eF-site ID 5zkq-AB
PDB Code 5zkq
Chain A, B

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Title Crystal structure of the human platelet-activating factor receptor in complex with ABT-491
Classification SIGNALING PROTEIN
Compound Platelet-activating factor receptor,Endolysin,Endolysin,Platelet-activating factor receptor
Source (PTAFR_HUMAN)
Sequence A:  HDSSHMDSEFRYTLFPIVYSIIFVLGVIANGYVLWVFARL
FNEIKIFMVNLTMADMLFLITLPLWIVYYQNQGNWILPKF
LCNVAGCLFFINTYCSVAFLGVITYNRYQAVTRPQANTRK
RGISLSLVIWVAIVGAASYFLILDSTNTVPDSAGSGDVTR
CFEHYEKGSVPVLIIHIFIVFSFFLVFLIILFCNLVIIRT
LLMQPAEVKRRDLWMACTVLAVFIICFVPHHVVQLPWTLA
ELGFQDSKFHQAINDAHQVTLCLLSTNCVLNPVIYCFLT
B:  SHMDSEFRYTLFPIVYSIIFVLGVIANGYVLWVFARLYPF
NEIKIFMVNLTMADMLFLITLPLWIVYYQNQGNWILPKFL
CNVAGCLFFINTYCSVAFLGVITYNRYQAVTRPIQANTRK
RGISLSLVIWVAIVGAASYFLILDSTNTVPDSAGSGDVTR
CFEHYEKGSVPVLIIHIFIVFSFFLVFLIILFCNLVIIRT
LLMQPVNIFEMLRIDEGGGSGGDEEKLFNQDVDAAVRGIL
RNAKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSLR
MLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWD
AYAEVKRRDLWMACTVLAVFIICFVPHHVVQLPWTLAELG
FQDSKFHQAINDAHQVTLCLLSTNCVLNPVIYCFLTKKF
Description


Functional site

1) chain A
residue 22
type
sequence Y
description binding site for residue 9EU A 501
source : AC1

2) chain A
residue 73
type
sequence W
description binding site for residue 9EU A 501
source : AC1

3) chain A
residue 77
type
sequence Y
description binding site for residue 9EU A 501
source : AC1

4) chain A
residue 94
type
sequence G
description binding site for residue 9EU A 501
source : AC1

5) chain A
residue 97
type
sequence F
description binding site for residue 9EU A 501
source : AC1

6) chain A
residue 173
type
sequence C
description binding site for residue 9EU A 501
source : AC1

7) chain A
residue 174
type
sequence F
description binding site for residue 9EU A 501
source : AC1

8) chain A
residue 175
type
sequence E
description binding site for residue 9EU A 501
source : AC1

9) chain A
residue 177
type
sequence Y
description binding site for residue 9EU A 501
source : AC1

10) chain A
residue 188
type
sequence H
description binding site for residue 9EU A 501
source : AC1

11) chain A
residue 191
type
sequence I
description binding site for residue 9EU A 501
source : AC1

12) chain A
residue 252
type
sequence Q
description binding site for residue 9EU A 501
source : AC1

13) chain A
residue 279
type
sequence L
description binding site for residue 9EU A 501
source : AC1

14) chain A
residue 151
type
sequence Y
description binding site for residue OLC A 502
source : AC2

15) chain A
residue 152
type
sequence F
description binding site for residue OLC A 502
source : AC2

16) chain A
residue 178
type
sequence E
description binding site for residue OLC A 502
source : AC2

17) chain A
residue 183
type
sequence P
description binding site for residue OLC A 502
source : AC2

18) chain A
residue 190
type
sequence F
description binding site for residue OLC A 502
source : AC2

19) chain A
residue 151
type
sequence Y
description binding site for residue OLC A 503
source : AC3

20) chain A
residue 155
type
sequence L
description binding site for residue OLC A 503
source : AC3

21) chain A
residue 156
type
sequence D
description binding site for residue OLC A 503
source : AC3

22) chain A
residue 102
type
sequence Y
description binding site for residue OLC A 504
source : AC4

23) chain A
residue 143
type
sequence V
description binding site for residue OLC A 504
source : AC4

24) chain A
residue 144
type
sequence A
description binding site for residue OLC A 504
source : AC4

25) chain A
residue 145
type
sequence I
description binding site for residue OLC A 504
source : AC4

26) chain A
residue 194
type
sequence S
description binding site for residue OLC A 504
source : AC4

27) chain A
residue 153
type
sequence L
description binding site for residue OLC A 505
source : AC5

28) chain A
residue 4
type
sequence H
description binding site for residue ZN A 506
source : AC6

29) chain A
residue 8
type
sequence H
description binding site for residue ZN A 506
source : AC6

30) chain A
residue 259
type
sequence E
description binding site for residue ZN A 506
source : AC6

31) chain A
residue 268
type
sequence H
description binding site for residue ZN A 506
source : AC6

32) chain A
residue 272
type
sequence N
description binding site for residue ZN A 506
source : AC6

33) chain B
residue 22
type
sequence Y
description binding site for residue 9EU B 1201
source : AC7

34) chain B
residue 73
type
sequence W
description binding site for residue 9EU B 1201
source : AC7

35) chain B
residue 77
type
sequence Y
description binding site for residue 9EU B 1201
source : AC7

36) chain B
residue 94
type
sequence G
description binding site for residue 9EU B 1201
source : AC7

37) chain B
residue 97
type
sequence F
description binding site for residue 9EU B 1201
source : AC7

38) chain B
residue 98
type
sequence F
description binding site for residue 9EU B 1201
source : AC7

39) chain B
residue 152
type
sequence F
description binding site for residue 9EU B 1201
source : AC7

40) chain B
residue 173
type
sequence C
description binding site for residue 9EU B 1201
source : AC7

41) chain B
residue 174
type
sequence F
description binding site for residue 9EU B 1201
source : AC7

42) chain B
residue 175
type
sequence E
description binding site for residue 9EU B 1201
source : AC7

43) chain B
residue 177
type
sequence Y
description binding site for residue 9EU B 1201
source : AC7

44) chain B
residue 188
type
sequence H
description binding site for residue 9EU B 1201
source : AC7

45) chain B
residue 191
type
sequence I
description binding site for residue 9EU B 1201
source : AC7

46) chain B
residue 248
type
sequence H
description binding site for residue 9EU B 1201
source : AC7

47) chain B
residue 252
type
sequence Q
description binding site for residue 9EU B 1201
source : AC7

48) chain B
residue 181
type
sequence S
description binding site for residue OLC B 1202
source : AC8

49) chain B
residue 183
type
sequence P
description binding site for residue OLC B 1202
source : AC8

50) chain B
residue 184
type
sequence V
description binding site for residue OLC B 1202
source : AC8

51) chain B
residue 151
type
sequence Y
description binding site for residue OLC B 1203
source : AC9

52) chain B
residue 58
type
sequence N
description binding site for residue OLC B 1204
source : AD1

53) chain B
residue 61
type
sequence M
description binding site for residue OLC B 1204
source : AD1

54) chain B
residue 131
type
sequence R
description binding site for residue OLC B 1204
source : AD1

55) chain B
residue 135
type
sequence I
description binding site for residue OLC B 1204
source : AD1

56) chain B
residue 139
type
sequence L
description binding site for residue OLC B 1204
source : AD1

57) chain B
residue 142
type
sequence W
description binding site for residue OLC B 1204
source : AD1

58) chain B
residue 8
type
sequence H
description binding site for residue ZN B 1205
source : AD2

59) chain B
residue 259
type
sequence E
description binding site for residue ZN B 1205
source : AD2

60) chain B
residue 268
type
sequence H
description binding site for residue ZN B 1205
source : AD2

61) chain B
residue 272
type
sequence N
description binding site for residue ZN B 1205
source : AD2

62) chain B
residue 1062
type
sequence M
description binding site for residue SO4 B 1206
source : AD3

63) chain B
residue 166
type
sequence G
description binding site for residue SO4 B 1207
source : AD4

64) chain B
residue 1032
type
sequence R
description binding site for residue SO4 B 1207
source : AD4

65) chain B
residue 1036
type
sequence R
description binding site for residue SO4 B 1207
source : AD4

66) chain B
residue 1075
type
sequence R
description binding site for residue SO4 B 1208
source : AD5

67) chain B
residue 1081
type
sequence R
description binding site for residue SO4 B 1208
source : AD5

68) chain B
residue 1069
type
sequence G
description binding site for residue SO4 B 1209
source : AD6

69) chain B
residue 1098
type
sequence T
description binding site for residue SO4 B 1210
source : AD7

70) chain B
residue 1099
type
sequence P
description binding site for residue SO4 B 1210
source : AD7

71) chain B
residue 1100
type
sequence N
description binding site for residue SO4 B 1210
source : AD7

72) chain B
residue 1101
type
sequence R
description binding site for residue SO4 B 1210
source : AD7

73) chain B
residue 1066
type
sequence G
description binding site for residue SO4 B 1211
source : AD8

74) chain B
residue 1010
type catalytic
sequence E
description 921
source MCSA : MCSA2

75) chain A
residue 169
type CARBOHYD
sequence D
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI10

76) chain B
residue 169
type CARBOHYD
sequence D
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI10

77) chain B
residue 1060
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:8266098
source Swiss-Prot : SWS_FT_FI12

78) chain B
residue 1073
type BINDING
sequence S
description BINDING => ECO:0000303|PubMed:7831309
source Swiss-Prot : SWS_FT_FI13

79) chain B
residue 1088
type BINDING
sequence N
description BINDING => ECO:0000303|PubMed:7831309
source Swiss-Prot : SWS_FT_FI13

80) chain B
residue 1010
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_FI11

81) chain A
residue 39-54
type TOPO_DOM
sequence VFARLFNEIKI
description Cytoplasmic => ECO:0000255
source Swiss-Prot : SWS_FT_FI2

82) chain A
residue 114-133
type TOPO_DOM
sequence NRYQAVTRPQANTRKR
description Cytoplasmic => ECO:0000255
source Swiss-Prot : SWS_FT_FI2

83) chain B
residue 39-54
type TOPO_DOM
sequence VFARLYPFNEIKI
description Cytoplasmic => ECO:0000255
source Swiss-Prot : SWS_FT_FI2

84) chain B
residue 114-133
type TOPO_DOM
sequence NRYQAVTRPIQANTRKR
description Cytoplasmic => ECO:0000255
source Swiss-Prot : SWS_FT_FI2

85) chain A
residue 55-74
type TRANSMEM
sequence FMVNLTMADMLFLITLPLWI
description Helical; Name=2 => ECO:0000255
source Swiss-Prot : SWS_FT_FI3

86) chain B
residue 55-74
type TRANSMEM
sequence FMVNLTMADMLFLITLPLWI
description Helical; Name=2 => ECO:0000255
source Swiss-Prot : SWS_FT_FI3

87) chain A
residue 75-91
type TOPO_DOM
sequence VYYQNQGNWILPKFLCN
description Extracellular => ECO:0000255
source Swiss-Prot : SWS_FT_FI4

88) chain A
residue 156-184
type TOPO_DOM
sequence DSTNTVPDSAGSGDVTRCFEHYEKGSVPV
description Extracellular => ECO:0000255
source Swiss-Prot : SWS_FT_FI4

89) chain A
residue 255-276
type TOPO_DOM
sequence WTLAELGFQDSKFHQAINDAHQ
description Extracellular => ECO:0000255
source Swiss-Prot : SWS_FT_FI4

90) chain B
residue 75-91
type TOPO_DOM
sequence VYYQNQGNWILPKFLCN
description Extracellular => ECO:0000255
source Swiss-Prot : SWS_FT_FI4

91) chain B
residue 156-184
type TOPO_DOM
sequence DSTNTVPDSAGSGDVTRCFEHYEKGSVPV
description Extracellular => ECO:0000255
source Swiss-Prot : SWS_FT_FI4

92) chain B
residue 255-276
type TOPO_DOM
sequence WTLAELGFQDSKFHQAINDAHQ
description Extracellular => ECO:0000255
source Swiss-Prot : SWS_FT_FI4

93) chain A
residue 92-113
type TRANSMEM
sequence VAGCLFFINTYCSVAFLGVITY
description Helical; Name=3 => ECO:0000255
source Swiss-Prot : SWS_FT_FI5

94) chain B
residue 92-113
type TRANSMEM
sequence VAGCLFFINTYCSVAFLGVITY
description Helical; Name=3 => ECO:0000255
source Swiss-Prot : SWS_FT_FI5

95) chain A
residue 134-155
type TRANSMEM
sequence GISLSLVIWVAIVGAASYFLIL
description Helical; Name=4 => ECO:0000255
source Swiss-Prot : SWS_FT_FI6

96) chain B
residue 134-155
type TRANSMEM
sequence GISLSLVIWVAIVGAASYFLIL
description Helical; Name=4 => ECO:0000255
source Swiss-Prot : SWS_FT_FI6

97) chain A
residue 185-205
type TRANSMEM
sequence LIIHIFIVFSFFLVFLIILFC
description Helical; Name=5 => ECO:0000255
source Swiss-Prot : SWS_FT_FI7

98) chain B
residue 185-205
type TRANSMEM
sequence LIIHIFIVFSFFLVFLIILFC
description Helical; Name=5 => ECO:0000255
source Swiss-Prot : SWS_FT_FI7

99) chain A
residue 234-254
type TRANSMEM
sequence ACTVLAVFIICFVPHHVVQLP
description Helical; Name=6 => ECO:0000255
source Swiss-Prot : SWS_FT_FI8

100) chain B
residue 234-254
type TRANSMEM
sequence ACTVLAVFIICFVPHHVVQLP
description Helical; Name=6 => ECO:0000255
source Swiss-Prot : SWS_FT_FI8

101) chain A
residue 277-296
type TRANSMEM
sequence VTLCLLSTNCVLNPVIYCFL
description Helical; Name=7 => ECO:0000255
source Swiss-Prot : SWS_FT_FI9

102) chain B
residue 277-296
type TRANSMEM
sequence VTLCLLSTNCVLNPVIYCFL
description Helical; Name=7 => ECO:0000255
source Swiss-Prot : SWS_FT_FI9

103) chain A
residue 17-38
type TRANSMEM
sequence LFPIVYSIIFVLGVIANGYVLW
description Helical; Name=1 => ECO:0000255
source Swiss-Prot : SWS_FT_FI1

104) chain B
residue 17-38
type TRANSMEM
sequence LFPIVYSIIFVLGVIANGYVLW
description Helical; Name=1 => ECO:0000255
source Swiss-Prot : SWS_FT_FI1

105) chain A
residue 103-119
type prosite
sequence CSVAFLGVITYNRYQAV
description G_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. CSVaFLGVITYNRYQaV
source prosite : PS00237


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