eF-site ID 6bw6-D PDB Code 6bw6 Chain 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 D:  PMPLLINLIVSLLGFVATVTLIPAFRGHFIAARLCGQDLN KTSRQQIPESQGVISGAVFLIILFCFIPFPFLNCAFPHHE FVALIGALLAICCMIFLGFADDVLNLRWRHKLLLHTAASL PLLMVYFTNFGNTTIVVHLDLGILYYVYMGLLAVFCTNAI NILAGINGLEAGQSLVISASIIVFNLVELEGDCRDDHVFS LYFMIPFFFTTLGLLYHNWYPSRVFVGDTFCYFAGMTFAV VGILGHFSKTMLLFFMPQVFNFLYSLPQLLHIIPCPRHRI PRLNIKTGKLEMSYSKFKTKSLSFLGTFILKVAESLQLVT VHQTECNNMTLINLLLKVLGPIHERNLTLLLLLLQILGSA ITFSIRYQL Description Functional site 1) chain D residue 28 type sequence L description binding site for residue PGW C 502 source : AC6 2) chain D residue 31 type sequence A description binding site for residue PGW C 502 source : AC6 3) chain D residue 32 type sequence F description binding site for residue PGW C 502 source : AC6 4) chain D residue 35 type sequence H description binding site for residue PGW C 502 source : AC6 5) chain D residue 64 type sequence A description binding site for residue PGW C 502 source : AC6 6) chain D residue 68 type sequence I description binding site for residue PGW C 502 source : AC6 7) chain D residue 71 type sequence F description binding site for residue PGW C 502 source : AC6 8) chain D residue 107 type sequence C description binding site for residue PGW C 503 source : AC7 9) chain D residue 110 type sequence F description binding site for residue PGW C 503 source : AC7 10) chain D residue 111 type sequence L description binding site for residue PGW C 503 source : AC7 11) chain D residue 114 type sequence A description binding site for residue PGW C 503 source : AC7 12) chain D residue 118 type sequence L description binding site for residue PGW C 503 source : AC7 13) chain D residue 124 type sequence H description binding site for residue PGW C 503 source : AC7 14) chain D residue 127 type sequence L description binding site for residue PGW C 503 source : AC7 15) chain D residue 44 type sequence Q description binding site for residue TUM D 501 source : AC8 16) chain D residue 45 type sequence D description binding site for residue TUM D 501 source : AC8 17) chain D residue 46 type sequence L description binding site for residue TUM D 501 source : AC8 18) chain D residue 122 type sequence W description binding site for residue TUM D 501 source : AC8 19) chain D residue 125 type sequence K description binding site for residue TUM D 501 source : AC8 20) chain D residue 185 type sequence N description binding site for residue TUM D 501 source : AC8 21) chain D residue 186 type sequence I description binding site for residue TUM D 501 source : AC8 22) chain D residue 188 type sequence A description binding site for residue TUM D 501 source : AC8 23) chain D residue 189 type sequence G description binding site for residue TUM D 501 source : AC8 24) chain D residue 190 type sequence I description binding site for residue TUM D 501 source : AC8 25) chain D residue 191 type sequence N description binding site for residue TUM D 501 source : AC8 26) chain D residue 249 type sequence F description binding site for residue TUM D 501 source : AC8 27) chain D residue 252 type sequence D description binding site for residue TUM D 501 source : AC8 28) chain D residue 293 type sequence L description binding site for residue TUM D 501 source : AC8 29) chain D residue 301 type sequence R description binding site for residue TUM D 501 source : AC8 30) chain D residue 302 type sequence H description binding site for residue TUM D 501 source : AC8 31) chain D residue 303 type sequence R description binding site for residue TUM D 501 source : AC8 32) chain D residue 304 type sequence I description binding site for residue TUM D 501 source : AC8 33) 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 34) 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 35) chain D residue 125 type BINDING sequence K description BINDING => ECO:0000305|PubMed:30388443 source Swiss-Prot : SWS_FT_FI16 36) chain D residue 178 type BINDING sequence V description BINDING => ECO:0000305|PubMed:30388443 source Swiss-Prot : SWS_FT_FI16 37) chain D residue 146 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI18 38) chain D residue 79-91 type TOPO_DOM sequence LNCAFP description Lumenal => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI1 39) chain D residue 144-166 type TOPO_DOM sequence FGNTTIVVHLDLG description Lumenal => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI1 40) chain D residue 214-218 type TOPO_DOM sequence EGDCR description Lumenal => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI1 41) chain D residue 270-271 type TOPO_DOM sequence HF description Lumenal => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI1 42) chain D residue 11-38 type TRANSMEM sequence LLINLIVSLLGFVATVTLIPAFRGHFIA description Helical; Name=Helix 1 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI2 43) chain D residue 39-58 type TOPO_DOM sequence ARLCGQDLNKTSRQQIPESQ description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 44) chain D residue 119-121 type TOPO_DOM sequence NLR description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 45) chain D residue 187-192 type TOPO_DOM sequence LAGING description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 46) chain D residue 243-250 type TOPO_DOM sequence WYPSRVFV description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 47) chain D residue 294-375 type TOPO_DOM sequence LHIIPCPRHRIPRLNIKTGKLEMSYSKFKTKSLSFLGTFI LKVAESLQLVTVHQTECNNMTLINLLLKVLGPIH description Cytoplasmic => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI3 48) chain D residue 59-78 type TRANSMEM sequence GVISGAVFLIILFCFIPFPF description Helical; Name=Helix 2 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI4 49) chain D residue 92-118 type TRANSMEM sequence HHEFVALIGALLAICCMIFLGFADDVL description Helical; Name=Helix 3 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI5 50) chain D residue 122-143 type TRANSMEM sequence WRHKLLLHTAASLPLLMVYFTN description Helical; Name=Helix 4 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI6 51) chain D residue 167-186 type TRANSMEM sequence ILYYVYMGLLAVFCTNAINI description Helical; Name=Helix 5 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI7 52) chain D residue 193-213 type TRANSMEM sequence LEAGQSLVISASIIVFNLVEL description Helical; Name=Helix 6 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI8 53) chain D residue 219-242 type TRANSMEM sequence DDHVFSLYFMIPFFFTTLGLLYHN description Helical; Name=Helix 7 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI9 54) chain D residue 251-269 type TRANSMEM sequence GDTFCYFAGMTFAVVGILG description Helical; Name=Helix 8 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI10 55) chain D residue 272-293 type TRANSMEM sequence SKTMLLFFMPQVFNFLYSLPQL description Helical; Name=Helix 9 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI11 56) chain D residue 376-400 type TRANSMEM sequence ERNLTLLLLLLQILGSAITFSIRYQ description Helical; Name=Helix 10 => ECO:0000269|PubMed:29459785 source Swiss-Prot : SWS_FT_FI12 57) chain D residue 44 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:30388443 source Swiss-Prot : SWS_FT_FI13 58) chain D residue 56 type BINDING sequence E description BINDING => ECO:0000269|PubMed:30388443 source Swiss-Prot : SWS_FT_FI13 59) chain D residue 191 type BINDING sequence N description BINDING => ECO:0000269|PubMed:30388443 source Swiss-Prot : SWS_FT_FI13 60) chain D residue 301 type BINDING sequence R description BINDING => ECO:0000269|PubMed:30388443 source Swiss-Prot : SWS_FT_FI13 61) chain D residue 119 type BINDING sequence N description BINDING => ECO:0000269|PubMed:29459785, ECO:0007744|PDB:6BW5 source Swiss-Prot : SWS_FT_FI15 62) chain D residue 252 type BINDING sequence D description BINDING => ECO:0000269|PubMed:29459785, ECO:0007744|PDB:6BW5 source Swiss-Prot : SWS_FT_FI15 63) chain D residue 185 type BINDING sequence N description BINDING => ECO:0000269|PubMed:29459785, ECO:0007744|PDB:6BW6 source Swiss-Prot : SWS_FT_FI17

Display surface Download Links