eF-site ID 3vw7-A
PDB Code 3vw7
Chain A

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Title Crystal structure of human protease-activated receptor 1 (PAR1) bound with antagonist vorapaxar at 2.2 angstrom
Classification Signaling protein/antagonist
Compound Proteinase-activated receptor 1, Lysozyme
Source Homo sapiens (Human) (PAR1_HUMAN)
Sequence A:  DASGYLTSSWLTLFVPSVYTGVFVVSLPLNIMAIVVFILK
MKVKKPAVVYMLHLATADVLFVSVLPFKISYYFSGSDWQF
GSELCRFVTAAFYCNMYASILLMTVISIDRFLAVVYPMRT
LGRASFTCLAIWALAIAGVVPLLLKEQTIQVPGLGITTCH
DVLSETLLEGYYAYYFSAFSAVFFFVPLIISTVCYVSIIR
CLSSSANIFEMLRIDEGLRLKIYKNTEGYYTIGIGHLLTK
SPSLNAAKSELDKAIGRNTNGVITKDEAEKLFNQDVDAAV
RGILRNAKLKPVYDSLDAVRRAALINMVFQMGETGVAGFT
NSLRMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRT
GTWDAYANRSKKSRALFLSAAVFCIFIICFGPTNVLLIAH
YSFLSHTSTTEAAYFAYLLCVCVSSISCCIDPLIYYYASS
EC
Description


Functional site

1) chain A
residue 183
type
sequence Y
description BINDING SITE FOR RESIDUE VPX A 2001
source : AC1

2) chain A
residue 187
type
sequence Y
description BINDING SITE FOR RESIDUE VPX A 2001
source : AC1

3) chain A
residue 236
type
sequence P
description BINDING SITE FOR RESIDUE VPX A 2001
source : AC1

4) chain A
residue 255
type
sequence H
description BINDING SITE FOR RESIDUE VPX A 2001
source : AC1

5) chain A
residue 256
type
sequence D
description BINDING SITE FOR RESIDUE VPX A 2001
source : AC1

6) chain A
residue 257
type
sequence V
description BINDING SITE FOR RESIDUE VPX A 2001
source : AC1

7) chain A
residue 258
type
sequence L
description BINDING SITE FOR RESIDUE VPX A 2001
source : AC1

8) chain A
residue 271
type
sequence F
description BINDING SITE FOR RESIDUE VPX A 2001
source : AC1

9) chain A
residue 1080
type
sequence R
description BINDING SITE FOR RESIDUE VPX A 2001
source : AC1

10) chain A
residue 332
type
sequence L
description BINDING SITE FOR RESIDUE VPX A 2001
source : AC1

11) chain A
residue 333
type
sequence L
description BINDING SITE FOR RESIDUE VPX A 2001
source : AC1

12) chain A
residue 337
type
sequence Y
description BINDING SITE FOR RESIDUE VPX A 2001
source : AC1

13) chain A
residue 349
type
sequence A
description BINDING SITE FOR RESIDUE VPX A 2001
source : AC1

14) chain A
residue 350
type
sequence Y
description BINDING SITE FOR RESIDUE VPX A 2001
source : AC1

15) chain A
residue 353
type
sequence Y
description BINDING SITE FOR RESIDUE VPX A 2001
source : AC1

16) chain A
residue 157
type
sequence F
description BINDING SITE FOR RESIDUE OLC A 2002
source : AC2

17) chain A
residue 206
type
sequence Y
description BINDING SITE FOR RESIDUE OLC A 2002
source : AC2

18) chain A
residue 284
type
sequence I
description BINDING SITE FOR RESIDUE OLC A 2002
source : AC2

19) chain A
residue 295
type
sequence R
description BINDING SITE FOR RESIDUE OLC A 2002
source : AC2

20) chain A
residue 160
type
sequence S
description BINDING SITE FOR RESIDUE OLC A 2003
source : AC3

21) chain A
residue 164
type
sequence S
description BINDING SITE FOR RESIDUE OLC A 2003
source : AC3

22) chain A
residue 113
type
sequence F
description BINDING SITE FOR RESIDUE OLC A 2004
source : AC4

23) chain A
residue 156
type
sequence P
description BINDING SITE FOR RESIDUE OLC A 2004
source : AC4

24) chain A
residue 160
type
sequence S
description BINDING SITE FOR RESIDUE OLC A 2004
source : AC4

25) chain A
residue 163
type
sequence F
description BINDING SITE FOR RESIDUE OLC A 2004
source : AC4

26) chain A
residue 164
type
sequence S
description BINDING SITE FOR RESIDUE OLC A 2004
source : AC4

27) chain A
residue 202
type
sequence L
description BINDING SITE FOR RESIDUE OLC A 2004
source : AC4

28) chain A
residue 229
type
sequence L
description BINDING SITE FOR RESIDUE OLC A 2004
source : AC4

29) chain A
residue 278
type
sequence F
description BINDING SITE FOR RESIDUE OLC A 2004
source : AC4

30) chain A
residue 122
type
sequence M
description BINDING SITE FOR RESIDUE OLC A 2005
source : AC5

31) chain A
residue 126
type
sequence V
description BINDING SITE FOR RESIDUE OLC A 2005
source : AC5

32) chain A
residue 127
type
sequence F
description BINDING SITE FOR RESIDUE OLC A 2005
source : AC5

33) chain A
residue 365
type
sequence C
description BINDING SITE FOR RESIDUE OLC A 2005
source : AC5

34) chain A
residue 368
type
sequence P
description BINDING SITE FOR RESIDUE OLC A 2005
source : AC5

35) chain A
residue 371
type
sequence Y
description BINDING SITE FOR RESIDUE OLC A 2005
source : AC5

36) chain A
residue 372
type
sequence Y
description BINDING SITE FOR RESIDUE OLC A 2005
source : AC5

37) chain A
residue 375
type
sequence S
description BINDING SITE FOR RESIDUE OLC A 2005
source : AC5

38) chain A
residue 100
type
sequence W
description BINDING SITE FOR RESIDUE OLC A 2006
source : AC6

39) chain A
residue 328
type
sequence P
description BINDING SITE FOR RESIDUE OLC A 2006
source : AC6

40) chain A
residue 348
type
sequence A
description BINDING SITE FOR RESIDUE OLC A 2006
source : AC6

41) chain A
residue 351
type
sequence F
description BINDING SITE FOR RESIDUE OLC A 2006
source : AC6

42) chain A
residue 356
type
sequence C
description BINDING SITE FOR RESIDUE OLC A 2006
source : AC6

43) chain A
residue 327
type
sequence G
description BINDING SITE FOR RESIDUE OLC A 2007
source : AC7

44) chain A
residue 328
type
sequence P
description BINDING SITE FOR RESIDUE OLC A 2007
source : AC7

45) chain A
residue 343
type
sequence T
description BINDING SITE FOR RESIDUE OLC A 2007
source : AC7

46) chain A
residue 346
type
sequence T
description BINDING SITE FOR RESIDUE OLC A 2007
source : AC7

47) chain A
residue 348
type
sequence A
description BINDING SITE FOR RESIDUE OLC A 2007
source : AC7

48) chain A
residue 356
type
sequence C
description BINDING SITE FOR RESIDUE OLC A 2007
source : AC7

49) chain A
residue 139
type
sequence V
description BINDING SITE FOR RESIDUE OLC A 2008
source : AC8

50) chain A
residue 143
type
sequence H
description BINDING SITE FOR RESIDUE OLC A 2008
source : AC8

51) chain A
residue 220
type
sequence S
description BINDING SITE FOR RESIDUE OLC A 2008
source : AC8

52) chain A
residue 224
type
sequence L
description BINDING SITE FOR RESIDUE OLC A 2008
source : AC8

53) chain A
residue 228
type
sequence A
description BINDING SITE FOR RESIDUE OLC A 2008
source : AC8

54) chain A
residue 236
type
sequence P
description BINDING SITE FOR RESIDUE OLC A 2009
source : AC9

55) chain A
residue 240
type
sequence K
description BINDING SITE FOR RESIDUE OLC A 2009
source : AC9

56) chain A
residue 270
type
sequence Y
description BINDING SITE FOR RESIDUE OLC A 2009
source : AC9

57) chain A
residue 271
type
sequence F
description BINDING SITE FOR RESIDUE OLC A 2009
source : AC9

58) chain A
residue 163
type
sequence F
description BINDING SITE FOR RESIDUE OLC A 2010
source : BC1

59) chain A
residue 221
type
sequence F
description BINDING SITE FOR RESIDUE OLC A 2010
source : BC1

60) chain A
residue 222
type
sequence T
description BINDING SITE FOR RESIDUE OLC A 2010
source : BC1

61) chain A
residue 135
type
sequence K
description BINDING SITE FOR RESIDUE CL A 2011
source : BC2

62) chain A
residue 307
type
sequence K
description BINDING SITE FOR RESIDUE CL A 2011
source : BC2

63) chain A
residue 144
type
sequence L
description BINDING SITE FOR RESIDUE NA A 2012
source : BC3

64) chain A
residue 148
type
sequence D
description BINDING SITE FOR RESIDUE NA A 2012
source : BC3

65) chain A
residue 189
type
sequence S
description BINDING SITE FOR RESIDUE NA A 2012
source : BC3

66) chain A
residue 367
type
sequence D
description BINDING SITE FOR RESIDUE NA A 2012
source : BC3

67) chain A
residue 1011
type catalytic
sequence E
description 921
source MCSA : MCSA1

68) chain A
residue 1020
type catalytic
sequence N
description 921
source MCSA : MCSA1

69) chain A
residue 250
type CARBOHYD
sequence G
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI10

70) chain A
residue 259
type CARBOHYD
sequence S
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI10

71) chain A
residue 1117
type BINDING
sequence S
description BINDING => ECO:0000303|PubMed:7831309
source Swiss-Prot : SWS_FT_FI14

72) chain A
residue 1132
type BINDING
sequence N
description BINDING => ECO:0000303|PubMed:7831309
source Swiss-Prot : SWS_FT_FI14

73) chain A
residue 1011
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

74) chain A
residue 1020
type ACT_SITE
sequence N
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_FI12

75) chain A
residue 312-334
type TRANSMEM
sequence LFLSAAVFCIFIICFGPTNVLLI
description Helical; Name=6 => ECO:0000255
source Swiss-Prot : SWS_FT_FI8

76) chain A
residue 1032
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:8266098
source Swiss-Prot : SWS_FT_FI13

77) chain A
residue 1104
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:8266098
source Swiss-Prot : SWS_FT_FI13

78) chain A
residue 351-374
type TRANSMEM
sequence FAYLLCVCVSSISCCIDPLIYYYA
description Helical; Name=7 => ECO:0000255
source Swiss-Prot : SWS_FT_FI9

79) chain A
residue 103-128
type TRANSMEM
sequence LFVPSVYTGVFVVSLPLNIMAIVVFI
description Helical; Name=1 => ECO:0000255
source Swiss-Prot : SWS_FT_FI1

80) chain A
residue 129-137
type TOPO_DOM
sequence LKMKVKKPA
description Cytoplasmic => ECO:0000255
source Swiss-Prot : SWS_FT_FI2

81) chain A
residue 199-218
type TOPO_DOM
sequence DRFLAVVYPMRTLGR
description Cytoplasmic => ECO:0000255
source Swiss-Prot : SWS_FT_FI2

82) chain A
residue 138-157
type TRANSMEM
sequence VVYMLHLATADVLFVSVLPF
description Helical; Name=2 => ECO:0000255
source Swiss-Prot : SWS_FT_FI3

83) chain A
residue 158-176
type TOPO_DOM
sequence KISYYFSGSDWQFGSELCR
description Extracellular => ECO:0000255
source Swiss-Prot : SWS_FT_FI4

84) chain A
residue 240-268
type TOPO_DOM
sequence KEQTIQVPGLGITTCHDVLSETLLEGYYA
description Extracellular => ECO:0000255
source Swiss-Prot : SWS_FT_FI4

85) chain A
residue 335-350
type TOPO_DOM
sequence AHYSFLSHTSTTEAAY
description Extracellular => ECO:0000255
source Swiss-Prot : SWS_FT_FI4

86) chain A
residue 177-198
type TRANSMEM
sequence FVTAAFYCNMYASILLMTVISI
description Helical; Name=3 => ECO:0000255
source Swiss-Prot : SWS_FT_FI5

87) chain A
residue 219-239
type TRANSMEM
sequence ASFTCLAIWALAIAGVVPLLL
description Helical; Name=4 => ECO:0000255
source Swiss-Prot : SWS_FT_FI6

88) chain A
residue 269-288
type TRANSMEM
sequence YYFSAFSAVFFFVPLIISTV
description Helical; Name=5 => ECO:0000255
source Swiss-Prot : SWS_FT_FI7

89) chain A
residue 188-204
type prosite
sequence ASILLMTVISIDRFLAV
description G_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASIlLMTVISIDRFLaV
source prosite : PS00237


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