eF-site ID 6e67-AB
PDB Code 6e67
Chain A, B

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Title Structure of beta2 adrenergic receptor fused to a Gs peptide
Classification MEMBRANE PROTEIN
Compound Beta-2 adrenergic receptor,Endolysin,Guanine nucleotide-binding protein G(s) subunit alpha isoforms short,Beta-2 adrenergic receptor chimera
Source (ADRB2_HUMAN)
Sequence A:  DEVWVVGMGIVMSLIVLAIVFGNVLVITAIAKFERLQTVT
NYFITSLACADLVMGLAVVPFGAAHILTKTWTFGNFWCEF
WTSIDVLCVTASIETLCVIAVDRYFAITSPFKYQSLLTKN
KARVIILMVWIVSGLTSFLPIQMHWYRATHQEAINCYAEE
TCCDFFTNQAYAIASSIVSFYVPLVIMVFVYSRVFQECKR
QLQKNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSP
SLNAAKSELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRG
ILRNAKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNS
LRMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGT
WDAYDIIQRMHLRQYELCGTGEHKALKTLGIIMGTFTLCW
LPFFIVNIVHVIQDNLIRKEVYILLNWIGYVNSGFNPLIY
CRSPDFRIAFQELLCLR
B:  FLLAPNRSHAPDHDVTQQRDEVWVVGMGIVMSLIVLAIVF
GNVLVITAIAKFERLQTVTNYFITSLACADLVMGLAVVPF
GAAHILTKTWTFGNFWCEFWTSIDVLCVTASIETLCVIAV
DRYFAITSPFKYQSLLTKNKARVIILMVWIVSGLTSFLPI
QMHWYRATHQEAINCYAEETCCDFFTNQAYAIASSIVSFY
VPLVIMVFVYSRVFQECKRQLQKNIFEMLRIDEGLRLKIY
KDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNTNGVI
TKDEAEKLFNQDVDAAVRGILRNAKLKPVYDSLDAVRRAA
LINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSRW
YNQTPNRAKRVITTFRTGTWDAYDIIQRMHLRQYELCGTG
EHKALKTLGIIMGTFTLCWLPFFIVNIVHVIQDNLIRKEV
YILLNWIGYVNSGFNPLIYCRSPDFRIAFQELLCLR
Description


Functional site

1) chain A
residue 109
type
sequence W
description binding site for residue P0G A 3101
source : AC1

2) chain A
residue 110
type
sequence T
description binding site for residue P0G A 3101
source : AC1

3) chain A
residue 113
type
sequence D
description binding site for residue P0G A 3101
source : AC1

4) chain A
residue 114
type
sequence V
description binding site for residue P0G A 3101
source : AC1

5) chain A
residue 193
type
sequence F
description binding site for residue P0G A 3101
source : AC1

6) chain A
residue 200
type
sequence A
description binding site for residue P0G A 3101
source : AC1

7) chain A
residue 203
type
sequence S
description binding site for residue P0G A 3101
source : AC1

8) chain A
residue 204
type
sequence S
description binding site for residue P0G A 3101
source : AC1

9) chain A
residue 207
type
sequence S
description binding site for residue P0G A 3101
source : AC1

10) chain A
residue 293
type
sequence N
description binding site for residue P0G A 3101
source : AC1

11) chain A
residue 308
type
sequence Y
description binding site for residue P0G A 3101
source : AC1

12) chain A
residue 309
type
sequence I
description binding site for residue P0G A 3101
source : AC1

13) chain A
residue 312
type
sequence N
description binding site for residue P0G A 3101
source : AC1

14) chain B
residue 109
type
sequence W
description binding site for residue P0G B 3101
source : AC2

15) chain B
residue 113
type
sequence D
description binding site for residue P0G B 3101
source : AC2

16) chain B
residue 117
type
sequence V
description binding site for residue P0G B 3101
source : AC2

17) chain B
residue 193
type
sequence F
description binding site for residue P0G B 3101
source : AC2

18) chain B
residue 200
type
sequence A
description binding site for residue P0G B 3101
source : AC2

19) chain B
residue 203
type
sequence S
description binding site for residue P0G B 3101
source : AC2

20) chain B
residue 207
type
sequence S
description binding site for residue P0G B 3101
source : AC2

21) chain B
residue 293
type
sequence N
description binding site for residue P0G B 3101
source : AC2

22) chain B
residue 308
type
sequence Y
description binding site for residue P0G B 3101
source : AC2

23) chain B
residue 309
type
sequence I
description binding site for residue P0G B 3101
source : AC2

24) chain B
residue 312
type
sequence N
description binding site for residue P0G B 3101
source : AC2

25) chain A
residue 96-106
type TOPO_DOM
sequence TKTWTFGNFWC
description Extracellular
source Swiss-Prot : SWS_FT_FI1

26) chain A
residue 175-196
type TOPO_DOM
sequence RATHQEAINCYAEETCCDFFTN
description Extracellular
source Swiss-Prot : SWS_FT_FI1

27) chain A
residue 299-305
type TOPO_DOM
sequence QDNLIRK
description Extracellular
source Swiss-Prot : SWS_FT_FI1

28) chain B
residue 96-106
type TOPO_DOM
sequence TKTWTFGNFWC
description Extracellular
source Swiss-Prot : SWS_FT_FI1

29) chain B
residue 175-196
type TOPO_DOM
sequence RATHQEAINCYAEETCCDFFTN
description Extracellular
source Swiss-Prot : SWS_FT_FI1

30) chain B
residue 299-305
type TOPO_DOM
sequence QDNLIRK
description Extracellular
source Swiss-Prot : SWS_FT_FI1

31) chain A
residue 35-58
type TRANSMEM
sequence GMGIVMSLIVLAIVFGNVLVITAI
description Helical; Name=1
source Swiss-Prot : SWS_FT_FI2

32) chain B
residue 35-58
type TRANSMEM
sequence GMGIVMSLIVLAIVFGNVLVITAI
description Helical; Name=1
source Swiss-Prot : SWS_FT_FI2

33) chain A
residue 59-71
type TOPO_DOM
sequence AKFERLQTVTNYF
description Cytoplasmic
source Swiss-Prot : SWS_FT_FI3

34) chain A
residue 130-150
type TOPO_DOM
sequence DRYFAITSPFKYQSLLTKNKA
description Cytoplasmic
source Swiss-Prot : SWS_FT_FI3

35) chain B
residue 59-71
type TOPO_DOM
sequence AKFERLQTVTNYF
description Cytoplasmic
source Swiss-Prot : SWS_FT_FI3

36) chain B
residue 130-150
type TOPO_DOM
sequence DRYFAITSPFKYQSLLTKNKA
description Cytoplasmic
source Swiss-Prot : SWS_FT_FI3

37) chain A
residue 72-95
type TRANSMEM
sequence ITSLACADLVMGLAVVPFGAAHIL
description Helical; Name=2
source Swiss-Prot : SWS_FT_FI4

38) chain B
residue 72-95
type TRANSMEM
sequence ITSLACADLVMGLAVVPFGAAHIL
description Helical; Name=2
source Swiss-Prot : SWS_FT_FI4

39) chain A
residue 107-129
type TRANSMEM
sequence EFWTSIDVLCVTASIETLCVIAV
description Helical; Name=3
source Swiss-Prot : SWS_FT_FI5

40) chain B
residue 107-129
type TRANSMEM
sequence EFWTSIDVLCVTASIETLCVIAV
description Helical; Name=3
source Swiss-Prot : SWS_FT_FI5

41) chain A
residue 151-174
type TRANSMEM
sequence RVIILMVWIVSGLTSFLPIQMHWY
description Helical; Name=4
source Swiss-Prot : SWS_FT_FI6

42) chain B
residue 151-174
type TRANSMEM
sequence RVIILMVWIVSGLTSFLPIQMHWY
description Helical; Name=4
source Swiss-Prot : SWS_FT_FI6

43) chain A
residue 197-220
type TRANSMEM
sequence QAYAIASSIVSFYVPLVIMVFVYS
description Helical; Name=5
source Swiss-Prot : SWS_FT_FI7

44) chain B
residue 197-220
type TRANSMEM
sequence QAYAIASSIVSFYVPLVIMVFVYS
description Helical; Name=5
source Swiss-Prot : SWS_FT_FI7

45) chain A
residue 275-298
type TRANSMEM
sequence LGIIMGTFTLCWLPFFIVNIVHVI
description Helical; Name=6
source Swiss-Prot : SWS_FT_FI8

46) chain B
residue 275-298
type TRANSMEM
sequence LGIIMGTFTLCWLPFFIVNIVHVI
description Helical; Name=6
source Swiss-Prot : SWS_FT_FI8

47) chain A
residue 306-329
type TRANSMEM
sequence EVYILLNWIGYVNSGFNPLIYCRS
description Helical; Name=7
source Swiss-Prot : SWS_FT_FI9

48) chain B
residue 306-329
type TRANSMEM
sequence EVYILLNWIGYVNSGFNPLIYCRS
description Helical; Name=7
source Swiss-Prot : SWS_FT_FI9

49) chain A
residue 113
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:18547522, ECO:0007744|PDB:3D4S
source Swiss-Prot : SWS_FT_FI10

50) chain B
residue 316
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:18547522, ECO:0007744|PDB:3D4S
source Swiss-Prot : SWS_FT_FI10

51) chain A
residue 118
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:18547522, ECO:0007744|PDB:3D4S
source Swiss-Prot : SWS_FT_FI10

52) chain A
residue 293
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:18547522, ECO:0007744|PDB:3D4S
source Swiss-Prot : SWS_FT_FI10

53) chain A
residue 312
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:18547522, ECO:0007744|PDB:3D4S
source Swiss-Prot : SWS_FT_FI10

54) chain A
residue 316
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:18547522, ECO:0007744|PDB:3D4S
source Swiss-Prot : SWS_FT_FI10

55) chain B
residue 113
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:18547522, ECO:0007744|PDB:3D4S
source Swiss-Prot : SWS_FT_FI10

56) chain B
residue 118
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:18547522, ECO:0007744|PDB:3D4S
source Swiss-Prot : SWS_FT_FI10

57) chain B
residue 293
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:18547522, ECO:0007744|PDB:3D4S
source Swiss-Prot : SWS_FT_FI10

58) chain B
residue 312
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:18547522, ECO:0007744|PDB:3D4S
source Swiss-Prot : SWS_FT_FI10

59) 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

60) chain B
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

61) chain A
residue 141
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000269|PubMed:8521811
source Swiss-Prot : SWS_FT_FI12

62) chain B
residue 141
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000269|PubMed:8521811
source Swiss-Prot : SWS_FT_FI12

63) 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_FI15

64) chain B
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_FI15

65) chain B
residue 15
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000305
source Swiss-Prot : SWS_FT_FI16

66) 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


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