eF-site ID 3p0g-A PDB Code 3p0g Chain A click to enlarge Title Structure of a nanobody-stabilized active state of the beta2 adrenoceptor Classification SIGNALING PROTEIN, Hydrolase Compound Beta-2 adrenergic receptor, Lysozyme Source null (3P0G) Sequence A:  DVTQQRDEVWVVGMGIVMSLIVLAIVFGNVLVITAIAKFE RLQTVTNYFITSLACADLVMGLAVVPFGAAHILMKMWTFG NFWCEFWTSIDVLCVTASIETLCVIAVDRYFAITSPFKYQ SLLTKNKARVIILMVWIVSGLTSFLPIQMHWYRATHQEAI NCYAEETCCDFFTNQAYAIASSIVSFYVPLVIMVFVYSRV FQEAKLKEHKALKTLGIIMGTFTLCWLPFFIVNIVHVIQD NLIRKEVYILLNWIGYVNSGFNPLIYCRSPDFRIAFQELL CLRR Description Functional site 1) chain A residue 109 type sequence W description BINDING SITE FOR RESIDUE P0G A 366 source : AC1 2) chain A residue 113 type sequence D description BINDING SITE FOR RESIDUE P0G A 366 source : AC1 3) chain A residue 117 type sequence V description BINDING SITE FOR RESIDUE P0G A 366 source : AC1 4) chain A residue 191 type sequence C description BINDING SITE FOR RESIDUE P0G A 366 source : AC1 5) chain A residue 193 type sequence F description BINDING SITE FOR RESIDUE P0G A 366 source : AC1 6) chain A residue 200 type sequence A description BINDING SITE FOR RESIDUE P0G A 366 source : AC1 7) chain A residue 203 type sequence S description BINDING SITE FOR RESIDUE P0G A 366 source : AC1 8) chain A residue 207 type sequence S description BINDING SITE FOR RESIDUE P0G A 366 source : AC1 9) chain A residue 289 type sequence F description BINDING SITE FOR RESIDUE P0G A 366 source : AC1 10) chain A residue 290 type sequence F description BINDING SITE FOR RESIDUE P0G A 366 source : AC1 11) chain A residue 293 type sequence N description BINDING SITE FOR RESIDUE P0G A 366 source : AC1 12) chain A residue 308 type sequence Y description BINDING SITE FOR RESIDUE P0G A 366 source : AC1 13) chain A residue 309 type sequence I description BINDING SITE FOR RESIDUE P0G A 366 source : AC1 14) chain A residue 312 type sequence N description BINDING SITE FOR RESIDUE P0G A 366 source : AC1 15) chain A residue 59-71 type TOPO_DOM sequence AKFERLQTVTNYF description Cytoplasmic source Swiss-Prot : SWS_FT_FI3 16) chain A residue 130-150 type TOPO_DOM sequence DRYFAITSPFKYQSLLTKNKA description Cytoplasmic source Swiss-Prot : SWS_FT_FI3 17) chain A residue 72-95 type TRANSMEM sequence ITSLACADLVMGLAVVPFGAAHIL description Helical; Name=2 source Swiss-Prot : SWS_FT_FI4 18) chain A residue 107-129 type TRANSMEM sequence EFWTSIDVLCVTASIETLCVIAV description Helical; Name=3 source Swiss-Prot : SWS_FT_FI5 19) chain A residue 151-174 type TRANSMEM sequence RVIILMVWIVSGLTSFLPIQMHWY description Helical; Name=4 source Swiss-Prot : SWS_FT_FI6 20) chain A residue 197-220 type TRANSMEM sequence QAYAIASSIVSFYVPLVIMVFVYS description Helical; Name=5 source Swiss-Prot : SWS_FT_FI7 21) chain A residue 275-298 type TRANSMEM sequence LGIIMGTFTLCWLPFFIVNIVHVI description Helical; Name=6 source Swiss-Prot : SWS_FT_FI8 22) chain A residue 306-329 type TRANSMEM sequence EVYILLNWIGYVNSGFNPLIYCRS description Helical; Name=7 source Swiss-Prot : SWS_FT_FI9 23) chain A residue 113 type BINDING sequence D description BINDING => ECO:0000269|PubMed:18547522, ECO:0007744|PDB:3D4S source Swiss-Prot : SWS_FT_FI10 24) chain A residue 118 type BINDING sequence T description BINDING => ECO:0000269|PubMed:18547522, ECO:0007744|PDB:3D4S source Swiss-Prot : SWS_FT_FI10 25) chain A residue 293 type BINDING sequence N description BINDING => ECO:0000269|PubMed:18547522, ECO:0007744|PDB:3D4S source Swiss-Prot : SWS_FT_FI10 26) chain A residue 312 type BINDING sequence N description BINDING => ECO:0000269|PubMed:18547522, ECO:0007744|PDB:3D4S source Swiss-Prot : SWS_FT_FI10 27) chain A residue 316 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:18547522, ECO:0007744|PDB:3D4S source Swiss-Prot : SWS_FT_FI10 28) chain A residue 203 type BINDING sequence S description BINDING => ECO:0000269|PubMed:17952055, ECO:0000269|PubMed:17962520, ECO:0007744|PDB:2RH1 source Swiss-Prot : SWS_FT_FI11 29) chain A residue 141 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:8521811 source Swiss-Prot : SWS_FT_FI12 30) chain A residue 341 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000269|PubMed:17962520, ECO:0000269|PubMed:18547522, ECO:0000269|PubMed:2540197, ECO:0000269|PubMed:27481942 source Swiss-Prot : SWS_FT_FI16 31) chain A residue 227 type ACT_SITE sequence K 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_FI18 32) chain A residue 227 type ACT_SITE sequence K description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:1892846, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI19 33) chain A residue 175-196 type TOPO_DOM sequence RATHQEAINCYAEETCCDFFTN description Extracellular source Swiss-Prot : SWS_FT_FI1 34) chain A residue 299-305 type TOPO_DOM sequence QDNLIRK description Extracellular source Swiss-Prot : SWS_FT_FI1 35) chain A residue 96-106 type TOPO_DOM sequence MKMWTFGNFWC description Extracellular source Swiss-Prot : SWS_FT_FI1 36) chain A residue 35-58 type TRANSMEM sequence GMGIVMSLIVLAIVFGNVLVITAI description Helical; Name=1 source Swiss-Prot : SWS_FT_FI2 37) chain A residue 119-135 type prosite sequence ASIETLCVIAVDRYFAI description G_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASIeTLCVIAVDRYFaI source prosite : PS00237 38) chain A residue 227 type catalytic sequence K description 921 source MCSA : MCSA1 39) chain A residue 227 type catalytic sequence K description 921 source MCSA : MCSA1

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