eF-site ID 5zkq-B PDB Code 5zkq Chain B click to enlarge Title Crystal structure of the human platelet-activating factor receptor in complex with ABT-491 Classification SIGNALING PROTEIN Compound Platelet-activating factor receptor,Endolysin,Endolysin,Platelet-activating factor receptor Source (PTAFR_HUMAN) Sequence B:  SHMDSEFRYTLFPIVYSIIFVLGVIANGYVLWVFARLYPF NEIKIFMVNLTMADMLFLITLPLWIVYYQNQGNWILPKFL CNVAGCLFFINTYCSVAFLGVITYNRYQAVTRPIQANTRK RGISLSLVIWVAIVGAASYFLILDSTNTVPDSAGSGDVTR CFEHYEKGSVPVLIIHIFIVFSFFLVFLIILFCNLVIIRT LLMQPVNIFEMLRIDEGGGSGGDEEKLFNQDVDAAVRGIL RNAKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSLR MLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWD AYAEVKRRDLWMACTVLAVFIICFVPHHVVQLPWTLAELG FQDSKFHQAINDAHQVTLCLLSTNCVLNPVIYCFLTKKF Description Functional site 1) chain B residue 22 type sequence Y description binding site for residue 9EU B 1201 source : AC7 2) chain B residue 73 type sequence W description binding site for residue 9EU B 1201 source : AC7 3) chain B residue 77 type sequence Y description binding site for residue 9EU B 1201 source : AC7 4) chain B residue 94 type sequence G description binding site for residue 9EU B 1201 source : AC7 5) chain B residue 97 type sequence F description binding site for residue 9EU B 1201 source : AC7 6) chain B residue 98 type sequence F description binding site for residue 9EU B 1201 source : AC7 7) chain B residue 152 type sequence F description binding site for residue 9EU B 1201 source : AC7 8) chain B residue 173 type sequence C description binding site for residue 9EU B 1201 source : AC7 9) chain B residue 174 type sequence F description binding site for residue 9EU B 1201 source : AC7 10) chain B residue 175 type sequence E description binding site for residue 9EU B 1201 source : AC7 11) chain B residue 177 type sequence Y description binding site for residue 9EU B 1201 source : AC7 12) chain B residue 188 type sequence H description binding site for residue 9EU B 1201 source : AC7 13) chain B residue 191 type sequence I description binding site for residue 9EU B 1201 source : AC7 14) chain B residue 248 type sequence H description binding site for residue 9EU B 1201 source : AC7 15) chain B residue 252 type sequence Q description binding site for residue 9EU B 1201 source : AC7 16) chain B residue 181 type sequence S description binding site for residue OLC B 1202 source : AC8 17) chain B residue 183 type sequence P description binding site for residue OLC B 1202 source : AC8 18) chain B residue 184 type sequence V description binding site for residue OLC B 1202 source : AC8 19) chain B residue 151 type sequence Y description binding site for residue OLC B 1203 source : AC9 20) chain B residue 58 type sequence N description binding site for residue OLC B 1204 source : AD1 21) chain B residue 61 type sequence M description binding site for residue OLC B 1204 source : AD1 22) chain B residue 131 type sequence R description binding site for residue OLC B 1204 source : AD1 23) chain B residue 135 type sequence I description binding site for residue OLC B 1204 source : AD1 24) chain B residue 139 type sequence L description binding site for residue OLC B 1204 source : AD1 25) chain B residue 142 type sequence W description binding site for residue OLC B 1204 source : AD1 26) chain B residue 8 type sequence H description binding site for residue ZN B 1205 source : AD2 27) chain B residue 259 type sequence E description binding site for residue ZN B 1205 source : AD2 28) chain B residue 268 type sequence H description binding site for residue ZN B 1205 source : AD2 29) chain B residue 272 type sequence N description binding site for residue ZN B 1205 source : AD2 30) chain B residue 1062 type sequence M description binding site for residue SO4 B 1206 source : AD3 31) chain B residue 166 type sequence G description binding site for residue SO4 B 1207 source : AD4 32) chain B residue 1032 type sequence R description binding site for residue SO4 B 1207 source : AD4 33) chain B residue 1036 type sequence R description binding site for residue SO4 B 1207 source : AD4 34) chain B residue 1075 type sequence R description binding site for residue SO4 B 1208 source : AD5 35) chain B residue 1081 type sequence R description binding site for residue SO4 B 1208 source : AD5 36) chain B residue 1069 type sequence G description binding site for residue SO4 B 1209 source : AD6 37) chain B residue 1098 type sequence T description binding site for residue SO4 B 1210 source : AD7 38) chain B residue 1099 type sequence P description binding site for residue SO4 B 1210 source : AD7 39) chain B residue 1100 type sequence N description binding site for residue SO4 B 1210 source : AD7 40) chain B residue 1101 type sequence R description binding site for residue SO4 B 1210 source : AD7 41) chain B residue 1066 type sequence G description binding site for residue SO4 B 1211 source : AD8 42) chain B residue 1010 type catalytic sequence E description 921 source MCSA : MCSA2 43) chain B residue 169 type CARBOHYD sequence D description N-linked (GlcNAc...) asparagine => ECO:0000255 source Swiss-Prot : SWS_FT_FI10 44) chain B residue 1060 type BINDING sequence F description BINDING => ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI12 45) chain B residue 1073 type BINDING sequence S description BINDING => ECO:0000303|PubMed:7831309 source Swiss-Prot : SWS_FT_FI13 46) chain B residue 1088 type BINDING sequence N description BINDING => ECO:0000303|PubMed:7831309 source Swiss-Prot : SWS_FT_FI13 47) chain B residue 1010 type ACT_SITE sequence E description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI11 48) chain B residue 39-54 type TOPO_DOM sequence VFARLYPFNEIKI description Cytoplasmic => ECO:0000255 source Swiss-Prot : SWS_FT_FI2 49) chain B residue 114-133 type TOPO_DOM sequence NRYQAVTRPIQANTRKR description Cytoplasmic => ECO:0000255 source Swiss-Prot : SWS_FT_FI2 50) chain B residue 55-74 type TRANSMEM sequence FMVNLTMADMLFLITLPLWI description Helical; Name=2 => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 51) chain B residue 75-91 type TOPO_DOM sequence VYYQNQGNWILPKFLCN description Extracellular => ECO:0000255 source Swiss-Prot : SWS_FT_FI4 52) chain B residue 156-184 type TOPO_DOM sequence DSTNTVPDSAGSGDVTRCFEHYEKGSVPV description Extracellular => ECO:0000255 source Swiss-Prot : SWS_FT_FI4 53) chain B residue 255-276 type TOPO_DOM sequence WTLAELGFQDSKFHQAINDAHQ description Extracellular => ECO:0000255 source Swiss-Prot : SWS_FT_FI4 54) chain B residue 92-113 type TRANSMEM sequence VAGCLFFINTYCSVAFLGVITY description Helical; Name=3 => ECO:0000255 source Swiss-Prot : SWS_FT_FI5 55) chain B residue 134-155 type TRANSMEM sequence GISLSLVIWVAIVGAASYFLIL description Helical; Name=4 => ECO:0000255 source Swiss-Prot : SWS_FT_FI6 56) chain B residue 185-205 type TRANSMEM sequence LIIHIFIVFSFFLVFLIILFC description Helical; Name=5 => ECO:0000255 source Swiss-Prot : SWS_FT_FI7 57) chain B residue 234-254 type TRANSMEM sequence ACTVLAVFIICFVPHHVVQLP description Helical; Name=6 => ECO:0000255 source Swiss-Prot : SWS_FT_FI8 58) chain B residue 277-296 type TRANSMEM sequence VTLCLLSTNCVLNPVIYCFL description Helical; Name=7 => ECO:0000255 source Swiss-Prot : SWS_FT_FI9 59) chain B residue 17-38 type TRANSMEM sequence LFPIVYSIIFVLGVIANGYVLW description Helical; Name=1 => ECO:0000255 source Swiss-Prot : SWS_FT_FI1

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