eF-site ID 6a93-AB PDB Code 6a93 Chain A, B click to enlarge Title Crystal structure of 5-HT2AR in complex with risperidone Classification MEMBRANE PROTEIN Compound 5-hydroxytryptamine receptor 2A,Soluble cytochrome b562 Source (5HT2A_HUMAN) Sequence A:  THLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNA TNYFLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLC AVWIYLDVLFSTAKIWHLCAISLDRYVAIQNPIHHSRFNS RTKAFLKIIAVWTISVGISMPIPVFGLQDDSKVFKEGSCL LADDNFVLIGSFVSFFIPLTIMVITYFLTIKSLQKEAADL EDNWETLNDNLKVIEKADNAAQVKDALTKMRAAALDAGSG SGDILVGQIDDALKLANEGKVKEAQAAAEQLKTTINAYIQ KYGQSISNEQKACKVLGIVFFLFVVMWCPFFITNIMAVIC KESCNEDVIGALLNVFVWIGYLSSAVNPLVYTLFNKTYRS AFSRYIQCQY B:  QEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNY FLMSLAIADMLLGFLVMPVSMLTILYGYRWPLPSKLCAVW IYLDVLFSTAKIWHLCAISLDRYVAIQNPSRTKAFLKIIA VWTISVGISMPIPVFGLQDDSKVFKEGSCLLADDNFVLIG SFVSFFIPLTIMVITYFLTIKSLQKEAADLEDNWETLNDN LKVIEKADNAAQVKDALTKMRAAALDAGGDILVGQIDDAL KLANEGKVKEAQAAAEQLKTTINAYIQKYGQSISNEQKAC KVLGIVFFLFVVMWCPFFITNIMAVICKESCNEDVIGALL NVFVWIGYLSSAVNPLVYTLFNKTYRSAFSRYIQCQYKE Description Functional site 1) chain A residue 131 type sequence S description binding site for residue 8NU A 3001 source : AC1 2) chain A residue 151 type sequence W description binding site for residue 8NU A 3001 source : AC1 3) chain A residue 155 type sequence D description binding site for residue 8NU A 3001 source : AC1 4) chain A residue 159 type sequence S description binding site for residue 8NU A 3001 source : AC1 5) chain A residue 160 type sequence T description binding site for residue 8NU A 3001 source : AC1 6) chain A residue 163 type sequence I description binding site for residue 8NU A 3001 source : AC1 7) chain A residue 228 type sequence L description binding site for residue 8NU A 3001 source : AC1 8) chain A residue 242 type sequence S description binding site for residue 8NU A 3001 source : AC1 9) chain A residue 243 type sequence F description binding site for residue 8NU A 3001 source : AC1 10) chain A residue 332 type sequence F description binding site for residue 8NU A 3001 source : AC1 11) chain A residue 336 type sequence W description binding site for residue 8NU A 3001 source : AC1 12) chain A residue 339 type sequence F description binding site for residue 8NU A 3001 source : AC1 13) chain A residue 340 type sequence F description binding site for residue 8NU A 3001 source : AC1 14) chain A residue 362 type sequence L description binding site for residue 8NU A 3001 source : AC1 15) chain A residue 363 type sequence N description binding site for residue 8NU A 3001 source : AC1 16) chain A residue 370 type sequence Y description binding site for residue 8NU A 3001 source : AC1 17) chain A residue 114 type sequence M description binding site for residue CLR A 3002 source : AC2 18) chain A residue 118 type sequence I description binding site for residue CLR A 3002 source : AC2 19) chain A residue 153 type sequence Y description binding site for residue CLR A 3002 source : AC2 20) chain A residue 193 type sequence F description binding site for residue CLR A 3002 source : AC2 21) chain A residue 196 type sequence I description binding site for residue CLR A 3002 source : AC2 22) chain A residue 200 type sequence W description binding site for residue CLR A 3002 source : AC2 23) chain A residue 204 type sequence V description binding site for residue CLR A 3002 source : AC2 24) chain A residue 182 type sequence H description binding site for residue ZN A 3003 source : AC3 25) chain A residue 183 type sequence H description binding site for residue ZN A 3003 source : AC3 26) chain A residue 264 type sequence E description binding site for residue ZN A 3003 source : AC3 27) chain A residue 318 type sequence E description binding site for residue ZN A 3003 source : AC3 28) chain A residue 226 type sequence S description binding site for residue 1PE A 3004 source : AC4 29) chain A residue 261 type sequence L description binding site for residue 1PE A 3005 source : AC5 30) chain A residue 262 type sequence Q description binding site for residue 1PE A 3005 source : AC5 31) chain A residue 265 type sequence A description binding site for residue 1PE A 3005 source : AC5 32) chain A residue 315 type sequence I description binding site for residue 1PE A 3005 source : AC5 33) chain A residue 319 type sequence Q description binding site for residue 1PE A 3005 source : AC5 34) chain A residue 1004 type sequence E description binding site for residue 1PE A 3005 source : AC5 35) chain A residue 1080 type sequence N description binding site for residue 1PE A 3005 source : AC5 36) chain A residue 1004 type sequence E description binding site for residue 1PE A 3006 source : AC6 37) chain A residue 1007 type sequence W description binding site for residue 1PE A 3006 source : AC6 38) chain A residue 1027 type sequence K description binding site for residue 1PE A 3006 source : AC6 39) chain B residue 131 type sequence S description binding site for residue 8NU B 3001 source : AC7 40) chain B residue 151 type sequence W description binding site for residue 8NU B 3001 source : AC7 41) chain B residue 155 type sequence D description binding site for residue 8NU B 3001 source : AC7 42) chain B residue 156 type sequence V description binding site for residue 8NU B 3001 source : AC7 43) chain B residue 159 type sequence S description binding site for residue 8NU B 3001 source : AC7 44) chain B residue 160 type sequence T description binding site for residue 8NU B 3001 source : AC7 45) chain B residue 163 type sequence I description binding site for residue 8NU B 3001 source : AC7 46) chain B residue 228 type sequence L description binding site for residue 8NU B 3001 source : AC7 47) chain B residue 242 type sequence S description binding site for residue 8NU B 3001 source : AC7 48) chain B residue 332 type sequence F description binding site for residue 8NU B 3001 source : AC7 49) chain B residue 336 type sequence W description binding site for residue 8NU B 3001 source : AC7 50) chain B residue 339 type sequence F description binding site for residue 8NU B 3001 source : AC7 51) chain B residue 340 type sequence F description binding site for residue 8NU B 3001 source : AC7 52) chain B residue 363 type sequence N description binding site for residue 8NU B 3001 source : AC7 53) chain B residue 370 type sequence Y description binding site for residue 8NU B 3001 source : AC7 54) chain B residue 395 type sequence I description binding site for residue PLM B 3002 source : AC8 55) chain B residue 396 type sequence Q description binding site for residue PLM B 3002 source : AC8 56) chain B residue 397 type sequence C description binding site for residue PLM B 3002 source : AC8 57) chain B residue 94 type sequence L description binding site for residue CLR B 3003 source : AC9 58) chain B residue 394 type sequence Y description binding site for residue CLR B 3003 source : AC9 59) chain B residue 399 type sequence Y description binding site for residue CLR B 3003 source : AC9 60) chain A residue 76-99 type TRANSMEM sequence WSALLTAVVIILTIAGNILVIMAV description Helical; Name=1 => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 61) chain B residue 76-99 type TRANSMEM sequence WSALLTAVVIILTIAGNILVIMAV description Helical; Name=1 => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 62) chain A residue 100-110 type TOPO_DOM sequence SLEKKLQNATN description Cytoplasmic => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 63) chain A residue 172-191 type TOPO_DOM sequence DRYVAIQNPIHHSRFNSRTK description Cytoplasmic => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 64) chain B residue 100-110 type TOPO_DOM sequence SLEKKLQNATN description Cytoplasmic => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 65) chain B residue 172-191 type TOPO_DOM sequence DRYVAIQNPSRTK description Cytoplasmic => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 66) chain A residue 155 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P41595 source Swiss-Prot : SWS_FT_FI10 67) chain A residue 160 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P41595 source Swiss-Prot : SWS_FT_FI10 68) chain A residue 229 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P41595 source Swiss-Prot : SWS_FT_FI10 69) chain B residue 155 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P41595 source Swiss-Prot : SWS_FT_FI10 70) chain B residue 160 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P41595 source Swiss-Prot : SWS_FT_FI10 71) chain B residue 229 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P41595 source Swiss-Prot : SWS_FT_FI10 72) chain A residue 229 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 73) chain B residue 229 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 74) chain A residue 111-132 type TRANSMEM sequence YFLMSLAIADMLLGFLVMPVSM description Helical; Name=2 => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 75) chain B residue 111-132 type TRANSMEM sequence YFLMSLAIADMLLGFLVMPVSM description Helical; Name=2 => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 76) chain A residue 133-148 type TOPO_DOM sequence LTILYGYRWPLPSKLC description Extracellular => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 77) chain A residue 216-233 type TOPO_DOM sequence QDDSKVFKEGSCLLADDN description Extracellular => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 78) chain A residue 347-362 type TOPO_DOM sequence VICKESCNEDVIGALL description Extracellular => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 79) chain B residue 133-148 type TOPO_DOM sequence LTILYGYRWPLPSKLC description Extracellular => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 80) chain B residue 216-233 type TOPO_DOM sequence QDDSKVFKEGSCLLADDN description Extracellular => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 81) chain B residue 347-362 type TOPO_DOM sequence VICKESCNEDVIGALL description Extracellular => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 82) chain A residue 149-171 type TRANSMEM sequence AVWIYLDVLFSTAKIWHLCAISL description Helical; Name=3 => ECO:0000250 source Swiss-Prot : SWS_FT_FI5 83) chain B residue 149-171 type TRANSMEM sequence AVWIYLDVLFSTAKIWHLCAISL description Helical; Name=3 => ECO:0000250 source Swiss-Prot : SWS_FT_FI5 84) chain A residue 192-215 type TRANSMEM sequence AFLKIIAVWTISVGISMPIPVFGL description Helical; Name=4 => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 85) chain B residue 192-215 type TRANSMEM sequence AFLKIIAVWTISVGISMPIPVFGL description Helical; Name=4 => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 86) chain A residue 234-254 type TRANSMEM sequence FVLIGSFVSFFIPLTIMVITY description Helical; Name=5 => ECO:0000250 source Swiss-Prot : SWS_FT_FI7 87) chain B residue 234-254 type TRANSMEM sequence FVLIGSFVSFFIPLTIMVITY description Helical; Name=5 => ECO:0000250 source Swiss-Prot : SWS_FT_FI7 88) chain A residue 325-346 type TRANSMEM sequence LGIVFFLFVVMWCPFFITNIMA description Helical; Name=6 => ECO:0000250 source Swiss-Prot : SWS_FT_FI8 89) chain B residue 325-346 type TRANSMEM sequence LGIVFFLFVVMWCPFFITNIMA description Helical; Name=6 => ECO:0000250 source Swiss-Prot : SWS_FT_FI8 90) chain A residue 363-384 type TRANSMEM sequence NVFVWIGYLSSAVNPLVYTLFN description Helical; Name=7 => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 91) chain B residue 363-384 type TRANSMEM sequence NVFVWIGYLSSAVNPLVYTLFN description Helical; Name=7 => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 92) chain A residue 1007 type BINDING sequence W description axial binding residue source Swiss-Prot : SWS_FT_FI12 93) chain A residue 1102 type BINDING sequence I description axial binding residue source Swiss-Prot : SWS_FT_FI12 94) chain B residue 1007 type BINDING sequence W description axial binding residue source Swiss-Prot : SWS_FT_FI12 95) chain B residue 1102 type BINDING sequence I description axial binding residue source Swiss-Prot : SWS_FT_FI12

Display surface Download Links