eF-site ID 1pu0-ABCDEFGHIJ
PDB Code 1pu0
Chain A, B, C, D, E, F, G, H, I, J

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Title Structure of Human Cu,Zn Superoxide Dismutase
Classification OXIDOREDUCTASE
Compound Superoxide dismutase [Cu-Zn]
Source Homo sapiens (Human) (SODC_HUMAN)
Sequence A:  ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTE
GLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVH
EKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
B:  ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTE
GLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVH
EKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
C:  ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTE
GLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVH
EKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
D:  ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTE
GLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVH
EKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
E:  ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTE
GLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVH
EKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
F:  ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTE
GLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVH
EKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
G:  ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTE
GLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVH
EKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
H:  ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTE
GLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVH
EKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
I:  ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTE
GLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVH
EKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
J:  ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTE
GLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVH
EKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
Description


Functional site

1) chain A
residue 46
type
sequence H
description BINDING SITE FOR RESIDUE CU1 A 200
source : AC1

2) chain A
residue 48
type
sequence H
description BINDING SITE FOR RESIDUE CU1 A 200
source : AC1

3) chain A
residue 63
type
sequence H
description BINDING SITE FOR RESIDUE CU1 A 200
source : AC1

4) chain A
residue 120
type
sequence H
description BINDING SITE FOR RESIDUE CU1 A 200
source : AC1

5) chain A
residue 63
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 201
source : AC2

6) chain A
residue 71
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 201
source : AC2

7) chain A
residue 80
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 201
source : AC2

8) chain A
residue 83
type
sequence D
description BINDING SITE FOR RESIDUE ZN A 201
source : AC2

9) chain B
residue 46
type
sequence H
description BINDING SITE FOR RESIDUE CU1 B 200
source : AC3

10) chain B
residue 48
type
sequence H
description BINDING SITE FOR RESIDUE CU1 B 200
source : AC3

11) chain B
residue 63
type
sequence H
description BINDING SITE FOR RESIDUE CU1 B 200
source : AC3

12) chain B
residue 120
type
sequence H
description BINDING SITE FOR RESIDUE CU1 B 200
source : AC3

13) chain B
residue 63
type
sequence H
description BINDING SITE FOR RESIDUE ZN B 201
source : AC4

14) chain B
residue 71
type
sequence H
description BINDING SITE FOR RESIDUE ZN B 201
source : AC4

15) chain B
residue 80
type
sequence H
description BINDING SITE FOR RESIDUE ZN B 201
source : AC4

16) chain B
residue 83
type
sequence D
description BINDING SITE FOR RESIDUE ZN B 201
source : AC4

17) chain C
residue 46
type
sequence H
description BINDING SITE FOR RESIDUE CU1 C 200
source : AC5

18) chain C
residue 48
type
sequence H
description BINDING SITE FOR RESIDUE CU1 C 200
source : AC5

19) chain C
residue 63
type
sequence H
description BINDING SITE FOR RESIDUE CU1 C 200
source : AC5

20) chain C
residue 120
type
sequence H
description BINDING SITE FOR RESIDUE CU1 C 200
source : AC5

21) chain C
residue 63
type
sequence H
description BINDING SITE FOR RESIDUE ZN C 201
source : AC6

22) chain C
residue 71
type
sequence H
description BINDING SITE FOR RESIDUE ZN C 201
source : AC6

23) chain C
residue 80
type
sequence H
description BINDING SITE FOR RESIDUE ZN C 201
source : AC6

24) chain C
residue 83
type
sequence D
description BINDING SITE FOR RESIDUE ZN C 201
source : AC6

25) chain D
residue 46
type
sequence H
description BINDING SITE FOR RESIDUE CU1 D 200
source : AC7

26) chain D
residue 48
type
sequence H
description BINDING SITE FOR RESIDUE CU1 D 200
source : AC7

27) chain D
residue 63
type
sequence H
description BINDING SITE FOR RESIDUE CU1 D 200
source : AC7

28) chain D
residue 120
type
sequence H
description BINDING SITE FOR RESIDUE CU1 D 200
source : AC7

29) chain D
residue 63
type
sequence H
description BINDING SITE FOR RESIDUE ZN D 201
source : AC8

30) chain D
residue 71
type
sequence H
description BINDING SITE FOR RESIDUE ZN D 201
source : AC8

31) chain D
residue 80
type
sequence H
description BINDING SITE FOR RESIDUE ZN D 201
source : AC8

32) chain D
residue 83
type
sequence D
description BINDING SITE FOR RESIDUE ZN D 201
source : AC8

33) chain E
residue 46
type
sequence H
description BINDING SITE FOR RESIDUE CU1 E 200
source : AC9

34) chain E
residue 48
type
sequence H
description BINDING SITE FOR RESIDUE CU1 E 200
source : AC9

35) chain E
residue 63
type
sequence H
description BINDING SITE FOR RESIDUE CU1 E 200
source : AC9

36) chain E
residue 120
type
sequence H
description BINDING SITE FOR RESIDUE CU1 E 200
source : AC9

37) chain E
residue 63
type
sequence H
description BINDING SITE FOR RESIDUE ZN E 201
source : BC1

38) chain E
residue 71
type
sequence H
description BINDING SITE FOR RESIDUE ZN E 201
source : BC1

39) chain E
residue 80
type
sequence H
description BINDING SITE FOR RESIDUE ZN E 201
source : BC1

40) chain E
residue 83
type
sequence D
description BINDING SITE FOR RESIDUE ZN E 201
source : BC1

41) chain F
residue 46
type
sequence H
description BINDING SITE FOR RESIDUE CU1 F 200
source : BC2

42) chain F
residue 48
type
sequence H
description BINDING SITE FOR RESIDUE CU1 F 200
source : BC2

43) chain F
residue 63
type
sequence H
description BINDING SITE FOR RESIDUE CU1 F 200
source : BC2

44) chain F
residue 120
type
sequence H
description BINDING SITE FOR RESIDUE CU1 F 200
source : BC2

45) chain F
residue 63
type
sequence H
description BINDING SITE FOR RESIDUE ZN F 201
source : BC3

46) chain F
residue 71
type
sequence H
description BINDING SITE FOR RESIDUE ZN F 201
source : BC3

47) chain F
residue 80
type
sequence H
description BINDING SITE FOR RESIDUE ZN F 201
source : BC3

48) chain F
residue 83
type
sequence D
description BINDING SITE FOR RESIDUE ZN F 201
source : BC3

49) chain G
residue 46
type
sequence H
description BINDING SITE FOR RESIDUE CU1 G 200
source : BC4

50) chain G
residue 48
type
sequence H
description BINDING SITE FOR RESIDUE CU1 G 200
source : BC4

51) chain G
residue 63
type
sequence H
description BINDING SITE FOR RESIDUE CU1 G 200
source : BC4

52) chain G
residue 120
type
sequence H
description BINDING SITE FOR RESIDUE CU1 G 200
source : BC4

53) chain G
residue 63
type
sequence H
description BINDING SITE FOR RESIDUE ZN G 201
source : BC5

54) chain G
residue 71
type
sequence H
description BINDING SITE FOR RESIDUE ZN G 201
source : BC5

55) chain G
residue 80
type
sequence H
description BINDING SITE FOR RESIDUE ZN G 201
source : BC5

56) chain G
residue 83
type
sequence D
description BINDING SITE FOR RESIDUE ZN G 201
source : BC5

57) chain G
residue 136
type
sequence K
description BINDING SITE FOR RESIDUE ZN G 201
source : BC5

58) chain H
residue 46
type
sequence H
description BINDING SITE FOR RESIDUE CU1 H 200
source : BC6

59) chain H
residue 48
type
sequence H
description BINDING SITE FOR RESIDUE CU1 H 200
source : BC6

60) chain H
residue 63
type
sequence H
description BINDING SITE FOR RESIDUE CU1 H 200
source : BC6

61) chain H
residue 120
type
sequence H
description BINDING SITE FOR RESIDUE CU1 H 200
source : BC6

62) chain H
residue 63
type
sequence H
description BINDING SITE FOR RESIDUE ZN H 201
source : BC7

63) chain H
residue 71
type
sequence H
description BINDING SITE FOR RESIDUE ZN H 201
source : BC7

64) chain H
residue 80
type
sequence H
description BINDING SITE FOR RESIDUE ZN H 201
source : BC7

65) chain H
residue 83
type
sequence D
description BINDING SITE FOR RESIDUE ZN H 201
source : BC7

66) chain I
residue 46
type
sequence H
description BINDING SITE FOR RESIDUE CU1 I 200
source : BC8

67) chain I
residue 48
type
sequence H
description BINDING SITE FOR RESIDUE CU1 I 200
source : BC8

68) chain I
residue 63
type
sequence H
description BINDING SITE FOR RESIDUE CU1 I 200
source : BC8

69) chain I
residue 120
type
sequence H
description BINDING SITE FOR RESIDUE CU1 I 200
source : BC8

70) chain I
residue 63
type
sequence H
description BINDING SITE FOR RESIDUE ZN I 201
source : BC9

71) chain I
residue 71
type
sequence H
description BINDING SITE FOR RESIDUE ZN I 201
source : BC9

72) chain I
residue 80
type
sequence H
description BINDING SITE FOR RESIDUE ZN I 201
source : BC9

73) chain I
residue 83
type
sequence D
description BINDING SITE FOR RESIDUE ZN I 201
source : BC9

74) chain J
residue 46
type
sequence H
description BINDING SITE FOR RESIDUE CU1 J 200
source : CC1

75) chain J
residue 48
type
sequence H
description BINDING SITE FOR RESIDUE CU1 J 200
source : CC1

76) chain J
residue 63
type
sequence H
description BINDING SITE FOR RESIDUE CU1 J 200
source : CC1

77) chain J
residue 120
type
sequence H
description BINDING SITE FOR RESIDUE CU1 J 200
source : CC1

78) chain J
residue 63
type
sequence H
description BINDING SITE FOR RESIDUE ZN J 201
source : CC2

79) chain J
residue 71
type
sequence H
description BINDING SITE FOR RESIDUE ZN J 201
source : CC2

80) chain J
residue 80
type
sequence H
description BINDING SITE FOR RESIDUE ZN J 201
source : CC2

81) chain J
residue 83
type
sequence D
description BINDING SITE FOR RESIDUE ZN J 201
source : CC2

82) chain B
residue 75
type
sequence K
description BINDING SITE FOR RESIDUE SO4 B 300
source : CC3

83) chain D
residue 128
type
sequence K
description BINDING SITE FOR RESIDUE SO4 B 300
source : CC3

84) chain E
residue 128
type
sequence K
description BINDING SITE FOR RESIDUE SO4 J 301
source : CC4

85) chain H
residue 75
type
sequence K
description BINDING SITE FOR RESIDUE SO4 J 301
source : CC4

86) chain H
residue 128
type
sequence K
description BINDING SITE FOR RESIDUE SO4 J 301
source : CC4

87) chain J
residue 128
type
sequence K
description BINDING SITE FOR RESIDUE SO4 J 301
source : CC4

88) chain J
residue 39
type
sequence T
description BINDING SITE FOR RESIDUE SO4 J 302
source : CC5

89) chain J
residue 40
type
sequence E
description BINDING SITE FOR RESIDUE SO4 J 302
source : CC5

90) chain A
residue 44-54
type prosite
sequence GFHVHEFGDNT
description SOD_CU_ZN_1 Copper/Zinc superoxide dismutase signature 1. GFHVHEfGDnT
source prosite : PS00087

91) chain A
residue 138-149
type prosite
sequence GNAGSRLACGVI
description SOD_CU_ZN_2 Copper/Zinc superoxide dismutase signature 2. GNAGsRlACgvI
source prosite : PS00332

92) chain A
residue 47
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825
source Swiss-Prot : SWS_FT_FI1

93) chain D
residue 47
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825
source Swiss-Prot : SWS_FT_FI1

94) chain D
residue 49
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825
source Swiss-Prot : SWS_FT_FI1

95) chain D
residue 121
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825
source Swiss-Prot : SWS_FT_FI1

96) chain E
residue 47
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825
source Swiss-Prot : SWS_FT_FI1

97) chain E
residue 49
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825
source Swiss-Prot : SWS_FT_FI1

98) chain E
residue 121
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825
source Swiss-Prot : SWS_FT_FI1

99) chain F
residue 47
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825
source Swiss-Prot : SWS_FT_FI1

100) chain F
residue 49
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825
source Swiss-Prot : SWS_FT_FI1

101) chain F
residue 121
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825
source Swiss-Prot : SWS_FT_FI1

102) chain G
residue 47
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825
source Swiss-Prot : SWS_FT_FI1

103) chain A
residue 49
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825
source Swiss-Prot : SWS_FT_FI1

104) chain G
residue 49
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825
source Swiss-Prot : SWS_FT_FI1

105) chain G
residue 121
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825
source Swiss-Prot : SWS_FT_FI1

106) chain H
residue 47
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825
source Swiss-Prot : SWS_FT_FI1

107) chain H
residue 49
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825
source Swiss-Prot : SWS_FT_FI1

108) chain H
residue 121
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825
source Swiss-Prot : SWS_FT_FI1

109) chain I
residue 47
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825
source Swiss-Prot : SWS_FT_FI1

110) chain I
residue 49
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825
source Swiss-Prot : SWS_FT_FI1

111) chain I
residue 121
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825
source Swiss-Prot : SWS_FT_FI1

112) chain J
residue 47
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825
source Swiss-Prot : SWS_FT_FI1

113) chain J
residue 49
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825
source Swiss-Prot : SWS_FT_FI1

114) chain A
residue 121
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825
source Swiss-Prot : SWS_FT_FI1

115) chain J
residue 121
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825
source Swiss-Prot : SWS_FT_FI1

116) chain B
residue 47
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825
source Swiss-Prot : SWS_FT_FI1

117) chain B
residue 49
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825
source Swiss-Prot : SWS_FT_FI1

118) chain B
residue 121
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825
source Swiss-Prot : SWS_FT_FI1

119) chain C
residue 47
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825
source Swiss-Prot : SWS_FT_FI1

120) chain C
residue 49
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825
source Swiss-Prot : SWS_FT_FI1

121) chain C
residue 121
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:12963370, ECO:0000269|PubMed:17548825
source Swiss-Prot : SWS_FT_FI1

122) chain A
residue 137
type MOD_RES
sequence T
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI10

123) chain J
residue 137
type MOD_RES
sequence T
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI10

124) chain B
residue 137
type MOD_RES
sequence T
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI10

125) chain C
residue 137
type MOD_RES
sequence T
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI10

126) chain D
residue 137
type MOD_RES
sequence T
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI10

127) chain E
residue 137
type MOD_RES
sequence T
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI10

128) chain F
residue 137
type MOD_RES
sequence T
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI10

129) chain G
residue 137
type MOD_RES
sequence T
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI10

130) chain H
residue 137
type MOD_RES
sequence T
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI10

131) chain I
residue 137
type MOD_RES
sequence T
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI10

132) chain A
residue 7
type LIPID
sequence V
description S-palmitoyl cysteine => ECO:0000269|PubMed:22496122
source Swiss-Prot : SWS_FT_FI11

133) chain J
residue 7
type LIPID
sequence V
description S-palmitoyl cysteine => ECO:0000269|PubMed:22496122
source Swiss-Prot : SWS_FT_FI11

134) chain B
residue 7
type LIPID
sequence V
description S-palmitoyl cysteine => ECO:0000269|PubMed:22496122
source Swiss-Prot : SWS_FT_FI11

135) chain C
residue 7
type LIPID
sequence V
description S-palmitoyl cysteine => ECO:0000269|PubMed:22496122
source Swiss-Prot : SWS_FT_FI11

136) chain D
residue 7
type LIPID
sequence V
description S-palmitoyl cysteine => ECO:0000269|PubMed:22496122
source Swiss-Prot : SWS_FT_FI11

137) chain E
residue 7
type LIPID
sequence V
description S-palmitoyl cysteine => ECO:0000269|PubMed:22496122
source Swiss-Prot : SWS_FT_FI11

138) chain F
residue 7
type LIPID
sequence V
description S-palmitoyl cysteine => ECO:0000269|PubMed:22496122
source Swiss-Prot : SWS_FT_FI11

139) chain G
residue 7
type LIPID
sequence V
description S-palmitoyl cysteine => ECO:0000269|PubMed:22496122
source Swiss-Prot : SWS_FT_FI11

140) chain H
residue 7
type LIPID
sequence V
description S-palmitoyl cysteine => ECO:0000269|PubMed:22496122
source Swiss-Prot : SWS_FT_FI11

141) chain I
residue 7
type LIPID
sequence V
description S-palmitoyl cysteine => ECO:0000269|PubMed:22496122
source Swiss-Prot : SWS_FT_FI11

142) chain A
residue 33
type CROSSLNK
sequence G
description 1-(tryptophan-3-yl)-tryptophan (Trp-Trp) (interchain with W-33) => ECO:0000269|PubMed:20600836
source Swiss-Prot : SWS_FT_FI12

143) chain F
residue 33
type CROSSLNK
sequence G
description 1-(tryptophan-3-yl)-tryptophan (Trp-Trp) (interchain with W-33) => ECO:0000269|PubMed:20600836
source Swiss-Prot : SWS_FT_FI12

144) chain G
residue 33
type CROSSLNK
sequence G
description 1-(tryptophan-3-yl)-tryptophan (Trp-Trp) (interchain with W-33) => ECO:0000269|PubMed:20600836
source Swiss-Prot : SWS_FT_FI12

145) chain H
residue 33
type CROSSLNK
sequence G
description 1-(tryptophan-3-yl)-tryptophan (Trp-Trp) (interchain with W-33) => ECO:0000269|PubMed:20600836
source Swiss-Prot : SWS_FT_FI12

146) chain I
residue 33
type CROSSLNK
sequence G
description 1-(tryptophan-3-yl)-tryptophan (Trp-Trp) (interchain with W-33) => ECO:0000269|PubMed:20600836
source Swiss-Prot : SWS_FT_FI12

147) chain J
residue 33
type CROSSLNK
sequence G
description 1-(tryptophan-3-yl)-tryptophan (Trp-Trp) (interchain with W-33) => ECO:0000269|PubMed:20600836
source Swiss-Prot : SWS_FT_FI12

148) chain B
residue 33
type CROSSLNK
sequence G
description 1-(tryptophan-3-yl)-tryptophan (Trp-Trp) (interchain with W-33) => ECO:0000269|PubMed:20600836
source Swiss-Prot : SWS_FT_FI12

149) chain C
residue 33
type CROSSLNK
sequence G
description 1-(tryptophan-3-yl)-tryptophan (Trp-Trp) (interchain with W-33) => ECO:0000269|PubMed:20600836
source Swiss-Prot : SWS_FT_FI12

150) chain D
residue 33
type CROSSLNK
sequence G
description 1-(tryptophan-3-yl)-tryptophan (Trp-Trp) (interchain with W-33) => ECO:0000269|PubMed:20600836
source Swiss-Prot : SWS_FT_FI12

151) chain E
residue 33
type CROSSLNK
sequence G
description 1-(tryptophan-3-yl)-tryptophan (Trp-Trp) (interchain with W-33) => ECO:0000269|PubMed:20600836
source Swiss-Prot : SWS_FT_FI12

152) chain A
residue 64
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

153) chain C
residue 72
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

154) chain C
residue 81
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

155) chain C
residue 84
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

156) chain D
residue 64
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

157) chain D
residue 72
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

158) chain D
residue 81
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

159) chain D
residue 84
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

160) chain E
residue 64
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

161) chain E
residue 72
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

162) chain E
residue 81
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

163) chain A
residue 72
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

164) chain E
residue 84
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

165) chain F
residue 64
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

166) chain F
residue 72
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

167) chain F
residue 81
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

168) chain F
residue 84
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

169) chain G
residue 64
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

170) chain G
residue 72
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

171) chain G
residue 81
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

172) chain G
residue 84
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

173) chain H
residue 64
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

174) chain A
residue 81
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

175) chain H
residue 72
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

176) chain H
residue 81
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

177) chain H
residue 84
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

178) chain I
residue 64
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

179) chain I
residue 72
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

180) chain I
residue 81
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

181) chain I
residue 84
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

182) chain J
residue 64
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

183) chain J
residue 72
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

184) chain J
residue 81
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

185) chain A
residue 84
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

186) chain J
residue 84
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

187) chain B
residue 64
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

188) chain B
residue 72
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

189) chain B
residue 81
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

190) chain B
residue 84
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

191) chain C
residue 64
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:20727846
source Swiss-Prot : SWS_FT_FI2

192) chain A
residue 2
type MOD_RES
sequence T
description N-acetylalanine => ECO:0000269|PubMed:1463506, ECO:0000269|PubMed:7002610, ECO:0007744|PubMed:25944712
source Swiss-Prot : SWS_FT_FI3

193) chain J
residue 2
type MOD_RES
sequence T
description N-acetylalanine => ECO:0000269|PubMed:1463506, ECO:0000269|PubMed:7002610, ECO:0007744|PubMed:25944712
source Swiss-Prot : SWS_FT_FI3

194) chain B
residue 2
type MOD_RES
sequence T
description N-acetylalanine => ECO:0000269|PubMed:1463506, ECO:0000269|PubMed:7002610, ECO:0007744|PubMed:25944712
source Swiss-Prot : SWS_FT_FI3

195) chain C
residue 2
type MOD_RES
sequence T
description N-acetylalanine => ECO:0000269|PubMed:1463506, ECO:0000269|PubMed:7002610, ECO:0007744|PubMed:25944712
source Swiss-Prot : SWS_FT_FI3

196) chain D
residue 2
type MOD_RES
sequence T
description N-acetylalanine => ECO:0000269|PubMed:1463506, ECO:0000269|PubMed:7002610, ECO:0007744|PubMed:25944712
source Swiss-Prot : SWS_FT_FI3

197) chain E
residue 2
type MOD_RES
sequence T
description N-acetylalanine => ECO:0000269|PubMed:1463506, ECO:0000269|PubMed:7002610, ECO:0007744|PubMed:25944712
source Swiss-Prot : SWS_FT_FI3

198) chain F
residue 2
type MOD_RES
sequence T
description N-acetylalanine => ECO:0000269|PubMed:1463506, ECO:0000269|PubMed:7002610, ECO:0007744|PubMed:25944712
source Swiss-Prot : SWS_FT_FI3

199) chain G
residue 2
type MOD_RES
sequence T
description N-acetylalanine => ECO:0000269|PubMed:1463506, ECO:0000269|PubMed:7002610, ECO:0007744|PubMed:25944712
source Swiss-Prot : SWS_FT_FI3

200) chain H
residue 2
type MOD_RES
sequence T
description N-acetylalanine => ECO:0000269|PubMed:1463506, ECO:0000269|PubMed:7002610, ECO:0007744|PubMed:25944712
source Swiss-Prot : SWS_FT_FI3

201) chain I
residue 2
type MOD_RES
sequence T
description N-acetylalanine => ECO:0000269|PubMed:1463506, ECO:0000269|PubMed:7002610, ECO:0007744|PubMed:25944712
source Swiss-Prot : SWS_FT_FI3

202) chain A
residue 4
type MOD_RES
sequence A
description N6-succinyllysine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI4

203) chain D
residue 4
type MOD_RES
sequence A
description N6-succinyllysine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI4

204) chain D
residue 10
type MOD_RES
sequence G
description N6-succinyllysine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI4

205) chain D
residue 92
type MOD_RES
sequence D
description N6-succinyllysine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI4

206) chain E
residue 4
type MOD_RES
sequence A
description N6-succinyllysine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI4

207) chain E
residue 10
type MOD_RES
sequence G
description N6-succinyllysine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI4

208) chain E
residue 92
type MOD_RES
sequence D
description N6-succinyllysine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI4

209) chain F
residue 4
type MOD_RES
sequence A
description N6-succinyllysine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI4

210) chain F
residue 10
type MOD_RES
sequence G
description N6-succinyllysine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI4

211) chain F
residue 92
type MOD_RES
sequence D
description N6-succinyllysine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI4

212) chain G
residue 4
type MOD_RES
sequence A
description N6-succinyllysine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI4

213) chain A
residue 10
type MOD_RES
sequence G
description N6-succinyllysine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI4

214) chain G
residue 10
type MOD_RES
sequence G
description N6-succinyllysine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI4

215) chain G
residue 92
type MOD_RES
sequence D
description N6-succinyllysine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI4

216) chain H
residue 4
type MOD_RES
sequence A
description N6-succinyllysine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI4

217) chain H
residue 10
type MOD_RES
sequence G
description N6-succinyllysine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI4

218) chain H
residue 92
type MOD_RES
sequence D
description N6-succinyllysine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI4

219) chain I
residue 4
type MOD_RES
sequence A
description N6-succinyllysine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI4

220) chain I
residue 10
type MOD_RES
sequence G
description N6-succinyllysine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI4

221) chain I
residue 92
type MOD_RES
sequence D
description N6-succinyllysine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI4

222) chain J
residue 4
type MOD_RES
sequence A
description N6-succinyllysine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI4

223) chain J
residue 10
type MOD_RES
sequence G
description N6-succinyllysine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI4

224) chain A
residue 92
type MOD_RES
sequence D
description N6-succinyllysine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI4

225) chain J
residue 92
type MOD_RES
sequence D
description N6-succinyllysine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI4

226) chain B
residue 4
type MOD_RES
sequence A
description N6-succinyllysine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI4

227) chain B
residue 10
type MOD_RES
sequence G
description N6-succinyllysine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI4

228) chain B
residue 92
type MOD_RES
sequence D
description N6-succinyllysine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI4

229) chain C
residue 4
type MOD_RES
sequence A
description N6-succinyllysine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI4

230) chain C
residue 10
type MOD_RES
sequence G
description N6-succinyllysine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI4

231) chain C
residue 92
type MOD_RES
sequence D
description N6-succinyllysine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI4

232) chain A
residue 99
type MOD_RES
sequence I
description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI5

233) chain J
residue 99
type MOD_RES
sequence I
description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI5

234) chain B
residue 99
type MOD_RES
sequence I
description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI5

235) chain C
residue 99
type MOD_RES
sequence I
description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI5

236) chain D
residue 99
type MOD_RES
sequence I
description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI5

237) chain E
residue 99
type MOD_RES
sequence I
description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI5

238) chain F
residue 99
type MOD_RES
sequence I
description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI5

239) chain G
residue 99
type MOD_RES
sequence I
description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI5

240) chain H
residue 99
type MOD_RES
sequence I
description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI5

241) chain I
residue 99
type MOD_RES
sequence I
description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI5

242) chain A
residue 103
type MOD_RES
sequence V
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI6

243) chain J
residue 103
type MOD_RES
sequence V
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI6

244) chain B
residue 103
type MOD_RES
sequence V
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI6

245) chain C
residue 103
type MOD_RES
sequence V
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI6

246) chain D
residue 103
type MOD_RES
sequence V
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI6

247) chain E
residue 103
type MOD_RES
sequence V
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI6

248) chain F
residue 103
type MOD_RES
sequence V
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI6

249) chain G
residue 103
type MOD_RES
sequence V
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI6

250) chain H
residue 103
type MOD_RES
sequence V
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI6

251) chain I
residue 103
type MOD_RES
sequence V
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI6

252) chain A
residue 106
type MOD_RES
sequence L
description Phosphoserine => ECO:0000250|UniProtKB:P07632
source Swiss-Prot : SWS_FT_FI7

253) chain J
residue 106
type MOD_RES
sequence L
description Phosphoserine => ECO:0000250|UniProtKB:P07632
source Swiss-Prot : SWS_FT_FI7

254) chain B
residue 106
type MOD_RES
sequence L
description Phosphoserine => ECO:0000250|UniProtKB:P07632
source Swiss-Prot : SWS_FT_FI7

255) chain C
residue 106
type MOD_RES
sequence L
description Phosphoserine => ECO:0000250|UniProtKB:P07632
source Swiss-Prot : SWS_FT_FI7

256) chain D
residue 106
type MOD_RES
sequence L
description Phosphoserine => ECO:0000250|UniProtKB:P07632
source Swiss-Prot : SWS_FT_FI7

257) chain E
residue 106
type MOD_RES
sequence L
description Phosphoserine => ECO:0000250|UniProtKB:P07632
source Swiss-Prot : SWS_FT_FI7

258) chain F
residue 106
type MOD_RES
sequence L
description Phosphoserine => ECO:0000250|UniProtKB:P07632
source Swiss-Prot : SWS_FT_FI7

259) chain G
residue 106
type MOD_RES
sequence L
description Phosphoserine => ECO:0000250|UniProtKB:P07632
source Swiss-Prot : SWS_FT_FI7

260) chain H
residue 106
type MOD_RES
sequence L
description Phosphoserine => ECO:0000250|UniProtKB:P07632
source Swiss-Prot : SWS_FT_FI7

261) chain I
residue 106
type MOD_RES
sequence L
description Phosphoserine => ECO:0000250|UniProtKB:P07632
source Swiss-Prot : SWS_FT_FI7

262) chain A
residue 108
type MOD_RES
sequence G
description Phosphoserine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI8

263) chain J
residue 108
type MOD_RES
sequence G
description Phosphoserine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI8

264) chain B
residue 108
type MOD_RES
sequence G
description Phosphoserine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI8

265) chain C
residue 108
type MOD_RES
sequence G
description Phosphoserine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI8

266) chain D
residue 108
type MOD_RES
sequence G
description Phosphoserine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI8

267) chain E
residue 108
type MOD_RES
sequence G
description Phosphoserine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI8

268) chain F
residue 108
type MOD_RES
sequence G
description Phosphoserine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI8

269) chain G
residue 108
type MOD_RES
sequence G
description Phosphoserine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI8

270) chain H
residue 108
type MOD_RES
sequence G
description Phosphoserine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI8

271) chain I
residue 108
type MOD_RES
sequence G
description Phosphoserine => ECO:0000250|UniProtKB:P08228
source Swiss-Prot : SWS_FT_FI8

272) chain A
residue 123
type MOD_RES
sequence A
description N6-succinyllysine; alternate => ECO:0000269|PubMed:24140062
source Swiss-Prot : SWS_FT_FI9

273) chain J
residue 123
type MOD_RES
sequence A
description N6-succinyllysine; alternate => ECO:0000269|PubMed:24140062
source Swiss-Prot : SWS_FT_FI9

274) chain B
residue 123
type MOD_RES
sequence A
description N6-succinyllysine; alternate => ECO:0000269|PubMed:24140062
source Swiss-Prot : SWS_FT_FI9

275) chain C
residue 123
type MOD_RES
sequence A
description N6-succinyllysine; alternate => ECO:0000269|PubMed:24140062
source Swiss-Prot : SWS_FT_FI9

276) chain D
residue 123
type MOD_RES
sequence A
description N6-succinyllysine; alternate => ECO:0000269|PubMed:24140062
source Swiss-Prot : SWS_FT_FI9

277) chain E
residue 123
type MOD_RES
sequence A
description N6-succinyllysine; alternate => ECO:0000269|PubMed:24140062
source Swiss-Prot : SWS_FT_FI9

278) chain F
residue 123
type MOD_RES
sequence A
description N6-succinyllysine; alternate => ECO:0000269|PubMed:24140062
source Swiss-Prot : SWS_FT_FI9

279) chain G
residue 123
type MOD_RES
sequence A
description N6-succinyllysine; alternate => ECO:0000269|PubMed:24140062
source Swiss-Prot : SWS_FT_FI9

280) chain H
residue 123
type MOD_RES
sequence A
description N6-succinyllysine; alternate => ECO:0000269|PubMed:24140062
source Swiss-Prot : SWS_FT_FI9

281) chain I
residue 123
type MOD_RES
sequence A
description N6-succinyllysine; alternate => ECO:0000269|PubMed:24140062
source Swiss-Prot : SWS_FT_FI9


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