_FT_FI13 117) chain D residue 44 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:30388443 source Swiss-Prot : SWS_FT_FI13 118) chain D residue 56 type BINDING sequence E description BINDING => ECO:0000269|PubMed:30388443 source Swiss-Prot : SWS_FT_FI13 119) chain D residue 191 type BINDING sequence N description BINDING => ECO:0000269|PubMed:30388443 source Swiss-Prot : SWS_FT_FI13 120) chain D residue 301 type BINDING sequence R description BINDING => ECO:0000269|PubMed:30388443 source Swiss-Prot : SWS_FT_FI13 121) chain A residue 56 type BINDING sequence E description BINDING => ECO:0000269|PubMed:30388443 source Swiss-Prot : SWS_FT_FI13 122) chain A residue 191 type BINDING sequence N description BINDING => ECO:0000269|PubMed:30388443 source Swiss-Prot : SWS_FT_FI13 123) chain A residue 301 type BINDING sequence R description BINDING => ECO:0000269|PubMed:30388443 source Swiss-Prot : SWS_FT_FI13 124) chain B residue 44 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:30388443 source Swiss-Prot : SWS_FT_FI13 125) chain B residue 56 type BINDING sequence E description BINDING => ECO:0000269|PubMed:30388443 source Swiss-Prot : SWS_FT_FI13 126) chain B residue 191 type BINDING sequence N description BINDING => ECO:0000269|PubMed:30388443 source Swiss-Prot : SWS_FT_FI13 127) chain B residue 301 type BINDING sequence R description BINDING => ECO:0000269|PubMed:30388443 source Swiss-Prot : SWS_FT_FI13 128) chain C residue 44 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:30388443 source Swiss-Prot : SWS_FT_FI13 129) 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 130) 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 131) 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 132) 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 133) 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 134) 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 135) 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 136) 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 137) chain B residue 214-218 type TOPO_DOM sequence EGDCR description Lumenal => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI1 138) chain B residue 270-271 type TOPO_DOM sequence HF description Lumenal => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI1 139) chain C residue 79-91 type TOPO_DOM sequence LNCAFP description Lumenal => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI1 140) chain C residue 144-166 type TOPO_DOM sequence FGNTTIVHLDLG description Lumenal => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI1 141) chain C residue 214-218 type TOPO_DOM sequence EGDCR description Lumenal => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI1 142) chain C residue 270-271 type TOPO_DOM sequence HF description Lumenal => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI1 143) chain A residue 79-91 type TOPO_DOM sequence LNCAFP 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 FGNTTIVVHLDLG 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 144-166 type TOPO_DOM sequence FGNTTIVVHLDLG description Lumenal => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI1 149) chain A residue 214-218 type TOPO_DOM sequence EGDCR description Lumenal => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI1 150) chain A residue 270-271 type TOPO_DOM sequence HF description Lumenal => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI1 151) chain B residue 79-91 type TOPO_DOM sequence LNCCKAFP description Lumenal => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI1 152) chain B residue 144-166 type TOPO_DOM sequence FGNTTIVVHLDLG description Lumenal => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI1 153) chain A residue 251-269 type TRANSMEM sequence GDTFCYFAGMTFAVVGILG description Helical; Name=Helix 8 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI10 154) chain B residue 251-269 type TRANSMEM sequence GDTFCYFAGMTFAVVGILG description Helical; Name=Helix 8 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI10 155) chain C residue 251-269 type TRANSMEM sequence GDTFCYFAGMTFAVVGILG description Helical; Name=Helix 8 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI10 156) chain D residue 251-269 type TRANSMEM sequence GDTFCYFAGMTFAVVGILG description Helical; Name=Helix 8 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI10 157) chain A residue 272-293 type TRANSMEM sequence SKTMLLFFMPQVFNFLYSLPQL description Helical; Name=Helix 9 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI11 158) chain B residue 272-293 type TRANSMEM sequence SKTMLLFFMPQVFNFLYSLPQL description Helical; Name=Helix 9 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI11 159) chain C residue 272-293 type TRANSMEM sequence SKTMLLFFMPQVFNFLYSLPQL description Helical; Name=Helix 9 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI11 160) chain D residue 272-293 type TRANSMEM sequence SKTMLLFFMPQVFNFLYSLPQL description Helical; Name=Helix 9 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI11 161) chain B residue 376-400 type TRANSMEM sequence ERNLTLLLLLLQILGSAITFSIRYQ description Helical; Name=Helix 10 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI12 162) chain C residue 376-400 type TRANSMEM sequence ERNLTLLLLLLQILGSAITFSIRYQ description Helical; Name=Helix 10 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI12 163) chain D residue 376-400 type TRANSMEM sequence ERNLTLLLLLLQILGSAITFSIRYQ description Helical; Name=Helix 10 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI12 164) chain A residue 119 type BINDING sequence N description BINDING => ECO:0000269|PubMed:29459785, ECO:0007744|PDB:6BW5 source Swiss-Prot : SWS_FT_FI15 165) chain A residue 252 type BINDING sequence D description BINDING => ECO:0000269|PubMed:29459785, ECO:0007744|PDB:6BW5 source Swiss-Prot : SWS_FT_FI15 166) chain B residue 119 type BINDING sequence N description BINDING => ECO:0000269|PubMed:29459785, ECO:0007744|PDB:6BW5 source Swiss-Prot : SWS_FT_FI15 167) chain B residue 252 type BINDING sequence D description BINDING => ECO:0000269|PubMed:29459785, ECO:0007744|PDB:6BW5 source Swiss-Prot : SWS_FT_FI15 168) chain C residue 119 type BINDING sequence N description BINDING => ECO:0000269|PubMed:29459785, ECO:0007744|PDB:6BW5 source Swiss-Prot : SWS_FT_FI15 169) chain C residue 252 type BINDING sequence D description BINDING => ECO:0000269|PubMed:29459785, ECO:0007744|PDB:6BW5 source Swiss-Prot : SWS_FT_FI15 170) chain D residue 119 type BINDING sequence N description BINDING => ECO:0000269|PubMed:29459785, ECO:0007744|PDB:6BW5 source Swiss-Prot : SWS_FT_FI15 171) chain D residue 252 type BINDING sequence D description BINDING => ECO:0000269|PubMed:29459785, ECO:0007744|PDB:6BW5 source Swiss-Prot : SWS_FT_FI15 172) chain A residue 125 type BINDING sequence K description BINDING => ECO:0000305|PubMed:30388443 source Swiss-Prot : SWS_FT_FI16 173) chain A residue 178 type BINDING sequence V description BINDING => ECO:0000305|PubMed:30388443 source Swiss-Prot : SWS_FT_FI16 174) chain B residue 125 type BINDING sequence K description BINDING => ECO:0000305|PubMed:30388443 source Swiss-Prot : SWS_FT_FI16 175) chain B residue 178 type BINDING sequence V description BINDING => ECO:0000305|PubMed:30388443 source Swiss-Prot : SWS_FT_FI16 176) chain C residue 125 type BINDING sequence K description BINDING => ECO:0000305|PubMed:30388443 source Swiss-Prot : SWS_FT_FI16 177) chain C residue 178 type BINDING sequence V description BINDING => ECO:0000305|PubMed:30388443 source Swiss-Prot : SWS_FT_FI16 178) chain D residue 125 type BINDING sequence K description BINDING => ECO:0000305|PubMed:30388443 source Swiss-Prot : SWS_FT_FI16 179) chain D residue 178 type BINDING sequence V description BINDING => ECO:0000305|PubMed:30388443 source Swiss-Prot : SWS_FT_FI16 180) chain A residue 59-78 type TRANSMEM sequence GVISGAVFLIILFCFIPFPF description Helical; Name=Helix 2 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI4 181) chain B residue 59-78 type TRANSMEM sequence GVISGAVFLIILFCFIPFPF description Helical; Name=Helix 2 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI4 182) chain C residue 59-78 type TRANSMEM sequence GVISGAVFLIILFCFIPFPF description Helical; Name=Helix 2 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI4 183) chain D residue 59-78 type TRANSMEM sequence GVISGAVFLIILFCFIPFPF description Helical; Name=Helix 2 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI4 184) chain A residue 146 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI18 185) chain B residue 146 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI18 186) chain C residue 146 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI18 187) chain D residue 146 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI18 188) chain A residue 11-38 type TRANSMEM sequence LLINLIVSLLGFVATVTLIPAFRGHFIA description Helical; Name=Helix 1 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI2 189) chain B residue 11-38 type TRANSMEM sequence LLINLIVSLLGFVATVTLIPAFRGHFIA description Helical; Name=Helix 1 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI2 190) chain C residue 11-38 type TRANSMEM sequence LLINLIVSLLGFVATVTLIPAFRGHFIA description Helical; Name=Helix 1 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI2 191) chain D residue 11-38 type TRANSMEM sequence LLINLIVSLLGFVATVTLIPAFRGHFIA description Helical; Name=Helix 1 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI2 192) chain A residue 39-58 type TOPO_DOM sequence ARLCGQDLNKTSRQQIPESQ description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 193) chain B residue 294-375 type TOPO_DOM sequence LHIIPCPRHRIPRLNIKTGKLEMSYSKFKTKSLSFLGTFI LKVAESLQLVTVHQFTECNNMTLINLLLKVLGPIH description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 194) chain C residue 39-58 type TOPO_DOM sequence ARLCGQDLNKTSRQQIPESQ description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 195) chain C residue 119-121 type TOPO_DOM sequence NLR description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 196) chain C residue 187-192 type TOPO_DOM sequence LAGING description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 197) chain C residue 243-250 type TOPO_DOM sequence WYPSRVFV description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 198) chain C residue 294-375 type TOPO_DOM sequence LHIIPCPRHRIPRLNIKTGKLEMSYSKFKTKSLSFLGTFI LKVAESLQLVTVHQCNNMTLINLLLKVLGPIH description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 199) chain D residue 39-58 type TOPO_DOM sequence ARLCGQDLNKTSRQQIPESQ description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 200) chain D residue 119-121 type TOPO_DOM sequence NLR description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 201) chain D residue 187-192 type TOPO_DOM sequence LAGING description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 202) chain D residue 243-250 type TOPO_DOM sequence WYPSRVFV description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 203) chain A residue 119-121 type TOPO_DOM sequence NLR description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 204) chain D residue 294-375 type TOPO_DOM sequence LHIIPCPRHRIPRLNIKTGKLEMSYSKFKTKSLSFLGTFI LKVAESLQLVTVHQTECNNMTLINLLLKVLGPIH description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 205) chain A residue 187-192 type TOPO_DOM sequence LAGING description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 206) chain A residue 243-250 type TOPO_DOM sequence WYPSRVFV description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 207) chain A residue 294-375 type TOPO_DOM sequence LHIIPCPRHRIPRLNIKTGKLEMSYSKFKTKSLSFLGTFI LKVAESLQLVTVHQFTECNNMTLINLLLKVLGPIH description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 208) chain B residue 39-58 type TOPO_DOM sequence ARLCGQDLNKTSRQQIPESQ description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 209) chain B residue 119-121 type TOPO_DOM sequence NLR description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 210) chain B residue 187-192 type TOPO_DOM sequence LAGING description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 211) chain B residue 243-250 type TOPO_DOM sequence WYPSRVFV description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 212) chain A residue 92-118 type TRANSMEM sequence HHEFVALIGALLAICCMIFLGFADDVL description Helical; Name=Helix 3 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI5 213) chain B residue 92-118 type TRANSMEM sequence HHEFVALIGALLAICCMIFLGFADDVL description Helical; Name=Helix 3 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI5 214) chain C residue 92-118 type TRANSMEM sequence HHEFVALIGALLAICCMIFLGFADDVL description Helical; Name=Helix 3 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI5 215) chain D residue 92-118 type TRANSMEM sequence HHEFVALIGALLAICCMIFLGFADDVL description Helical; Name=Helix 3 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI5 216) chain A residue 122-143 type TRANSMEM sequence WRHKLLLHTAASLPLLMVYFTN description Helical; Name=Helix 4 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI6 217) chain B residue 122-143 type TRANSMEM sequence WRHKLLLHTAASLPLLMVYFTN description Helical; Name=Helix 4 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI6 218) chain C residue 122-143 type TRANSMEM sequence WRHKLLLHTAASLPLLMVYFTN description Helical; Name=Helix 4 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI6 219) chain D residue 122-143 type TRANSMEM sequence WRHKLLLHTAASLPLLMVYFTN description Helical; Name=Helix 4 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI6 220) chain A residue 167-186 type TRANSMEM sequence ILYYVYMGLLAVFCTNAINI description Helical; Name=Helix 5 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI7 221) chain B residue 167-186 type TRANSMEM sequence ILYYVYMGLLAVFCTNAINI description Helical; Name=Helix 5 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI7 222) chain C residue 167-186 type TRANSMEM sequence ILYYVYMGLLAVFCTNAINI description Helical; Name=Helix 5 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI7 223) chain D residue 167-186 type TRANSMEM sequence ILYYVYMGLLAVFCTNAINI description Helical; Name=Helix 5 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI7 224) chain A residue 193-213 type TRANSMEM sequence LEAGQSLVISASIIVFNLVEL description Helical; Name=Helix 6 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI8 225) chain B residue 193-213 type TRANSMEM sequence LEAGQSLVISASIIVFNLVEL description Helical; Name=Helix 6 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI8 226) chain C residue 193-213 type TRANSMEM sequence LEAGQSLVISASIIVFNLVEL description Helical; Name=Helix 6 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI8 227) chain D residue 193-213 type TRANSMEM sequence LEAGQSLVISASIIVFNLVEL description Helical; Name=Helix 6 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI8 228) chain A residue 219-242 type TRANSMEM sequence DDHVFSLYFMIPFFFTTLGLLYHN description Helical; Name=Helix 7 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI9 229) chain B residue 219-242 type TRANSMEM sequence DDHVFSLYFMIPFFFTTLGLLYHN description Helical; Name=Helix 7 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI9 230) chain C residue 219-242 type TRANSMEM sequence DDHVFSLYFMIPFFFTTLGLLYHN description Helical; Name=Helix 7 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI9 231) chain D residue 219-242 type TRANSMEM sequence DDHVFSLYFMIPFFFTTLGLLYHN description Helical; Name=Helix 7 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI9 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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