eF-site ID 2o7d-ABCDEFGH
PDB Code 2o7d
Chain A, B, C, D, E, F, G, H

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Title Tyrosine ammonia-lyase from Rhodobacter sphaeroides, complexed with caffeate
Classification LYASE
Compound Putative histidine ammonia-lyase
Source Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158) (Q3IWB0_RHOS4)
Sequence A:  PKPAVELDRHIDLDQAHAVASGGARIVLAPPARDRCRASE
ARLGAVIREARHVYGLTTGFGPLANRLISGENVRTLQANL
VHHLASGVGPVLDWTTARAMVLARLVSIAQGASGASEGTI
ARLIDLLNSELAPAVPSRGTVGXDLTPLAHMVLCLQGRGD
FLDRDGTRLDGAEGLRRGRLQPLDLSHRDALALVNGTSAM
TGIALVNAHACRHLGNWAVALTALLAECLRGRTEAWAAAL
SDLRPHPGQKDAAARLRARVDGSARVVRHVIAERRLDAGD
IGTEPEAGQDAYSLRCAPQVLGAGFDTLAWHDRVLTIELN
AVTDNPVFPPDGSVPALHGGNFMGQHVALTSDALATAVTV
LAGLAERQIARLTDERLNRGLPPFLHRGPAGLNSGFMGAQ
VTATALLAEMRATGPASIHSISTNAANQDVVSLGTIAARL
CREKIDRWAEILAILALCLAQAAELRCGSGLDGVSPAGKK
LVQALREQFPPLETDRPLGQEIAALATHLLQQSPV
B:  PKPAVELDRHIDLDQAHAVASGGARIVLAPPARDRCRASE
ARLGAVIREARHVYGLTTGFGPLANRLISGENVRTLQANL
VHHLASGVGPVLDWTTARAMVLARLVSIAQGASGASEGTI
ARLIDLLNSELAPAVPSRGTVGXDLTPLAHMVLCLQGRGD
FLDRDGTRLDGAEGLRRGRLQPLDLSHRDALALVNGTSAM
TGIALVNAHACRHLGNWAVALTALLAECLRGRTEAWAAAL
SDLRPHPGQKDAAARLRARVDGSARVVRHVIAERRLDAGD
IGTEPEAGQDAYSLRCAPQVLGAGFDTLAWHDRVLTIELN
AVTDNPVFPPDGSVPALHGGNFMGQHVALTSDALATAVTV
LAGLAERQIARLTDERLNRGLPPFLHRGPAGLNSGFMGAQ
VTATALLAEMRATGPASIHSISTNAANQDVVSLGTIAARL
CREKIDRWAEILAILALCLAQAAELRCGSGLDGVSPAGKK
LVQALREQFPPLETDRPLGQEIAALATHLLQQSPV
C:  KPAVELDRHIDLDQAHAVASGGARIVLAPPARDRCRASEA
RLGAVIREARHVYGLTTGFGPLANRLISGENVRTLQANLV
HHLASGVGPVLDWTTARAMVLARLVSIAQGASGASEGTIA
RLIDLLNSELAPAVPSRGTVGXDLTPLAHMVLCLQGRGDF
LDRDGTRLDGAEGLRRGRLQPLDLSHRDALALVNGTSAMT
GIALVNAHACRHLGNWAVALTALLAECLRGRTEAWAAALS
DLRPHPGQKDAAARLRARVDGSARVVRHVIAERRLDAGDI
GTEPEAGQDAYSLRCAPQVLGAGFDTLAWHDRVLTIELNA
VTDNPVFPPDGSVPALHGGNFMGQHVALTSDALATAVTVL
AGLAERQIARLTDERLNRGLPPFLHRGPAGLNSGFMGAQV
TATALLAEMRATGPASIHSISTNAANQDVVSLGTIAARLC
REKIDRWAEILAILALCLAQAAELRCGSGLDGVSPAGKKL
VQALREQFPPLETDRPLGQEIAALATHLLQQSPV
D:  KPAVELDRHIDLDQAHAVASGGARIVLAPPARDRCRASEA
RLGAVIREARHVYGLTTGFGPLANRLISGENVRTLQANLV
HHLASGVGPVLDWTTARAMVLARLVSIAQGASGASEGTIA
RLIDLLNSELAPAVPSRGTVGXDLTPLAHMVLCLQGRGDF
LDRDGTRLDGAEGLRRGRLQPLDLSHRDALALVNGTSAMT
GIALVNAHACRHLGNWAVALTALLAECLRGRTEAWAAALS
DLRPHPGQKDAAARLRARVDGSARVVRHVIAERRLDAGDI
GTEPEAGQDAYSLRCAPQVLGAGFDTLAWHDRVLTIELNA
VTDNPVFPPDGSVPALHGGNFMGQHVALTSDALATAVTVL
AGLAERQIARLTDERLNRGLPPFLHRGPAGLNSGFMGAQV
TATALLAEMRATGPASIHSISTNAANQDVVSLGTIAARLC
REKIDRWAEILAILALCLAQAAELRCGSGLDGVSPAGKKL
VQALREQFPPLETDRPLGQEIAALATHLLQQSPV
E:  KPAVELDRHIDLDQAHAVASGGARIVLAPPARDRCRASEA
RLGAVIREARHVYGLTTGFGPLANRLISGENVRTLQANLV
HHLASGVGPVLDWTTARAMVLARLVSIAQGASGASEGTIA
RLIDLLNSELAPAVPSRGTVGXDLTPLAHMVLCLQGRGDF
LDRDGTRLDGAEGLRRGRLQPLDLSHRDALALVNGTSAMT
GIALVNAHACRHLGNWAVALTALLAECLRGRTEAWAAALS
DLRPHPGQKDAAARLRARVDGSARVVRHVIAERRLDAGDI
GTEPEAGQDAYSLRCAPQVLGAGFDTLAWHDRVLTIELNA
VTDNPVFPPDGSVPALHGGNFMGQHVALTSDALATAVTVL
AGLAERQIARLTDERLNRGLPPFLHRGPAGLNSGFMGAQV
TATALLAEMRATGPASIHSISTNAANQDVVSLGTIAARLC
REKIDRWAEILAILALCLAQAAELRCGSGLDGVSPAGKKL
VQALREQFPPLETDRPLGQEIAALATHLLQQSPV
F:  KPAVELDRHIDLDQAHAVASGGARIVLAPPARDRCRASEA
RLGAVIREARHVYGLTTGFGPLANRLISGENVRTLQANLV
HHLASGVGPVLDWTTARAMVLARLVSIAQGASGASEGTIA
RLIDLLNSELAPAVPSRGTVGXDLTPLAHMVLCLQGRGDF
LDRDGTRLDGAEGLRRGRLQPLDLSHRDALALVNGTSAMT
GIALVNAHACRHLGNWAVALTALLAECLRGRTEAWAAALS
DLRPHPGQKDAAARLRARVDGSARVVRHVIAERRLDAGDI
GTEPEAGQDAYSLRCAPQVLGAGFDTLAWHDRVLTIELNA
VTDNPVFPPDGSVPALHGGNFMGQHVALTSDALATAVTVL
AGLAERQIARLTDERLNRGLPPFLHRGPAGLNSGFMGAQV
TATALLAEMRATGPASIHSISTNAANQDVVSLGTIAARLC
REKIDRWAEILAILALCLAQAAELRCGSGLDGVSPAGKKL
VQALREQFPPLETDRPLGQEIAALATHLLQQSPV
G:  KPAVELDRHIDLDQAHAVASGGARIVLAPPARDRCRASEA
RLGAVIREARHVYGLTTGFGPLANRLISGENVRTLQANLV
HHLASGVGPVLDWTTARAMVLARLVSIAQGASGASEGTIA
RLIDLLNSELAPAVPSRGTVGXDLTPLAHMVLCLQGRGDF
LDRDGTRLDGAEGLRRGRLQPLDLSHRDALALVNGTSAMT
GIALVNAHACRHLGNWAVALTALLAECLRGRTEAWAAALS
DLRPHPGQKDAAARLRARVDGSARVVRHVIAERRLDAGDI
GTEPEAGQDAYSLRCAPQVLGAGFDTLAWHDRVLTIELNA
VTDNPVFPPDGSVPALHGGNFMGQHVALTSDALATAVTVL
AGLAERQIARLTDERLNRGLPPFLHRGPAGLNSGFMGAQV
TATALLAEMRATGPASIHSISTNAANQDVVSLGTIAARLC
REKIDRWAEILAILALCLAQAAELRCGSGLDGVSPAGKKL
VQALREQFPPLETDRPLGQEIAALATHLLQQSPV
H:  KPAVELDRHIDLDQAHAVASGGARIVLAPPARDRCRASEA
RLGAVIREARHVYGLTTGFGPLANRLISGENVRTLQANLV
HHLASGVGPVLDWTTARAMVLARLVSIAQGASGASEGTIA
RLIDLLNSELAPAVPSRGTVGXDLTPLAHMVLCLQGRGDF
LDRDGTRLDGAEGLRRGRLQPLDLSHRDALALVNGTSAMT
GIALVNAHACRHLGNWAVALTALLAECLRGRTEAWAAALS
DLRPHPGQKDAAARLRARVDGSARVVRHVIAERRLDAGDI
GTEPEAGQDAYSLRCAPQVLGAGFDTLAWHDRVLTIELNA
VTDNPVFPPDGSVPALHGGNFMGQHVALTSDALATAVTVL
AGLAERQIARLTDERLNRGLPPFLHRGPAGLNSGFMGAQV
TATALLAEMRATGPASIHSISTNAANQDVVSLGTIAARLC
REKIDRWAEILAILALCLAQAAELRCGSGLDGVSPAGKKL
VQALREQFPPLETDRPLGQEIAALATHLLQQSPV
Description


Functional site

1) chain A
residue 60
type
sequence Y
description BINDING SITE FOR RESIDUE DHC A 701
source : AC1

2) chain A
residue 67
type
sequence G
description BINDING SITE FOR RESIDUE DHC A 701
source : AC1

3) chain A
residue 86
type
sequence L
description BINDING SITE FOR RESIDUE DHC A 701
source : AC1

4) chain A
residue 89
type
sequence H
description BINDING SITE FOR RESIDUE DHC A 701
source : AC1

5) chain A
residue 90
type
sequence L
description BINDING SITE FOR RESIDUE DHC A 701
source : AC1

6) chain A
residue 432
type
sequence N
description BINDING SITE FOR RESIDUE DHC A 701
source : AC1

7) chain A
residue 435
type
sequence N
description BINDING SITE FOR RESIDUE DHC A 701
source : AC1

8) chain A
residue 436
type
sequence Q
description BINDING SITE FOR RESIDUE DHC A 701
source : AC1

9) chain B
residue 405
type
sequence M
description BINDING SITE FOR RESIDUE DHC A 701
source : AC1

10) chain D
residue 300
type
sequence Y
description BINDING SITE FOR RESIDUE DHC A 701
source : AC1

11) chain D
residue 303
type
sequence R
description BINDING SITE FOR RESIDUE DHC A 701
source : AC1

12) chain A
residue 405
type
sequence M
description BINDING SITE FOR RESIDUE DHC B 701
source : AC2

13) chain B
residue 60
type
sequence Y
description BINDING SITE FOR RESIDUE DHC B 701
source : AC2

14) chain B
residue 67
type
sequence G
description BINDING SITE FOR RESIDUE DHC B 701
source : AC2

15) chain B
residue 89
type
sequence H
description BINDING SITE FOR RESIDUE DHC B 701
source : AC2

16) chain B
residue 90
type
sequence L
description BINDING SITE FOR RESIDUE DHC B 701
source : AC2

17) chain B
residue 432
type
sequence N
description BINDING SITE FOR RESIDUE DHC B 701
source : AC2

18) chain B
residue 435
type
sequence N
description BINDING SITE FOR RESIDUE DHC B 701
source : AC2

19) chain B
residue 436
type
sequence Q
description BINDING SITE FOR RESIDUE DHC B 701
source : AC2

20) chain C
residue 300
type
sequence Y
description BINDING SITE FOR RESIDUE DHC B 701
source : AC2

21) chain C
residue 303
type
sequence R
description BINDING SITE FOR RESIDUE DHC B 701
source : AC2

22) chain B
residue 300
type
sequence Y
description BINDING SITE FOR RESIDUE DHC C 701
source : AC3

23) chain B
residue 303
type
sequence R
description BINDING SITE FOR RESIDUE DHC C 701
source : AC3

24) chain C
residue 60
type
sequence Y
description BINDING SITE FOR RESIDUE DHC C 701
source : AC3

25) chain C
residue 67
type
sequence G
description BINDING SITE FOR RESIDUE DHC C 701
source : AC3

26) chain C
residue 86
type
sequence L
description BINDING SITE FOR RESIDUE DHC C 701
source : AC3

27) chain C
residue 89
type
sequence H
description BINDING SITE FOR RESIDUE DHC C 701
source : AC3

28) chain C
residue 90
type
sequence L
description BINDING SITE FOR RESIDUE DHC C 701
source : AC3

29) chain C
residue 432
type
sequence N
description BINDING SITE FOR RESIDUE DHC C 701
source : AC3

30) chain C
residue 435
type
sequence N
description BINDING SITE FOR RESIDUE DHC C 701
source : AC3

31) chain D
residue 405
type
sequence M
description BINDING SITE FOR RESIDUE DHC C 701
source : AC3

32) chain A
residue 300
type
sequence Y
description BINDING SITE FOR RESIDUE DHC D 701
source : AC4

33) chain A
residue 303
type
sequence R
description BINDING SITE FOR RESIDUE DHC D 701
source : AC4

34) chain C
residue 405
type
sequence M
description BINDING SITE FOR RESIDUE DHC D 701
source : AC4

35) chain D
residue 60
type
sequence Y
description BINDING SITE FOR RESIDUE DHC D 701
source : AC4

36) chain D
residue 67
type
sequence G
description BINDING SITE FOR RESIDUE DHC D 701
source : AC4

37) chain D
residue 89
type
sequence H
description BINDING SITE FOR RESIDUE DHC D 701
source : AC4

38) chain D
residue 90
type
sequence L
description BINDING SITE FOR RESIDUE DHC D 701
source : AC4

39) chain D
residue 432
type
sequence N
description BINDING SITE FOR RESIDUE DHC D 701
source : AC4

40) chain D
residue 435
type
sequence N
description BINDING SITE FOR RESIDUE DHC D 701
source : AC4

41) chain D
residue 436
type
sequence Q
description BINDING SITE FOR RESIDUE DHC D 701
source : AC4

42) chain E
residue 60
type
sequence Y
description BINDING SITE FOR RESIDUE DHC E 701
source : AC5

43) chain E
residue 67
type
sequence G
description BINDING SITE FOR RESIDUE DHC E 701
source : AC5

44) chain E
residue 89
type
sequence H
description BINDING SITE FOR RESIDUE DHC E 701
source : AC5

45) chain E
residue 90
type
sequence L
description BINDING SITE FOR RESIDUE DHC E 701
source : AC5

46) chain E
residue 432
type
sequence N
description BINDING SITE FOR RESIDUE DHC E 701
source : AC5

47) chain E
residue 435
type
sequence N
description BINDING SITE FOR RESIDUE DHC E 701
source : AC5

48) chain E
residue 436
type
sequence Q
description BINDING SITE FOR RESIDUE DHC E 701
source : AC5

49) chain F
residue 405
type
sequence M
description BINDING SITE FOR RESIDUE DHC E 701
source : AC5

50) chain H
residue 300
type
sequence Y
description BINDING SITE FOR RESIDUE DHC E 701
source : AC5

51) chain H
residue 303
type
sequence R
description BINDING SITE FOR RESIDUE DHC E 701
source : AC5

52) chain E
residue 406
type
sequence G
description BINDING SITE FOR RESIDUE DHC F 701
source : AC6

53) chain F
residue 60
type
sequence Y
description BINDING SITE FOR RESIDUE DHC F 701
source : AC6

54) chain F
residue 67
type
sequence G
description BINDING SITE FOR RESIDUE DHC F 701
source : AC6

55) chain F
residue 89
type
sequence H
description BINDING SITE FOR RESIDUE DHC F 701
source : AC6

56) chain F
residue 90
type
sequence L
description BINDING SITE FOR RESIDUE DHC F 701
source : AC6

57) chain F
residue 432
type
sequence N
description BINDING SITE FOR RESIDUE DHC F 701
source : AC6

58) chain F
residue 435
type
sequence N
description BINDING SITE FOR RESIDUE DHC F 701
source : AC6

59) chain F
residue 436
type
sequence Q
description BINDING SITE FOR RESIDUE DHC F 701
source : AC6

60) chain G
residue 300
type
sequence Y
description BINDING SITE FOR RESIDUE DHC F 701
source : AC6

61) chain G
residue 303
type
sequence R
description BINDING SITE FOR RESIDUE DHC F 701
source : AC6

62) chain F
residue 300
type
sequence Y
description BINDING SITE FOR RESIDUE DHC G 701
source : AC7

63) chain F
residue 303
type
sequence R
description BINDING SITE FOR RESIDUE DHC G 701
source : AC7

64) chain G
residue 60
type
sequence Y
description BINDING SITE FOR RESIDUE DHC G 701
source : AC7

65) chain G
residue 67
type
sequence G
description BINDING SITE FOR RESIDUE DHC G 701
source : AC7

66) chain G
residue 89
type
sequence H
description BINDING SITE FOR RESIDUE DHC G 701
source : AC7

67) chain G
residue 90
type
sequence L
description BINDING SITE FOR RESIDUE DHC G 701
source : AC7

68) chain G
residue 432
type
sequence N
description BINDING SITE FOR RESIDUE DHC G 701
source : AC7

69) chain G
residue 435
type
sequence N
description BINDING SITE FOR RESIDUE DHC G 701
source : AC7

70) chain G
residue 436
type
sequence Q
description BINDING SITE FOR RESIDUE DHC G 701
source : AC7

71) chain H
residue 406
type
sequence G
description BINDING SITE FOR RESIDUE DHC G 701
source : AC7

72) chain E
residue 297
type
sequence Q
description BINDING SITE FOR RESIDUE DHC H 701
source : AC8

73) chain E
residue 300
type
sequence Y
description BINDING SITE FOR RESIDUE DHC H 701
source : AC8

74) chain E
residue 303
type
sequence R
description BINDING SITE FOR RESIDUE DHC H 701
source : AC8

75) chain G
residue 405
type
sequence M
description BINDING SITE FOR RESIDUE DHC H 701
source : AC8

76) chain H
residue 60
type
sequence Y
description BINDING SITE FOR RESIDUE DHC H 701
source : AC8

77) chain H
residue 67
type
sequence G
description BINDING SITE FOR RESIDUE DHC H 701
source : AC8

78) chain H
residue 86
type
sequence L
description BINDING SITE FOR RESIDUE DHC H 701
source : AC8

79) chain H
residue 89
type
sequence H
description BINDING SITE FOR RESIDUE DHC H 701
source : AC8

80) chain H
residue 90
type
sequence L
description BINDING SITE FOR RESIDUE DHC H 701
source : AC8

81) chain H
residue 432
type
sequence N
description BINDING SITE FOR RESIDUE DHC H 701
source : AC8

82) chain H
residue 435
type
sequence N
description BINDING SITE FOR RESIDUE DHC H 701
source : AC8

83) chain H
residue 436
type
sequence Q
description BINDING SITE FOR RESIDUE DHC H 701
source : AC8

84) chain A
residue 89
type BINDING
sequence H
description
source Swiss-Prot : SWS_FT_FI2

85) chain D
residue 89
type BINDING
sequence H
description
source Swiss-Prot : SWS_FT_FI2

86) chain D
residue 305
type BINDING
sequence A
description
source Swiss-Prot : SWS_FT_FI2

87) chain D
residue 434
type BINDING
sequence A
description
source Swiss-Prot : SWS_FT_FI2

88) chain E
residue 89
type BINDING
sequence H
description
source Swiss-Prot : SWS_FT_FI2

89) chain E
residue 305
type BINDING
sequence A
description
source Swiss-Prot : SWS_FT_FI2

90) chain E
residue 434
type BINDING
sequence A
description
source Swiss-Prot : SWS_FT_FI2

91) chain F
residue 89
type BINDING
sequence H
description
source Swiss-Prot : SWS_FT_FI2

92) chain F
residue 305
type BINDING
sequence A
description
source Swiss-Prot : SWS_FT_FI2

93) chain F
residue 434
type BINDING
sequence A
description
source Swiss-Prot : SWS_FT_FI2

94) chain G
residue 89
type BINDING
sequence H
description
source Swiss-Prot : SWS_FT_FI2

95) chain A
residue 305
type BINDING
sequence A
description
source Swiss-Prot : SWS_FT_FI2

96) chain G
residue 305
type BINDING
sequence A
description
source Swiss-Prot : SWS_FT_FI2

97) chain G
residue 434
type BINDING
sequence A
description
source Swiss-Prot : SWS_FT_FI2

98) chain H
residue 89
type BINDING
sequence H
description
source Swiss-Prot : SWS_FT_FI2

99) chain H
residue 305
type BINDING
sequence A
description
source Swiss-Prot : SWS_FT_FI2

100) chain H
residue 434
type BINDING
sequence A
description
source Swiss-Prot : SWS_FT_FI2

101) chain A
residue 434
type BINDING
sequence A
description
source Swiss-Prot : SWS_FT_FI2

102) chain B
residue 89
type BINDING
sequence H
description
source Swiss-Prot : SWS_FT_FI2

103) chain B
residue 305
type BINDING
sequence A
description
source Swiss-Prot : SWS_FT_FI2

104) chain B
residue 434
type BINDING
sequence A
description
source Swiss-Prot : SWS_FT_FI2

105) chain C
residue 89
type BINDING
sequence H
description
source Swiss-Prot : SWS_FT_FI2

106) chain C
residue 305
type BINDING
sequence A
description
source Swiss-Prot : SWS_FT_FI2

107) chain C
residue 434
type BINDING
sequence A
description
source Swiss-Prot : SWS_FT_FI2

108) chain A
residue 60
type ACT_SITE
sequence Y
description Proton donor/acceptor => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

109) chain B
residue 60
type ACT_SITE
sequence Y
description Proton donor/acceptor => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

110) chain C
residue 60
type ACT_SITE
sequence Y
description Proton donor/acceptor => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

111) chain D
residue 60
type ACT_SITE
sequence Y
description Proton donor/acceptor => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

112) chain E
residue 60
type ACT_SITE
sequence Y
description Proton donor/acceptor => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

113) chain F
residue 60
type ACT_SITE
sequence Y
description Proton donor/acceptor => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

114) chain G
residue 60
type ACT_SITE
sequence Y
description Proton donor/acceptor => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

115) chain H
residue 60
type ACT_SITE
sequence Y
description Proton donor/acceptor => ECO:0000250
source Swiss-Prot : SWS_FT_FI1

116) chain A
residue 152
type MOD_RES
sequence D
description 2,3-didehydroalanine (Ser) => ECO:0000305|PubMed:17185228
source Swiss-Prot : SWS_FT_FI3

117) chain B
residue 152
type MOD_RES
sequence D
description 2,3-didehydroalanine (Ser) => ECO:0000305|PubMed:17185228
source Swiss-Prot : SWS_FT_FI3

118) chain C
residue 152
type MOD_RES
sequence D
description 2,3-didehydroalanine (Ser) => ECO:0000305|PubMed:17185228
source Swiss-Prot : SWS_FT_FI3

119) chain D
residue 152
type MOD_RES
sequence D
description 2,3-didehydroalanine (Ser) => ECO:0000305|PubMed:17185228
source Swiss-Prot : SWS_FT_FI3

120) chain E
residue 152
type MOD_RES
sequence D
description 2,3-didehydroalanine (Ser) => ECO:0000305|PubMed:17185228
source Swiss-Prot : SWS_FT_FI3

121) chain F
residue 152
type MOD_RES
sequence D
description 2,3-didehydroalanine (Ser) => ECO:0000305|PubMed:17185228
source Swiss-Prot : SWS_FT_FI3

122) chain G
residue 152
type MOD_RES
sequence D
description 2,3-didehydroalanine (Ser) => ECO:0000305|PubMed:17185228
source Swiss-Prot : SWS_FT_FI3

123) chain H
residue 152
type MOD_RES
sequence D
description 2,3-didehydroalanine (Ser) => ECO:0000305|PubMed:17185228
source Swiss-Prot : SWS_FT_FI3

124) chain A
residue 149
type CROSSLNK
sequence X
description 5-imidazolinone (Ala-Gly) => ECO:0000305|PubMed:17185228
source Swiss-Prot : SWS_FT_FI4

125) chain E
residue 153
type CROSSLNK
sequence L
description 5-imidazolinone (Ala-Gly) => ECO:0000305|PubMed:17185228
source Swiss-Prot : SWS_FT_FI4

126) chain F
residue 149
type CROSSLNK
sequence X
description 5-imidazolinone (Ala-Gly) => ECO:0000305|PubMed:17185228
source Swiss-Prot : SWS_FT_FI4

127) chain F
residue 153
type CROSSLNK
sequence L
description 5-imidazolinone (Ala-Gly) => ECO:0000305|PubMed:17185228
source Swiss-Prot : SWS_FT_FI4

128) chain G
residue 149
type CROSSLNK
sequence X
description 5-imidazolinone (Ala-Gly) => ECO:0000305|PubMed:17185228
source Swiss-Prot : SWS_FT_FI4

129) chain G
residue 153
type CROSSLNK
sequence L
description 5-imidazolinone (Ala-Gly) => ECO:0000305|PubMed:17185228
source Swiss-Prot : SWS_FT_FI4

130) chain H
residue 149
type CROSSLNK
sequence X
description 5-imidazolinone (Ala-Gly) => ECO:0000305|PubMed:17185228
source Swiss-Prot : SWS_FT_FI4

131) chain H
residue 153
type CROSSLNK
sequence L
description 5-imidazolinone (Ala-Gly) => ECO:0000305|PubMed:17185228
source Swiss-Prot : SWS_FT_FI4

132) chain A
residue 153
type CROSSLNK
sequence L
description 5-imidazolinone (Ala-Gly) => ECO:0000305|PubMed:17185228
source Swiss-Prot : SWS_FT_FI4

133) chain B
residue 149
type CROSSLNK
sequence X
description 5-imidazolinone (Ala-Gly) => ECO:0000305|PubMed:17185228
source Swiss-Prot : SWS_FT_FI4

134) chain B
residue 153
type CROSSLNK
sequence L
description 5-imidazolinone (Ala-Gly) => ECO:0000305|PubMed:17185228
source Swiss-Prot : SWS_FT_FI4

135) chain C
residue 149
type CROSSLNK
sequence X
description 5-imidazolinone (Ala-Gly) => ECO:0000305|PubMed:17185228
source Swiss-Prot : SWS_FT_FI4

136) chain C
residue 153
type CROSSLNK
sequence L
description 5-imidazolinone (Ala-Gly) => ECO:0000305|PubMed:17185228
source Swiss-Prot : SWS_FT_FI4

137) chain D
residue 149
type CROSSLNK
sequence X
description 5-imidazolinone (Ala-Gly) => ECO:0000305|PubMed:17185228
source Swiss-Prot : SWS_FT_FI4

138) chain D
residue 153
type CROSSLNK
sequence L
description 5-imidazolinone (Ala-Gly) => ECO:0000305|PubMed:17185228
source Swiss-Prot : SWS_FT_FI4

139) chain E
residue 149
type CROSSLNK
sequence X
description 5-imidazolinone (Ala-Gly) => ECO:0000305|PubMed:17185228
source Swiss-Prot : SWS_FT_FI4

140) chain A
residue 145-163
type prosite
sequence GTVGXDLTPLAHMVLCL
description PAL_HISTIDASE Phenylalanine and histidine ammonia-lyases signature. GTVGASGDLtPLAhmvL
source prosite : PS00488


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