eF-site ID 4ldl-AB PDB Code 4ldl Chain A, B click to enlarge Title Structure of beta2 adrenoceptor bound to hydroxybenzylisoproterenol and an engineered nanobody Classification MEMBRANE PROTEIN/HYDROLASE Compound Lysozyme, Beta-2 adrenergic receptor Source Homo sapiens (Human) (4LDL) Sequence A:  DAENLYFQGNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHL LTKSPSLNAAKSELDKAIGRNTNGVITKDEAEKLFNQDVD AAVRGILRNAKLKPVYDSLDAVRRAALINMVFQMGETGVA GFTNSLRMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITT FRTGTWDAYAADEVWVVGMGIVMSLIVLAIVFGNVLVITA IAKFERLQTVTNYFITSLACADLVMGLAVVPFGAAHILTK TWTFGNFWCEFWTSIDVLCVTASIETLCVIAVDRYFAITS PFKYQSLLTKNKARVIILMVWIVSGLTSFLPIQMHWYRAT HQEAINCYAEETCCDFFTNQAYAIASSIVSFYVPLVIMVF VYSRVFQEAKRQLQKFALKEHKALKTLGIIMGTFTLCWLP FFIVNIVHVIQDNLIRKEVYILLNWIGYVNSGFNPLIYCR SPDFRIAFQELLCL B:  QVQLQESGGGLVQAGGSLRLSCAASGSIFALNIMGWYRQA PGKQRELVAAIHSGGTTNYANSVKGRFTISRDNAANTVYL QMNSLKPEDTAVYYCNVKDFGAIIYDYDYWGQGTQVTVSS Description Functional site 1) chain A residue 1113 type sequence D description BINDING SITE FOR RESIDUE XQC A 1401 source : AC1 2) chain A residue 1191 type sequence C description BINDING SITE FOR RESIDUE XQC A 1401 source : AC1 3) chain A residue 1192 type sequence D description BINDING SITE FOR RESIDUE XQC A 1401 source : AC1 4) chain A residue 1193 type sequence F description BINDING SITE FOR RESIDUE XQC A 1401 source : AC1 5) chain A residue 1203 type sequence S description BINDING SITE FOR RESIDUE XQC A 1401 source : AC1 6) chain A residue 1207 type sequence S description BINDING SITE FOR RESIDUE XQC A 1401 source : AC1 7) chain A residue 1289 type sequence F description BINDING SITE FOR RESIDUE XQC A 1401 source : AC1 8) chain A residue 1293 type sequence N description BINDING SITE FOR RESIDUE XQC A 1401 source : AC1 9) chain A residue 1309 type sequence I description BINDING SITE FOR RESIDUE XQC A 1401 source : AC1 10) chain A residue 1312 type sequence N description BINDING SITE FOR RESIDUE XQC A 1401 source : AC1 11) chain A residue 1316 type sequence Y description BINDING SITE FOR RESIDUE XQC A 1401 source : AC1 12) chain A residue 1103 type sequence N description BINDING SITE FOR RESIDUE NA A 1402 source : AC2 13) chain A residue 1184 type sequence C description BINDING SITE FOR RESIDUE NA A 1402 source : AC2 14) chain A residue 1185 type sequence Y description BINDING SITE FOR RESIDUE NA A 1402 source : AC2 15) chain A residue 1187 type sequence E description BINDING SITE FOR RESIDUE NA A 1402 source : AC2 16) chain A residue 1190 type sequence C description BINDING SITE FOR RESIDUE NA A 1402 source : AC2 17) chain A residue 1306 type sequence E description BINDING SITE FOR RESIDUE 1WV A 1403 source : AC3 18) chain A residue 1313 type sequence W description BINDING SITE FOR RESIDUE 1WV A 1403 source : AC3 19) chain A residue 897 type BINDING sequence L description BINDING => ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI3 20) chain A residue 969 type BINDING sequence F description BINDING => ECO:0000269|PubMed:8266098 source Swiss-Prot : SWS_FT_FI3 21) chain A residue 982 type BINDING sequence S description BINDING => ECO:0000303|PubMed:7831309 source Swiss-Prot : SWS_FT_FI4 22) chain A residue 997 type BINDING sequence N description BINDING => ECO:0000303|PubMed:7831309 source Swiss-Prot : SWS_FT_FI4 23) chain A residue 1035-1058 type TRANSMEM sequence GMGIVMSLIVLAIVFGNVLVITAI description Helical; Name=1 source Swiss-Prot : SWS_FT_FI5 24) chain A residue 1059-1071 type TOPO_DOM sequence AKFERLQTVTNYF description Cytoplasmic source Swiss-Prot : SWS_FT_FI6 25) chain A residue 1130-1150 type TOPO_DOM sequence DRYFAITSPFKYQSLLTKNKA description Cytoplasmic source Swiss-Prot : SWS_FT_FI6 26) chain A residue 1221-1302 type TOPO_DOM sequence RVFQEAKRQLQKFALKEHKALKTLGIIMGTFTLCWLPFFI VNIVHVIQDNL description Cytoplasmic source Swiss-Prot : SWS_FT_FI6 27) chain A residue 1072-1095 type TRANSMEM sequence ITSLACADLVMGLAVVPFGAAHIL description Helical; Name=2 source Swiss-Prot : SWS_FT_FI7 28) chain A residue 1096-1106 type TOPO_DOM sequence TKTWTFGNFWC description Extracellular source Swiss-Prot : SWS_FT_FI8 29) chain A residue 1175-1196 type TOPO_DOM sequence RATHQEAINCYAEETCCDFFTN description Extracellular source Swiss-Prot : SWS_FT_FI8 30) chain A residue 1327-1333 type TOPO_DOM sequence CRSPDFR description Extracellular source Swiss-Prot : SWS_FT_FI8 31) chain A residue 1107-1129 type TRANSMEM sequence EFWTSIDVLCVTASIETLCVIAV description Helical; Name=3 source Swiss-Prot : SWS_FT_FI9 32) chain A residue 1151-1174 type TRANSMEM sequence RVIILMVWIVSGLTSFLPIQMHWY description Helical; Name=4 source Swiss-Prot : SWS_FT_FI10 33) chain A residue 1197-1220 type TRANSMEM sequence QAYAIASSIVSFYVPLVIMVFVYS description Helical; Name=5 source Swiss-Prot : SWS_FT_FI11 34) chain A residue 1303-1326 type TRANSMEM sequence IRKEVYILLNWIGYVNSGFNPLIY description Helical; Name=6 source Swiss-Prot : SWS_FT_FI12 35) chain A residue 1113 type BINDING sequence D description BINDING => ECO:0000269|PubMed:18547522, ECO:0007744|PDB:3D4S source Swiss-Prot : SWS_FT_FI14 36) chain A residue 1118 type BINDING sequence T description BINDING => ECO:0000269|PubMed:18547522, ECO:0007744|PDB:3D4S source Swiss-Prot : SWS_FT_FI14 37) chain A residue 1321 type BINDING sequence F description BINDING => ECO:0000269|PubMed:18547522, ECO:0007744|PDB:3D4S source Swiss-Prot : SWS_FT_FI14 38) chain A residue 1340 type BINDING sequence L description BINDING => ECO:0000269|PubMed:18547522, ECO:0007744|PDB:3D4S source Swiss-Prot : SWS_FT_FI14 39) chain A residue 1203 type BINDING sequence S description BINDING => ECO:0000269|PubMed:17952055, ECO:0000269|PubMed:17962520, ECO:0007744|PDB:2RH1 source Swiss-Prot : SWS_FT_FI15 40) chain A residue 1141 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:8521811 source Swiss-Prot : SWS_FT_FI16 41) chain A residue 1274 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:17525332 source Swiss-Prot : SWS_FT_FI17 42) chain A residue 1289 type MOD_RES sequence F description Phosphoserine; by PKA => ECO:0000255 source Swiss-Prot : SWS_FT_FI18 43) chain A residue 1290 type MOD_RES sequence F description Phosphoserine; by PKA => ECO:0000255 source Swiss-Prot : SWS_FT_FI18 44) chain A residue 1293 type LIPID sequence N description S-palmitoyl cysteine => ECO:0000269|PubMed:27481942 source Swiss-Prot : SWS_FT_FI20 45) chain A residue 876 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_FI1 46) chain A residue 885 type ACT_SITE sequence D 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_FI2 47) chain A residue 1119-1135 type prosite sequence ASIETLCVIAVDRYFAI description G_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASIeTLCVIAVDRYFaI source prosite : PS00237 48) chain A residue 876 type catalytic sequence E description 921 source MCSA : MCSA1 49) chain A residue 885 type catalytic sequence D description 921 source MCSA : MCSA1

Display surface Download Links