eF-site ID 6bw6-A PDB Code 6bw6 Chain A 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 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 A residue 107 type sequence C description binding site for residue PGW B 501 source : AC3 20) chain A residue 110 type sequence F description binding site for residue PGW B 501 source : AC3 21) chain A residue 114 type sequence A description binding site for residue PGW B 501 source : AC3 22) chain A residue 118 type sequence L description binding site for residue PGW B 501 source : AC3 23) chain A residue 124 type sequence H description binding site for residue PGW B 501 source : AC3 24) chain A residue 44 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:30388443 source Swiss-Prot : SWS_FT_FI13 25) chain A residue 56 type BINDING sequence E description BINDING => ECO:0000269|PubMed:30388443 source Swiss-Prot : SWS_FT_FI13 26) chain A residue 191 type BINDING sequence N description BINDING => ECO:0000269|PubMed:30388443 source Swiss-Prot : SWS_FT_FI13 27) chain A residue 301 type BINDING sequence R description BINDING => ECO:0000269|PubMed:30388443 source Swiss-Prot : SWS_FT_FI13 28) 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 29) 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 30) chain A residue 79-91 type TOPO_DOM sequence LNCAFP description Lumenal => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI1 31) chain A residue 144-166 type TOPO_DOM sequence FGNTTIVVHLDLG description Lumenal => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI1 32) chain A residue 214-218 type TOPO_DOM sequence EGDCR description Lumenal => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI1 33) chain A residue 270-271 type TOPO_DOM sequence HF description Lumenal => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI1 34) chain A residue 251-269 type TRANSMEM sequence GDTFCYFAGMTFAVVGILG description Helical; Name=Helix 8 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI10 35) chain A residue 272-293 type TRANSMEM sequence SKTMLLFFMPQVFNFLYSLPQL description Helical; Name=Helix 9 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI11 36) chain A residue 119 type BINDING sequence N description BINDING => ECO:0000269|PubMed:29459785, ECO:0007744|PDB:6BW5 source Swiss-Prot : SWS_FT_FI15 37) chain A residue 252 type BINDING sequence D description BINDING => ECO:0000269|PubMed:29459785, ECO:0007744|PDB:6BW5 source Swiss-Prot : SWS_FT_FI15 38) chain A residue 125 type BINDING sequence K description BINDING => ECO:0000305|PubMed:30388443 source Swiss-Prot : SWS_FT_FI16 39) chain A residue 178 type BINDING sequence V description BINDING => ECO:0000305|PubMed:30388443 source Swiss-Prot : SWS_FT_FI16 40) chain A residue 59-78 type TRANSMEM sequence GVISGAVFLIILFCFIPFPF description Helical; Name=Helix 2 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI4 41) chain A residue 146 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI18 42) chain A residue 11-38 type TRANSMEM sequence LLINLIVSLLGFVATVTLIPAFRGHFIA description Helical; Name=Helix 1 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI2 43) chain A residue 39-58 type TOPO_DOM sequence ARLCGQDLNKTSRQQIPESQ description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 44) chain A residue 119-121 type TOPO_DOM sequence NLR description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 45) chain A residue 187-192 type TOPO_DOM sequence LAGING description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 46) chain A residue 243-250 type TOPO_DOM sequence WYPSRVFV description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 47) chain A residue 294-375 type TOPO_DOM sequence LHIIPCPRHRIPRLNIKTGKLEMSYSKFKTKSLSFLGTFI LKVAESLQLVTVHQFTECNNMTLINLLLKVLGPIH description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 48) chain A residue 92-118 type TRANSMEM sequence HHEFVALIGALLAICCMIFLGFADDVL description Helical; Name=Helix 3 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI5 49) chain A residue 122-143 type TRANSMEM sequence WRHKLLLHTAASLPLLMVYFTN description Helical; Name=Helix 4 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI6 50) chain A residue 167-186 type TRANSMEM sequence ILYYVYMGLLAVFCTNAINI description Helical; Name=Helix 5 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI7 51) chain A residue 193-213 type TRANSMEM sequence LEAGQSLVISASIIVFNLVEL description Helical; Name=Helix 6 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI8 52) chain A residue 219-242 type TRANSMEM sequence DDHVFSLYFMIPFFFTTLGLLYHN description Helical; Name=Helix 7 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI9 53) chain A 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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