eF-site ID 2ycw-AB PDB Code 2ycw Chain A, B click to enlarge Title TURKEY BETA1 ADRENERGIC RECEPTOR WITH STABILISING MUTATIONS AND BOUND ANTAGONIST CARAZOLOL Classification RECEPTOR Compound BETA-1 ADRENERGIC RECEPTOR Source (ADRB1_MELGA) Sequence A:  AELLSQQWEAGMSLLMALVVLLIVAGNVLVIAAIGSTQRL QTLTNLFITSLACADLVVGLLVVPFGATLVVRGTWLWGSF LCELWTSLDVLCVTASIETLCVIAIDRYLAITSPFRYQSL MTRARAKVIICTVWAISALVSFLPIMMHWWRDEDPQALKC YQDPGCCDFVTNRAYAIASSIISFYIPLLIMIFVALRVYR EAKEQIRKIDRASKRKRVMLMREHKALKTLGIIMGVFTLC WLPFFLVNIVNVFNRDLVPDWLFVAFNWLGYANSAMNPII YCRSPDFRKAFKRLLAF B:  AELLSQQWEAGMSLLMALVVLLIVAGNVLVIAAIGSTQRL QTLTNLFITSLACADLVVGLLVVPFGATLVVRGTWLWGSF LCELWTSLDVLCVTASIETLCVIAIDRYLAITSPFRYQSL MTRARAKVIICTVWAISALVSFLPIMMHWWRDEDPQALKC YQDPGCCDFVTNRAYAIASSIISFYIPLLIMIFVALRVYR EAKEQIRKIDRASKRKRVMLMREHKALKTLGIIMGVFTLC WLPFFLVNIVNVFNRDLVPDWLFVAFNWLGYANSAMNPII YCRSPDFRKAFKRLLAF Description Functional site 1) chain A residue 117 type sequence W description BINDING SITE FOR RESIDUE CAU A 400 source : AC1 2) chain A residue 121 type sequence D description BINDING SITE FOR RESIDUE CAU A 400 source : AC1 3) chain A residue 122 type sequence V description BINDING SITE FOR RESIDUE CAU A 400 source : AC1 4) chain A residue 201 type sequence F description BINDING SITE FOR RESIDUE CAU A 400 source : AC1 5) chain A residue 207 type sequence Y description BINDING SITE FOR RESIDUE CAU A 400 source : AC1 6) chain A residue 211 type sequence S description BINDING SITE FOR RESIDUE CAU A 400 source : AC1 7) chain A residue 215 type sequence S description BINDING SITE FOR RESIDUE CAU A 400 source : AC1 8) chain A residue 306 type sequence F description BINDING SITE FOR RESIDUE CAU A 400 source : AC1 9) chain A residue 310 type sequence N description BINDING SITE FOR RESIDUE CAU A 400 source : AC1 10) chain A residue 329 type sequence N description BINDING SITE FOR RESIDUE CAU A 400 source : AC1 11) chain A residue 333 type sequence Y description BINDING SITE FOR RESIDUE CAU A 400 source : AC1 12) chain B residue 117 type sequence W description BINDING SITE FOR RESIDUE CAU B 400 source : AC2 13) chain B residue 121 type sequence D description BINDING SITE FOR RESIDUE CAU B 400 source : AC2 14) chain B residue 201 type sequence F description BINDING SITE FOR RESIDUE CAU B 400 source : AC2 15) chain B residue 207 type sequence Y description BINDING SITE FOR RESIDUE CAU B 400 source : AC2 16) chain B residue 211 type sequence S description BINDING SITE FOR RESIDUE CAU B 400 source : AC2 17) chain B residue 306 type sequence F description BINDING SITE FOR RESIDUE CAU B 400 source : AC2 18) chain B residue 307 type sequence F description BINDING SITE FOR RESIDUE CAU B 400 source : AC2 19) chain B residue 310 type sequence N description BINDING SITE FOR RESIDUE CAU B 400 source : AC2 20) chain B residue 329 type sequence N description BINDING SITE FOR RESIDUE CAU B 400 source : AC2 21) chain B residue 333 type sequence Y description BINDING SITE FOR RESIDUE CAU B 400 source : AC2 22) chain A residue 286 type sequence H description BINDING SITE FOR RESIDUE 2CV A 1360 source : AC3 23) chain A residue 289 type sequence L description BINDING SITE FOR RESIDUE 2CV A 1360 source : AC3 24) chain A residue 290 type sequence K description BINDING SITE FOR RESIDUE 2CV A 1360 source : AC3 25) chain A residue 296 type sequence M description BINDING SITE FOR RESIDUE 2CV A 1360 source : AC3 26) chain A residue 176 type sequence P description BINDING SITE FOR RESIDUE 2CV A 1361 source : AC4 27) chain A residue 181 type sequence W description BINDING SITE FOR RESIDUE 2CV A 1361 source : AC4 28) chain A residue 185 type sequence E description BINDING SITE FOR RESIDUE 2CV A 1361 source : AC4 29) chain A residue 204 type sequence N description BINDING SITE FOR RESIDUE 2CV A 1361 source : AC4 30) chain A residue 205 type sequence R description BINDING SITE FOR RESIDUE 2CV A 1361 source : AC4 31) chain A residue 206 type sequence A description BINDING SITE FOR RESIDUE 2CV A 1361 source : AC4 32) chain B residue 160 type sequence V description BINDING SITE FOR RESIDUE 2CV A 1361 source : AC4 33) chain A residue 160 type sequence V description BINDING SITE FOR RESIDUE 2CV B 1360 source : AC5 34) chain A residue 164 type sequence T description BINDING SITE FOR RESIDUE 2CV B 1360 source : AC5 35) chain B residue 181 type sequence W description BINDING SITE FOR RESIDUE 2CV B 1360 source : AC5 36) chain B residue 206 type sequence A description BINDING SITE FOR RESIDUE 2CV B 1360 source : AC5 37) chain B residue 157 type sequence R description BINDING SITE FOR RESIDUE 2CV B 1362 source : AC6 38) chain B residue 160 type sequence V description BINDING SITE FOR RESIDUE 2CV B 1362 source : AC6 39) chain A residue 111 type sequence S description BINDING SITE FOR RESIDUE NA A 1362 source : AC7 40) chain A residue 195 type sequence D description BINDING SITE FOR RESIDUE NA A 1362 source : AC7 41) chain A residue 198 type sequence C description BINDING SITE FOR RESIDUE NA A 1362 source : AC7 42) chain B residue 111 type sequence S description BINDING SITE FOR RESIDUE NA B 1363 source : AC8 43) chain B residue 192 type sequence C description BINDING SITE FOR RESIDUE NA B 1363 source : AC8 44) chain B residue 195 type sequence D description BINDING SITE FOR RESIDUE NA B 1363 source : AC8 45) chain B residue 198 type sequence C description BINDING SITE FOR RESIDUE NA B 1363 source : AC8 46) chain A residue 104-115 type TOPO_DOM sequence RGTWLWGSFLCE description Extracellular => ECO:0000269|PubMed:18594507 source Swiss-Prot : SWS_FT_FI4 47) chain A residue 180-205 type TOPO_DOM sequence HWWRDEDPQALKCYQDPGCCDFVTNR description Extracellular => ECO:0000269|PubMed:18594507 source Swiss-Prot : SWS_FT_FI4 48) chain A residue 346-350 type TOPO_DOM sequence SPDFR description Extracellular => ECO:0000269|PubMed:18594507 source Swiss-Prot : SWS_FT_FI4 49) chain B residue 104-115 type TOPO_DOM sequence RGTWLWGSFLCE description Extracellular => ECO:0000269|PubMed:18594507 source Swiss-Prot : SWS_FT_FI4 50) chain B residue 180-205 type TOPO_DOM sequence HWWRDEDPQALKCYQDPGCCDFVTNR description Extracellular => ECO:0000269|PubMed:18594507 source Swiss-Prot : SWS_FT_FI4 51) chain B residue 316-320 type TOPO_DOM sequence NRDLV description Extracellular => ECO:0000269|PubMed:18594507 source Swiss-Prot : SWS_FT_FI4 52) chain A residue 127-143 type prosite sequence ASIETLCVIAIDRYLAI description G_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASIeTLCVIAIDRYLaI source prosite : PS00237 53) chain A residue 39-67 type TRANSMEM sequence QWEAGMSLLMALVVLLIVAGNVLVIAAIG description Helical; Name=1 source Swiss-Prot : SWS_FT_FI1 54) chain B residue 39-67 type TRANSMEM sequence QWEAGMSLLMALVVLLIVAGNVLVIAAIG description Helical; Name=1 source Swiss-Prot : SWS_FT_FI1 55) chain A residue 77-103 type TRANSMEM sequence NLFITSLACADLVVGLLVVPFGATLVV description Helical; Name=2 source Swiss-Prot : SWS_FT_FI3 56) chain B residue 77-103 type TRANSMEM sequence NLFITSLACADLVVGLLVVPFGATLVV description Helical; Name=2 source Swiss-Prot : SWS_FT_FI3 57) chain A residue 116-137 type TRANSMEM sequence LWTSLDVLCVTASIETLCVIAI description Helical; Name=3 source Swiss-Prot : SWS_FT_FI5 58) chain B residue 116-137 type TRANSMEM sequence LWTSLDVLCVTASIETLCVIAI description Helical; Name=3 source Swiss-Prot : SWS_FT_FI5 59) chain A residue 156-179 type TRANSMEM sequence ARAKVIICTVWAISALVSFLPIMM description Helical; Name=4 source Swiss-Prot : SWS_FT_FI6 60) chain B residue 156-179 type TRANSMEM sequence ARAKVIICTVWAISALVSFLPIMM description Helical; Name=4 source Swiss-Prot : SWS_FT_FI6 61) chain A residue 206-231 type TRANSMEM sequence AYAIASSIISFYIPLLIMIFVALRVY description Helical; Name=5 source Swiss-Prot : SWS_FT_FI7 62) chain B residue 206-231 type TRANSMEM sequence AYAIASSIISFYIPLLIMIFVALRVY description Helical; Name=5 source Swiss-Prot : SWS_FT_FI7 63) chain A residue 316-345 type TRANSMEM sequence NRDLVPDWLFVAFNWLGYANSAMNPIIYCR description Helical; Name=6 source Swiss-Prot : SWS_FT_FI8 64) chain B residue 286-315 type TRANSMEM sequence HKALKTLGIIMGVFTLCWLPFFLVNIVNVF description Helical; Name=6 source Swiss-Prot : SWS_FT_FI8 65) chain B residue 321-343 type TRANSMEM sequence PDWLFVAFNWLGYANSAMNPIIY description Helical; Name=7 source Swiss-Prot : SWS_FT_FI9 66) chain A residue 121 type BINDING sequence D description BINDING => ECO:0000269|PubMed:18594507, ECO:0007744|PDB:2VT4 source Swiss-Prot : SWS_FT_FI10 67) chain A residue 211 type BINDING sequence S description BINDING => ECO:0000269|PubMed:18594507, ECO:0007744|PDB:2VT4 source Swiss-Prot : SWS_FT_FI10 68) chain A residue 359 type BINDING sequence F description BINDING => ECO:0000269|PubMed:18594507, ECO:0007744|PDB:2VT4 source Swiss-Prot : SWS_FT_FI10 69) chain B residue 121 type BINDING sequence D description BINDING => ECO:0000269|PubMed:18594507, ECO:0007744|PDB:2VT4 source Swiss-Prot : SWS_FT_FI10 70) chain B residue 211 type BINDING sequence S description BINDING => ECO:0000269|PubMed:18594507, ECO:0007744|PDB:2VT4 source Swiss-Prot : SWS_FT_FI10 71) chain B residue 329 type BINDING sequence N description BINDING => ECO:0000269|PubMed:18594507, ECO:0007744|PDB:2VT4 source Swiss-Prot : SWS_FT_FI10 72) chain B residue 358 type LIPID sequence A description S-palmitoyl cysteine => ECO:0000250 source Swiss-Prot : SWS_FT_FI11 73) chain A residue 68-76 type TOPO_DOM sequence STQRLQTLT description Cytoplasmic => ECO:0000269|PubMed:18594507 source Swiss-Prot : SWS_FT_FI2 74) chain A residue 138-155 type TOPO_DOM sequence DRYLAITSPFRYQSLMTR description Cytoplasmic => ECO:0000269|PubMed:18594507 source Swiss-Prot : SWS_FT_FI2 75) chain A residue 232-315 type TOPO_DOM sequence REAKEQIRKIDRASKRKRVMLMREHKALKTLGIIMGVFTL CWLPFFLVNIVNVF description Cytoplasmic => ECO:0000269|PubMed:18594507 source Swiss-Prot : SWS_FT_FI2 76) chain B residue 68-76 type TOPO_DOM sequence STQRLQTLT description Cytoplasmic => ECO:0000269|PubMed:18594507 source Swiss-Prot : SWS_FT_FI2 77) chain B residue 138-155 type TOPO_DOM sequence DRYLAITSPFRYQSLMTR description Cytoplasmic => ECO:0000269|PubMed:18594507 source Swiss-Prot : SWS_FT_FI2 78) chain B residue 232-315 type TOPO_DOM sequence REAKEQIRKIDRASKRKRVMLMREHKALKTLGIIMGVFTL CWLPFFLVNIVNVF description Cytoplasmic => ECO:0000269|PubMed:18594507 source Swiss-Prot : SWS_FT_FI2

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