eF-site ID 6a94-AB PDB Code 6a94 Chain A, B click to enlarge Title Crystal structure of 5-HT2AR in complex with zotepine 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 155 type sequence D description binding site for residue ZOT A 3001 source : AC1 2) chain A residue 159 type sequence S description binding site for residue ZOT A 3001 source : AC1 3) chain A residue 229 type sequence L description binding site for residue ZOT A 3001 source : AC1 4) chain A residue 235 type sequence V description binding site for residue ZOT A 3001 source : AC1 5) chain A residue 238 type sequence G description binding site for residue ZOT A 3001 source : AC1 6) chain A residue 242 type sequence S description binding site for residue ZOT A 3001 source : AC1 7) chain A residue 336 type sequence W description binding site for residue ZOT A 3001 source : AC1 8) chain A residue 339 type sequence F description binding site for residue ZOT A 3001 source : AC1 9) chain A residue 340 type sequence F description binding site for residue ZOT A 3001 source : AC1 10) chain A residue 343 type sequence N description binding site for residue ZOT A 3001 source : AC1 11) chain A residue 111 type sequence Y description binding site for residue CLR A 3002 source : AC2 12) chain A residue 114 type sequence M description binding site for residue CLR A 3002 source : AC2 13) chain A residue 118 type sequence I description binding site for residue CLR A 3002 source : AC2 14) chain A residue 122 type sequence L description binding site for residue CLR A 3002 source : AC2 15) chain A residue 153 type sequence Y description binding site for residue CLR A 3002 source : AC2 16) chain A residue 193 type sequence F description binding site for residue CLR A 3002 source : AC2 17) chain A residue 196 type sequence I description binding site for residue CLR A 3002 source : AC2 18) chain A residue 200 type sequence W description binding site for residue CLR A 3002 source : AC2 19) chain A residue 204 type sequence V description binding site for residue CLR A 3002 source : AC2 20) chain A residue 261 type sequence L description binding site for residue 1PE A 3003 source : AC3 21) chain A residue 262 type sequence Q description binding site for residue 1PE A 3003 source : AC3 22) chain A residue 265 type sequence A description binding site for residue 1PE A 3003 source : AC3 23) chain A residue 315 type sequence I description binding site for residue 1PE A 3003 source : AC3 24) chain A residue 316 type sequence S description binding site for residue 1PE A 3003 source : AC3 25) chain A residue 319 type sequence Q description binding site for residue 1PE A 3003 source : AC3 26) chain A residue 1004 type sequence E description binding site for residue 1PE A 3003 source : AC3 27) chain A residue 1080 type sequence N description binding site for residue 1PE A 3003 source : AC3 28) chain A residue 182 type sequence H description binding site for residue ZN A 3004 source : AC4 29) chain A residue 183 type sequence H description binding site for residue ZN A 3004 source : AC4 30) chain A residue 264 type sequence E description binding site for residue ZN A 3004 source : AC4 31) chain A residue 318 type sequence E description binding site for residue ZN A 3004 source : AC4 32) chain B residue 155 type sequence D description binding site for residue ZOT B 3001 source : AC5 33) chain B residue 156 type sequence V description binding site for residue ZOT B 3001 source : AC5 34) chain B residue 159 type sequence S description binding site for residue ZOT B 3001 source : AC5 35) chain B residue 160 type sequence T description binding site for residue ZOT B 3001 source : AC5 36) chain B residue 229 type sequence L description binding site for residue ZOT B 3001 source : AC5 37) chain B residue 235 type sequence V description binding site for residue ZOT B 3001 source : AC5 38) chain B residue 238 type sequence G description binding site for residue ZOT B 3001 source : AC5 39) chain B residue 242 type sequence S description binding site for residue ZOT B 3001 source : AC5 40) chain B residue 339 type sequence F description binding site for residue ZOT B 3001 source : AC5 41) chain B residue 340 type sequence F description binding site for residue ZOT B 3001 source : AC5 42) chain B residue 395 type sequence I description binding site for residue PLM B 3002 source : AC6 43) chain B residue 396 type sequence Q description binding site for residue PLM B 3002 source : AC6 44) chain B residue 397 type sequence C description binding site for residue PLM B 3002 source : AC6 45) chain B residue 86 type sequence I description binding site for residue CLR B 3003 source : AC7 46) chain B residue 394 type sequence Y description binding site for residue CLR B 3003 source : AC7 47) chain B residue 399 type sequence Y description binding site for residue CLR B 3003 source : AC7 48) chain A residue 253 type sequence T description binding site for residue A6L B 3004 source : AC8 49) chain A residue 256 type sequence L description binding site for residue A6L B 3004 source : AC8 50) chain B residue 399 type sequence Y description binding site for residue A6L B 3004 source : AC8 51) chain A residue 1007 type BINDING sequence W description axial binding residue source Swiss-Prot : SWS_FT_FI12 52) chain A residue 1102 type BINDING sequence I description axial binding residue source Swiss-Prot : SWS_FT_FI12 53) chain B residue 1007 type BINDING sequence W description axial binding residue source Swiss-Prot : SWS_FT_FI12 54) chain B residue 1102 type BINDING sequence I description axial binding residue source Swiss-Prot : SWS_FT_FI12 55) chain A residue 155 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P41595 source Swiss-Prot : SWS_FT_FI10 56) chain A residue 160 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P41595 source Swiss-Prot : SWS_FT_FI10 57) chain A residue 229 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P41595 source Swiss-Prot : SWS_FT_FI10 58) chain B residue 155 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P41595 source Swiss-Prot : SWS_FT_FI10 59) chain B residue 160 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P41595 source Swiss-Prot : SWS_FT_FI10 60) chain B residue 229 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P41595 source Swiss-Prot : SWS_FT_FI10 61) 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 62) 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 63) chain A residue 76-99 type TRANSMEM sequence WSALLTAVVIILTIAGNILVIMAV description Helical; Name=1 => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 64) chain B residue 76-99 type TRANSMEM sequence WSALLTAVVIILTIAGNILVIMAV description Helical; Name=1 => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 65) chain A residue 363-384 type TRANSMEM sequence NVFVWIGYLSSAVNPLVYTLFN description Helical; Name=7 => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 66) chain B residue 363-384 type TRANSMEM sequence NVFVWIGYLSSAVNPLVYTLFN description Helical; Name=7 => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 67) chain A residue 100-110 type TOPO_DOM sequence SLEKKLQNATN description Cytoplasmic => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 68) chain A residue 172-191 type TOPO_DOM sequence DRYVAIQNPIHHSRFNSRTK description Cytoplasmic => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 69) chain B residue 100-110 type TOPO_DOM sequence SLEKKLQNATN description Cytoplasmic => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 70) chain B residue 172-191 type TOPO_DOM sequence DRYVAIQNPSRTK description Cytoplasmic => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 71) chain A residue 111-132 type TRANSMEM sequence YFLMSLAIADMLLGFLVMPVSM description Helical; Name=2 => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 72) chain B residue 111-132 type TRANSMEM sequence YFLMSLAIADMLLGFLVMPVSM description Helical; Name=2 => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 73) chain A residue 133-148 type TOPO_DOM sequence LTILYGYRWPLPSKLC description Extracellular => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 74) chain A residue 216-233 type TOPO_DOM sequence QDDSKVFKEGSCLLADDN description Extracellular => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 75) chain A residue 347-362 type TOPO_DOM sequence VICKESCNEDVIGALL description Extracellular => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 76) chain B residue 133-148 type TOPO_DOM sequence LTILYGYRWPLPSKLC description Extracellular => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 77) chain B residue 216-233 type TOPO_DOM sequence QDDSKVFKEGSCLLADDN description Extracellular => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 78) chain B residue 347-362 type TOPO_DOM sequence VICKESCNEDVIGALL description Extracellular => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 79) chain A residue 149-171 type TRANSMEM sequence AVWIYLDVLFSTAKIWHLCAISL description Helical; Name=3 => ECO:0000250 source Swiss-Prot : SWS_FT_FI5 80) chain B residue 149-171 type TRANSMEM sequence AVWIYLDVLFSTAKIWHLCAISL description Helical; Name=3 => ECO:0000250 source Swiss-Prot : SWS_FT_FI5 81) chain A residue 192-215 type TRANSMEM sequence AFLKIIAVWTISVGISMPIPVFGL description Helical; Name=4 => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 82) chain B residue 192-215 type TRANSMEM sequence AFLKIIAVWTISVGISMPIPVFGL description Helical; Name=4 => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 83) chain A residue 234-254 type TRANSMEM sequence FVLIGSFVSFFIPLTIMVITY description Helical; Name=5 => ECO:0000250 source Swiss-Prot : SWS_FT_FI7 84) chain B residue 234-254 type TRANSMEM sequence FVLIGSFVSFFIPLTIMVITY description Helical; Name=5 => ECO:0000250 source Swiss-Prot : SWS_FT_FI7 85) chain A residue 325-346 type TRANSMEM sequence LGIVFFLFVVMWCPFFITNIMA description Helical; Name=6 => ECO:0000250 source Swiss-Prot : SWS_FT_FI8 86) chain B residue 325-346 type TRANSMEM sequence LGIVFFLFVVMWCPFFITNIMA description Helical; Name=6 => ECO:0000250 source Swiss-Prot : SWS_FT_FI8

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