eF-site ID 4nc3-A PDB Code 4nc3 Chain A click to enlarge Title Crystal structure of the 5-HT2B receptor solved using serial femtosecond crystallography in lipidic cubic phase. Classification SIGNALING PROTEIN, ELECTRON TRANSPORT Compound Chimera protein of human 5-hydroxytryptamine receptor 2B and E. Coli soluble cytochrome b562 Source Homo sapiens (Human) (5HT2B_HUMAN) Sequence A:  EEQGNKLHWAALLILMVIIPTIGGNTLVILAVSLEKKLQY ATNYFLMSLAVADLLVGLFVMPIALLTIMFEAMWPLPLVL CPAWLFLDVLFSTASIWHLCAISVDRYIAIKKPIQANQYN SRATAFIKITVVWLISIGIAIPVPIKGIETVDNPNNITCV LTKERFGDFMLFGSLAAFFTPLAIMIVTYFLTIHALQKKA ADLEDNWETLNDNLKVIEKADNAAQVKDALTKMRAKDFRH GFDILVGQIDDALKLANEGKVKEAQAAAEQLKTTRNAYIQ KYLQTISNEQRASKVLGIVFFLFLLMWCPFFITNITLVLC DSCNQTTLQMLLEIFVWIGYVSSGVNPLVYTLFNKTFRDA FGRYITCNYR Description Functional site 1) chain A residue 62 type sequence L description BINDING SITE FOR RESIDUE PLM A 1201 source : AC1 2) chain A residue 353 type sequence C description BINDING SITE FOR RESIDUE PLM A 1201 source : AC1 3) chain A residue 395 type sequence I description BINDING SITE FOR RESIDUE PLM A 1201 source : AC1 4) chain A residue 396 type sequence T description BINDING SITE FOR RESIDUE PLM A 1201 source : AC1 5) chain A residue 397 type sequence C description BINDING SITE FOR RESIDUE PLM A 1201 source : AC1 6) chain A residue 135 type sequence D description BINDING SITE FOR RESIDUE ERM A 1202 source : AC2 7) chain A residue 139 type sequence S description BINDING SITE FOR RESIDUE ERM A 1202 source : AC2 8) chain A residue 140 type sequence T description BINDING SITE FOR RESIDUE ERM A 1202 source : AC2 9) chain A residue 208 type sequence V description BINDING SITE FOR RESIDUE ERM A 1202 source : AC2 10) chain A residue 209 type sequence L description BINDING SITE FOR RESIDUE ERM A 1202 source : AC2 11) chain A residue 217 type sequence F description BINDING SITE FOR RESIDUE ERM A 1202 source : AC2 12) chain A residue 218 type sequence M description BINDING SITE FOR RESIDUE ERM A 1202 source : AC2 13) chain A residue 225 type sequence A description BINDING SITE FOR RESIDUE ERM A 1202 source : AC2 14) chain A residue 340 type sequence F description BINDING SITE FOR RESIDUE ERM A 1202 source : AC2 15) chain A residue 344 type sequence N description BINDING SITE FOR RESIDUE ERM A 1202 source : AC2 16) chain A residue 359 type sequence Q description BINDING SITE FOR RESIDUE ERM A 1202 source : AC2 17) chain A residue 61 type sequence I description BINDING SITE FOR RESIDUE CLR A 1203 source : AC3 18) chain A residue 69 type sequence I description BINDING SITE FOR RESIDUE CLR A 1203 source : AC3 19) chain A residue 70 type sequence G description BINDING SITE FOR RESIDUE CLR A 1203 source : AC3 20) chain A residue 394 type sequence Y description BINDING SITE FOR RESIDUE CLR A 1203 source : AC3 21) chain A residue 399 type sequence Y description BINDING SITE FOR RESIDUE CLR A 1203 source : AC3 22) chain A residue 150 type sequence S description BINDING SITE FOR RESIDUE OLC A 1204 source : AC4 23) chain A residue 233 type sequence M description BINDING SITE FOR RESIDUE OLC A 1204 source : AC4 24) chain A residue 240 type sequence T description BINDING SITE FOR RESIDUE OLC A 1204 source : AC4 25) chain A residue 326 type sequence L description BINDING SITE FOR RESIDUE OLC A 1204 source : AC4 26) chain A residue 399 type sequence Y description BINDING SITE FOR RESIDUE OLC A 1205 source : AC5 27) chain A residue 87 type sequence Y description BINDING SITE FOR RESIDUE PEG A 1206 source : AC6 28) chain A residue 380 type sequence Y description BINDING SITE FOR RESIDUE PEG A 1206 source : AC6 29) chain A residue 384 type sequence N description BINDING SITE FOR RESIDUE PEG A 1206 source : AC6 30) chain A residue 77 type sequence L description BINDING SITE FOR RESIDUE OLC A 1207 source : AC7 31) chain A residue 193 type sequence K description BINDING SITE FOR RESIDUE OLC A 1208 source : AC8 32) chain A residue 216 type sequence D description BINDING SITE FOR RESIDUE OLC A 1208 source : AC8 33) chain A residue 217 type sequence F description BINDING SITE FOR RESIDUE OLC A 1208 source : AC8 34) chain A residue 216 type sequence D description BINDING SITE FOR RESIDUE TRS A 1209 source : AC9 35) chain A residue 63 type sequence M description BINDING SITE FOR RESIDUE OLA A 1211 source : BC1 36) chain A residue 174 type sequence I description BINDING SITE FOR RESIDUE OLA A 1212 source : BC2 37) chain A residue 239 type sequence L description BINDING SITE FOR RESIDUE DGA A 1213 source : BC3 38) chain A residue 242 type sequence H description BINDING SITE FOR RESIDUE DGA A 1213 source : BC3 39) chain A residue 55 type sequence H description BINDING SITE FOR RESIDUE DGA A 1214 source : BC4 40) chain A residue 242 type sequence H description BINDING SITE FOR RESIDUE DGA A 1214 source : BC4 41) chain A residue 135 type BINDING sequence D description BINDING => ECO:0000269|PubMed:23519215, ECO:0007744|PDB:4IB4, ECO:0007744|PDB:4NC3 source Swiss-Prot : SWS_FT_FI10 42) chain A residue 140 type BINDING sequence T description BINDING => ECO:0000269|PubMed:23519215, ECO:0007744|PDB:4IB4, ECO:0007744|PDB:4NC3 source Swiss-Prot : SWS_FT_FI10 43) chain A residue 209 type BINDING sequence L description BINDING => ECO:0000269|PubMed:23519215, ECO:0007744|PDB:4IB4, ECO:0007744|PDB:4NC3 source Swiss-Prot : SWS_FT_FI10 44) chain A residue 209 type SITE sequence L description Hydrophobic barrier that decreases the speed of ligand binding and dissociation => ECO:0000269|PubMed:28129538 source Swiss-Prot : SWS_FT_FI11 45) chain A residue 80-90 type TOPO_DOM sequence SLEKKLQYATN description Cytoplasmic => ECO:0000269|PubMed:23519215, ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538 source Swiss-Prot : SWS_FT_FI2 46) chain A residue 152-171 type TOPO_DOM sequence DRYIAIKKPIQANQYNSRAT description Cytoplasmic => ECO:0000269|PubMed:23519215, ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538 source Swiss-Prot : SWS_FT_FI2 47) chain A residue 397 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000255 source Swiss-Prot : SWS_FT_FI12 48) chain A residue 91-113 type TRANSMEM sequence YFLMSLAVADLLVGLFVMPIALL description Helical; Name=2 => ECO:0000269|PubMed:23519215, ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538 source Swiss-Prot : SWS_FT_FI3 49) chain A residue 114-129 type TOPO_DOM sequence TIMFEAMWPLPLVLCP description Extracellular => ECO:0000269|PubMed:23519215, ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538 source Swiss-Prot : SWS_FT_FI4 50) chain A residue 193-216 type TOPO_DOM sequence KGIETVDNPNNITCVLTKERFGD description Extracellular => ECO:0000269|PubMed:23519215, ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538 source Swiss-Prot : SWS_FT_FI4 51) chain A residue 346-360 type TOPO_DOM sequence TLVLCDSCNQTTLQM description Extracellular => ECO:0000269|PubMed:23519215, ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538 source Swiss-Prot : SWS_FT_FI4 52) chain A residue 130-151 type TRANSMEM sequence AWLFLDVLFSTASIWHLCAISV description Helical; Name=3 => ECO:0000269|PubMed:23519215, ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538 source Swiss-Prot : SWS_FT_FI5 53) chain A residue 172-192 type TRANSMEM sequence AFIKITVVWLISIGIAIPVPI description Helical; Name=4 => ECO:0000269|PubMed:23519215, ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538 source Swiss-Prot : SWS_FT_FI6 54) chain A residue 217-239 type TRANSMEM sequence FMLFGSLAAFFTPLAIMIVTYFL description Helical; Name=5 => ECO:0000269|PubMed:23519215, ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538 source Swiss-Prot : SWS_FT_FI7 55) chain A residue 325-345 type TRANSMEM sequence VLGIVFFLFLLMWCPFFITNI description Helical; Name=6 => ECO:0000269|PubMed:23519215, ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538 source Swiss-Prot : SWS_FT_FI8 56) chain A residue 361-382 type TRANSMEM sequence LLEIFVWIGYVSSGVNPLVYTL description Helical; Name=7 => ECO:0000269|PubMed:23519215, ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538 source Swiss-Prot : SWS_FT_FI9 57) chain A residue 57-79 type TRANSMEM sequence AALLILMVIIPTIGGNTLVILAV description Helical; Name=1 => ECO:0000269|PubMed:23519215, ECO:0000269|PubMed:24357322, ECO:0000269|PubMed:28129538 source Swiss-Prot : SWS_FT_FI1 58) chain A residue 141-157 type prosite sequence ASIWHLCAISVDRYIAI description G_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASIwHLCAISVDRYIaI source prosite : PS00237 59) chain A residue 1007 type BINDING sequence W description axial binding residue source Swiss-Prot : SWS_FT_FI13 60) chain A residue 1102 type BINDING sequence I description axial binding residue source Swiss-Prot : SWS_FT_FI13

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