eF-site ID 4rwa-AB
PDB Code 4rwa
Chain A, B

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Title Synchrotron structure of the human delta opioid receptor in complex with a bifunctional peptide (PSI community target)
Classification MEMBRANE PROTEIN
Compound Soluble cytochrome b562,Delta-type opioid receptor
Source (4RWA)
Sequence A:  DLEDNWETLNDNLKVIEKADNAAQVKDALTKMRAAALDAQ
KATPPKLEDKSPDSPEMKDFRHGFDILVGQIDDALKLANE
GKVKEAQAAAEQLKTTRNAYIQKYLGARSASSLALAIAIT
ALYSAVCAVGLLGNVLVMFGIVRYTKMKTATNIYIFNLAL
ADALATSTLPFQSAKYLMETWPFGELLCKAVLSIDYYNMF
TSIFTLTMMSVDRYIAVCHPVKALDFRTPAKAKLINICIW
VLASGVGVPIMVMAVTRPRDGAVVCMLQFPSPSWYWDTVT
KICVFLFAFVVPILIITVCYGLMLLGSKEKDRSLRRITRM
VLVVVGAFVVCWAPIHIFVIVWTLVDIDRRDPLVVAALHL
CIALGYANSSLNPVLYAFLDENFKRCFRQLC
B:  DLEDNWETLNDNLKVIEKADNAAQVKDALTKMRAAALDAQ
KATPPKLEDKSPDSPEMKDFRHGFDILVGQIDDALKLANE
GKVKEAQAAAEQLKTTRNAYIQKYLGARSASSLALAIAIT
ALYSAVCAVGLLGNVLVMFGIVRYTKMKTATNIYIFNLAL
ADALATSTLPFQSAKYLMETWPFGELLCKAVLSIDYYNMF
TSIFTLTMMSVDRYIAVCHPVKALDFRTPAKAKLINICIW
VLASGVGVPIMVMAVTRPRDGAVVCMLQFPSPSWYWDTVT
KICVFLFAFVVPILIITVCYGLMLLRGSKEKDRSLRRITR
MVLVVVGAFVVCWAPIHIFVIVWTLVDIDRRDPLVVAALH
LCIALGYANSSLNPVLYAFLDENFKRCFR
Description


Functional site

1) chain A
residue 137
type
sequence F
description BINDING SITE FOR RESIDUE OLC A 1201
source : AC1

2) chain A
residue 141
type
sequence M
description BINDING SITE FOR RESIDUE OLC A 1201
source : AC1

3) chain A
residue 171
type
sequence C
description BINDING SITE FOR RESIDUE OLC A 1201
source : AC1

4) chain A
residue 172
type
sequence I
description BINDING SITE FOR RESIDUE OLC A 1201
source : AC1

5) chain A
residue 225
type
sequence P
description BINDING SITE FOR RESIDUE OLC A 1201
source : AC1

6) chain B
residue 125
type
sequence L
description BINDING SITE FOR CHAIN G OF BIFUNCTIONAL PEPTIDE
source : AC2

7) chain B
residue 128
type
sequence D
description BINDING SITE FOR CHAIN G OF BIFUNCTIONAL PEPTIDE
source : AC2

8) chain B
residue 129
type
sequence Y
description BINDING SITE FOR CHAIN G OF BIFUNCTIONAL PEPTIDE
source : AC2

9) chain B
residue 132
type
sequence M
description BINDING SITE FOR CHAIN G OF BIFUNCTIONAL PEPTIDE
source : AC2

10) chain B
residue 217
type
sequence V
description BINDING SITE FOR CHAIN G OF BIFUNCTIONAL PEPTIDE
source : AC2

11) chain B
residue 281
type
sequence V
description BINDING SITE FOR CHAIN G OF BIFUNCTIONAL PEPTIDE
source : AC2

12) chain B
residue 284
type
sequence W
description BINDING SITE FOR CHAIN G OF BIFUNCTIONAL PEPTIDE
source : AC2

13) chain B
residue 304
type
sequence I
description BINDING SITE FOR CHAIN G OF BIFUNCTIONAL PEPTIDE
source : AC2

14) chain B
residue 308
type
sequence Y
description BINDING SITE FOR CHAIN G OF BIFUNCTIONAL PEPTIDE
source : AC2

15) chain A
residue 125
type
sequence L
description BINDING SITE FOR CHAIN H OF BIFUNCTIONAL PEPTIDE
source : AC3

16) chain A
residue 128
type
sequence D
description BINDING SITE FOR CHAIN H OF BIFUNCTIONAL PEPTIDE
source : AC3

17) chain A
residue 129
type
sequence Y
description BINDING SITE FOR CHAIN H OF BIFUNCTIONAL PEPTIDE
source : AC3

18) chain A
residue 132
type
sequence M
description BINDING SITE FOR CHAIN H OF BIFUNCTIONAL PEPTIDE
source : AC3

19) chain A
residue 199
type
sequence M
description BINDING SITE FOR CHAIN H OF BIFUNCTIONAL PEPTIDE
source : AC3

20) chain A
residue 200
type
sequence L
description BINDING SITE FOR CHAIN H OF BIFUNCTIONAL PEPTIDE
source : AC3

21) chain A
residue 217
type
sequence V
description BINDING SITE FOR CHAIN H OF BIFUNCTIONAL PEPTIDE
source : AC3

22) chain A
residue 277
type
sequence I
description BINDING SITE FOR CHAIN H OF BIFUNCTIONAL PEPTIDE
source : AC3

23) chain A
residue 281
type
sequence V
description BINDING SITE FOR CHAIN H OF BIFUNCTIONAL PEPTIDE
source : AC3

24) chain A
residue 304
type
sequence I
description BINDING SITE FOR CHAIN H OF BIFUNCTIONAL PEPTIDE
source : AC3

25) chain A
residue 308
type
sequence Y
description BINDING SITE FOR CHAIN H OF BIFUNCTIONAL PEPTIDE
source : AC3

26) chain A
residue 48-75
type TRANSMEM
sequence LAIAITALYSAVCAVGLLGNVLVMFGIV
description Helical; Name=1 => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

27) chain B
residue 48-75
type TRANSMEM
sequence LAIAITALYSAVCAVGLLGNVLVMFGIV
description Helical; Name=1 => ECO:0000250
source Swiss-Prot : SWS_FT_FI2

28) chain A
residue 76-85
type TOPO_DOM
sequence RYTKMKTATN
description Cytoplasmic => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

29) chain A
residue 145-163
type TOPO_DOM
sequence DRYIAVCHPVKALDFRTPA
description Cytoplasmic => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

30) chain B
residue 76-85
type TOPO_DOM
sequence RYTKMKTATN
description Cytoplasmic => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

31) chain B
residue 145-163
type TOPO_DOM
sequence DRYIAVCHPVKALDFRTPA
description Cytoplasmic => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

32) chain B
residue 239-261
type TOPO_DOM
sequence RGSKEKDRSLRRITR
description Cytoplasmic => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

33) chain A
residue 86-110
type TRANSMEM
sequence IYIFNLALADALATSTLPFQSAKYL
description Helical; Name=2 => ECO:0000250
source Swiss-Prot : SWS_FT_FI4

34) chain B
residue 86-110
type TRANSMEM
sequence IYIFNLALADALATSTLPFQSAKYL
description Helical; Name=2 => ECO:0000250
source Swiss-Prot : SWS_FT_FI4

35) chain A
residue 111-122
type TOPO_DOM
sequence METWPFGELLCK
description Extracellular => ECO:0000250
source Swiss-Prot : SWS_FT_FI5

36) chain A
residue 187-206
type TOPO_DOM
sequence AVTRPRDGAVVCMLQFPSPS
description Extracellular => ECO:0000250
source Swiss-Prot : SWS_FT_FI5

37) chain A
residue 285-299
type TOPO_DOM
sequence TLVDIDRRDPLVVAA
description Extracellular => ECO:0000250
source Swiss-Prot : SWS_FT_FI5

38) chain B
residue 111-122
type TOPO_DOM
sequence METWPFGELLCK
description Extracellular => ECO:0000250
source Swiss-Prot : SWS_FT_FI5

39) chain B
residue 187-206
type TOPO_DOM
sequence AVTRPRDGAVVCMLQFPSPS
description Extracellular => ECO:0000250
source Swiss-Prot : SWS_FT_FI5

40) chain B
residue 285-299
type TOPO_DOM
sequence TLVDIDRRDPLVVAA
description Extracellular => ECO:0000250
source Swiss-Prot : SWS_FT_FI5

41) chain A
residue 123-144
type TRANSMEM
sequence AVLSIDYYNMFTSIFTLTMMSV
description Helical; Name=3 => ECO:0000250
source Swiss-Prot : SWS_FT_FI6

42) chain B
residue 123-144
type TRANSMEM
sequence AVLSIDYYNMFTSIFTLTMMSV
description Helical; Name=3 => ECO:0000250
source Swiss-Prot : SWS_FT_FI6

43) chain A
residue 164-186
type TRANSMEM
sequence KAKLINICIWVLASGVGVPIMVM
description Helical; Name=4 => ECO:0000250
source Swiss-Prot : SWS_FT_FI7

44) chain B
residue 164-186
type TRANSMEM
sequence KAKLINICIWVLASGVGVPIMVM
description Helical; Name=4 => ECO:0000250
source Swiss-Prot : SWS_FT_FI7

45) chain A
residue 207-238
type TRANSMEM
sequence WYWDTVTKICVFLFAFVVPILIITVCYGLMLL
description Helical; Name=5 => ECO:0000250
source Swiss-Prot : SWS_FT_FI8

46) chain B
residue 207-238
type TRANSMEM
sequence WYWDTVTKICVFLFAFVVPILIITVCYGLMLL
description Helical; Name=5 => ECO:0000250
source Swiss-Prot : SWS_FT_FI8

47) chain A
residue 262-284
type TRANSMEM
sequence MVLVVVGAFVVCWAPIHIFVIVW
description Helical; Name=6 => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

48) chain B
residue 262-284
type TRANSMEM
sequence MVLVVVGAFVVCWAPIHIFVIVW
description Helical; Name=6 => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

49) chain A
residue 300-321
type TRANSMEM
sequence LHLCIALGYANSSLNPVLYAFL
description Helical; Name=7 => ECO:0000250
source Swiss-Prot : SWS_FT_FI10

50) chain B
residue 300-321
type TRANSMEM
sequence LHLCIALGYANSSLNPVLYAFL
description Helical; Name=7 => ECO:0000250
source Swiss-Prot : SWS_FT_FI10

51) chain A
residue 333
type LIPID
sequence C
description S-palmitoyl cysteine => ECO:0000255
source Swiss-Prot : SWS_FT_FI11

52) chain A
residue 134-150
type prosite
sequence TSIFTLTMMSVDRYIAV
description G_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. TSIfTLTMMSVDRYIaV
source prosite : PS00237

53) chain A
residue 1007
type BINDING
sequence W
description axial binding residue
source Swiss-Prot : SWS_FT_FI1

54) chain A
residue 1102
type BINDING
sequence I
description axial binding residue
source Swiss-Prot : SWS_FT_FI1

55) chain B
residue 1007
type BINDING
sequence W
description axial binding residue
source Swiss-Prot : SWS_FT_FI1

56) chain B
residue 1102
type BINDING
sequence I
description axial binding residue
source Swiss-Prot : SWS_FT_FI1


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