eF-site ID 1bh5-ABCD
PDB Code 1bh5
Chain A, B, C, D

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Title HUMAN GLYOXALASE I Q33E, E172Q DOUBLE MUTANT
Classification LYASE
Compound LACTOYLGLUTATHIONE LYASE
Source Homo sapiens (Human) (LGUL_HUMAN)
Sequence A:  SGGLTDEAALSCCSDADPSTKDFLLQETMLRVKDPKKSLD
FYTRVLGMTLIQKCDFPIMKFSLYFLAYEDKNDIPKEKDE
KIAWALSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGH
IGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDP
DGYWIQILNPNKMATLM
B:  EPQPPSGGLTDEAALSCCSDADPSTKDFLLQETMLRVKDP
KKSLDFYTRVLGMTLIQKCDFPIMKFSLYFLAYEDKNDIP
KEKDEKIAWALSRKATLELTHNWGTEDDETQSYHNGNSDP
RGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLA
FIQDPDGYWIQILNPNKMATLM
C:  SGGLTDEAALSCCSDADPSTKDFLLQETMLRVKDPKKSLD
FYTRVLGMTLIQKCDFPIMKFSLYFLAYEDKNDIPKEKDE
KIAWALSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGH
IGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDP
DGYWIQILNPNKMATLM
D:  EPQPPSGGLTDEAALSCCSDADPSTKDFLLQETMLRVKDP
KKSLDFYTRVLGMTLIQKCDFPIMKFSLYFLAYEDKNDIP
KEKDEKIAWALSRKATLELTHNWGTEDDETQSYHNGNSDP
RGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLA
FIQDPDGYWIQILNPNKMATLM
Description


Functional site

1) chain A
residue 33
type
sequence E
description ZINC BINDING SITE AT DIMER INTERFACE.
source : ZN1

2) chain A
residue 99
type
sequence E
description ZINC BINDING SITE AT DIMER INTERFACE.
source : ZN1

3) chain B
residue 126
type
sequence H
description ZINC BINDING SITE AT DIMER INTERFACE.
source : ZN1

4) chain B
residue 172
type
sequence Q
description ZINC BINDING SITE AT DIMER INTERFACE.
source : ZN1

5) chain B
residue 33
type
sequence E
description ZINC BINDING SITE AT DIMER INTERFACE.
source : ZN2

6) chain B
residue 99
type
sequence E
description ZINC BINDING SITE AT DIMER INTERFACE.
source : ZN2

7) chain A
residue 126
type
sequence H
description ZINC BINDING SITE AT DIMER INTERFACE.
source : ZN2

8) chain A
residue 172
type
sequence Q
description ZINC BINDING SITE AT DIMER INTERFACE.
source : ZN2

9) chain C
residue 33
type
sequence E
description ZINC BINDING SITE AT DIMER INTERFACE.
source : ZN3

10) chain C
residue 99
type
sequence E
description ZINC BINDING SITE AT DIMER INTERFACE.
source : ZN3

11) chain D
residue 126
type
sequence H
description ZINC BINDING SITE AT DIMER INTERFACE.
source : ZN3

12) chain D
residue 172
type
sequence Q
description ZINC BINDING SITE AT DIMER INTERFACE.
source : ZN3

13) chain D
residue 33
type
sequence E
description ZINC BINDING SITE AT DIMER INTERFACE.
source : ZN4

14) chain D
residue 99
type
sequence E
description ZINC BINDING SITE AT DIMER INTERFACE.
source : ZN4

15) chain C
residue 126
type
sequence H
description ZINC BINDING SITE AT DIMER INTERFACE.
source : ZN4

16) chain C
residue 172
type
sequence Q
description ZINC BINDING SITE AT DIMER INTERFACE.
source : ZN4

17) chain A
residue 60
type
sequence C
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD2

18) chain A
residue 62
type
sequence F
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD2

19) chain A
residue 65
type
sequence M
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD2

20) chain A
residue 67
type
sequence F
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD2

21) chain A
residue 69
type
sequence L
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD2

22) chain A
residue 71
type
sequence F
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD2

23) chain A
residue 88
type
sequence I
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD2

24) chain A
residue 92
type
sequence L
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD2

25) chain B
residue 157
type
sequence M
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD2

26) chain B
residue 160
type
sequence L
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD2

27) chain B
residue 162
type
sequence F
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD2

28) chain B
residue 174
type
sequence L
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD2

29) chain B
residue 179
type
sequence M
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD2

30) chain B
residue 183
type
sequence M
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD2

31) chain B
residue 60
type
sequence C
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD3

32) chain B
residue 62
type
sequence F
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD3

33) chain B
residue 65
type
sequence M
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD3

34) chain B
residue 67
type
sequence F
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD3

35) chain B
residue 69
type
sequence L
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD3

36) chain B
residue 71
type
sequence F
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD3

37) chain B
residue 88
type
sequence I
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD3

38) chain B
residue 92
type
sequence L
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD3

39) chain A
residue 157
type
sequence M
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD3

40) chain A
residue 160
type
sequence L
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD3

41) chain A
residue 162
type
sequence F
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD3

42) chain A
residue 174
type
sequence L
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD3

43) chain A
residue 179
type
sequence M
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD3

44) chain A
residue 183
type
sequence M
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD3

45) chain C
residue 60
type
sequence C
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD4

46) chain C
residue 62
type
sequence F
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD4

47) chain C
residue 65
type
sequence M
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD4

48) chain C
residue 67
type
sequence F
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD4

49) chain C
residue 69
type
sequence L
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD4

50) chain C
residue 71
type
sequence F
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD4

51) chain C
residue 88
type
sequence I
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD4

52) chain C
residue 92
type
sequence L
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD4

53) chain D
residue 157
type
sequence M
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD4

54) chain D
residue 160
type
sequence L
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD4

55) chain D
residue 162
type
sequence F
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD4

56) chain D
residue 174
type
sequence L
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD4

57) chain D
residue 179
type
sequence M
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD4

58) chain D
residue 183
type
sequence M
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD4

59) chain D
residue 60
type
sequence C
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD5

60) chain D
residue 62
type
sequence F
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD5

61) chain D
residue 65
type
sequence M
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD5

62) chain D
residue 67
type
sequence F
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD5

63) chain D
residue 69
type
sequence L
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD5

64) chain D
residue 71
type
sequence F
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD5

65) chain D
residue 88
type
sequence I
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD5

66) chain D
residue 92
type
sequence L
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD5

67) chain C
residue 157
type
sequence M
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD5

68) chain C
residue 160
type
sequence L
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD5

69) chain C
residue 162
type
sequence F
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD5

70) chain C
residue 174
type
sequence L
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD5

71) chain C
residue 179
type
sequence M
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD5

72) chain C
residue 183
type
sequence M
description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE.
source : HD5

73) chain B
residue 37
type
sequence R
description BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN1 HYD1 AND GSH1.
source : GH2

74) chain B
residue 103
type
sequence N
description BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN1 HYD1 AND GSH1.
source : GH2

75) chain A
residue 122
type
sequence R
description BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN1 HYD1 AND GSH1.
source : GH2

76) chain A
residue 37
type
sequence R
description BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN2 HYD2 AND GSH2.
source : GH1

77) chain A
residue 103
type
sequence N
description BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN2 HYD2 AND GSH2.
source : GH1

78) chain B
residue 122
type
sequence R
description BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN2 HYD2 AND GSH2.
source : GH1

79) chain D
residue 37
type
sequence R
description BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN1 HYD1 AND GSH1.
source : GH4

80) chain D
residue 103
type
sequence N
description BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN1 HYD1 AND GSH1.
source : GH4

81) chain C
residue 122
type
sequence R
description BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN1 HYD1 AND GSH1.
source : GH4

82) chain C
residue 37
type
sequence R
description BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN2 HYD2 AND GSH2.
source : GH3

83) chain C
residue 103
type
sequence N
description BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN2 HYD2 AND GSH2.
source : GH3

84) chain D
residue 122
type
sequence R
description BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN2 HYD2 AND GSH2.
source : GH3

85) chain A
residue 126
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 201
source : AC1

86) chain A
residue 172
type
sequence Q
description BINDING SITE FOR RESIDUE ZN A 201
source : AC1

87) chain B
residue 33
type
sequence E
description BINDING SITE FOR RESIDUE ZN A 201
source : AC1

88) chain B
residue 99
type
sequence E
description BINDING SITE FOR RESIDUE ZN A 201
source : AC1

89) chain A
residue 33
type
sequence E
description BINDING SITE FOR RESIDUE ZN B 201
source : AC2

90) chain A
residue 99
type
sequence E
description BINDING SITE FOR RESIDUE ZN B 201
source : AC2

91) chain B
residue 126
type
sequence H
description BINDING SITE FOR RESIDUE ZN B 201
source : AC2

92) chain B
residue 172
type
sequence Q
description BINDING SITE FOR RESIDUE ZN B 201
source : AC2

93) chain C
residue 126
type
sequence H
description BINDING SITE FOR RESIDUE ZN C 201
source : AC3

94) chain C
residue 172
type
sequence Q
description BINDING SITE FOR RESIDUE ZN C 201
source : AC3

95) chain D
residue 33
type
sequence E
description BINDING SITE FOR RESIDUE ZN C 201
source : AC3

96) chain D
residue 99
type
sequence E
description BINDING SITE FOR RESIDUE ZN C 201
source : AC3

97) chain C
residue 33
type
sequence E
description BINDING SITE FOR RESIDUE ZN D 201
source : AC4

98) chain C
residue 99
type
sequence E
description BINDING SITE FOR RESIDUE ZN D 201
source : AC4

99) chain D
residue 126
type
sequence H
description BINDING SITE FOR RESIDUE ZN D 201
source : AC4

100) chain D
residue 172
type
sequence Q
description BINDING SITE FOR RESIDUE ZN D 201
source : AC4

101) chain A
residue 122
type
sequence R
description BINDING SITE FOR RESIDUE GTX A 200
source : AC5

102) chain A
residue 157
type
sequence M
description BINDING SITE FOR RESIDUE GTX A 200
source : AC5

103) chain A
residue 162
type
sequence F
description BINDING SITE FOR RESIDUE GTX A 200
source : AC5

104) chain B
residue 37
type
sequence R
description BINDING SITE FOR RESIDUE GTX A 200
source : AC5

105) chain B
residue 60
type
sequence C
description BINDING SITE FOR RESIDUE GTX A 200
source : AC5

106) chain B
residue 67
type
sequence F
description BINDING SITE FOR RESIDUE GTX A 200
source : AC5

107) chain B
residue 92
type
sequence L
description BINDING SITE FOR RESIDUE GTX A 200
source : AC5

108) chain B
residue 101
type
sequence T
description BINDING SITE FOR RESIDUE GTX A 200
source : AC5

109) chain B
residue 103
type
sequence N
description BINDING SITE FOR RESIDUE GTX A 200
source : AC5

110) chain C
residue 17
type
sequence S
description BINDING SITE FOR RESIDUE GTX A 200
source : AC5

111) chain A
residue 37
type
sequence R
description BINDING SITE FOR RESIDUE GTX B 200
source : AC6

112) chain A
residue 60
type
sequence C
description BINDING SITE FOR RESIDUE GTX B 200
source : AC6

113) chain A
residue 67
type
sequence F
description BINDING SITE FOR RESIDUE GTX B 200
source : AC6

114) chain A
residue 101
type
sequence T
description BINDING SITE FOR RESIDUE GTX B 200
source : AC6

115) chain A
residue 103
type
sequence N
description BINDING SITE FOR RESIDUE GTX B 200
source : AC6

116) chain A
residue 139
type
sequence K
description BINDING SITE FOR RESIDUE GTX B 200
source : AC6

117) chain B
residue 122
type
sequence R
description BINDING SITE FOR RESIDUE GTX B 200
source : AC6

118) chain B
residue 150
type
sequence K
description BINDING SITE FOR RESIDUE GTX B 200
source : AC6

119) chain B
residue 157
type
sequence M
description BINDING SITE FOR RESIDUE GTX B 200
source : AC6

120) chain B
residue 162
type
sequence F
description BINDING SITE FOR RESIDUE GTX B 200
source : AC6

121) chain B
residue 183
type
sequence M
description BINDING SITE FOR RESIDUE GTX B 200
source : AC6

122) chain A
residue 17
type
sequence S
description BINDING SITE FOR RESIDUE GTX C 200
source : AC7

123) chain C
residue 122
type
sequence R
description BINDING SITE FOR RESIDUE GTX C 200
source : AC7

124) chain C
residue 157
type
sequence M
description BINDING SITE FOR RESIDUE GTX C 200
source : AC7

125) chain C
residue 160
type
sequence L
description BINDING SITE FOR RESIDUE GTX C 200
source : AC7

126) chain C
residue 162
type
sequence F
description BINDING SITE FOR RESIDUE GTX C 200
source : AC7

127) chain C
residue 179
type
sequence M
description BINDING SITE FOR RESIDUE GTX C 200
source : AC7

128) chain D
residue 37
type
sequence R
description BINDING SITE FOR RESIDUE GTX C 200
source : AC7

129) chain D
residue 60
type
sequence C
description BINDING SITE FOR RESIDUE GTX C 200
source : AC7

130) chain D
residue 67
type
sequence F
description BINDING SITE FOR RESIDUE GTX C 200
source : AC7

131) chain D
residue 92
type
sequence L
description BINDING SITE FOR RESIDUE GTX C 200
source : AC7

132) chain D
residue 103
type
sequence N
description BINDING SITE FOR RESIDUE GTX C 200
source : AC7

133) chain C
residue 37
type
sequence R
description BINDING SITE FOR RESIDUE GTX D 200
source : AC8

134) chain C
residue 60
type
sequence C
description BINDING SITE FOR RESIDUE GTX D 200
source : AC8

135) chain C
residue 67
type
sequence F
description BINDING SITE FOR RESIDUE GTX D 200
source : AC8

136) chain C
residue 101
type
sequence T
description BINDING SITE FOR RESIDUE GTX D 200
source : AC8

137) chain C
residue 103
type
sequence N
description BINDING SITE FOR RESIDUE GTX D 200
source : AC8

138) chain D
residue 122
type
sequence R
description BINDING SITE FOR RESIDUE GTX D 200
source : AC8

139) chain D
residue 160
type
sequence L
description BINDING SITE FOR RESIDUE GTX D 200
source : AC8

140) chain D
residue 162
type
sequence F
description BINDING SITE FOR RESIDUE GTX D 200
source : AC8

141) chain D
residue 183
type
sequence M
description BINDING SITE FOR RESIDUE GTX D 200
source : AC8

142) chain A
residue 173
type ACT_SITE
sequence I
description Proton donor/acceptor => ECO:0000269|PubMed:10521255, ECO:0000269|PubMed:9705294
source Swiss-Prot : SWS_FT_FI1

143) chain B
residue 173
type ACT_SITE
sequence I
description Proton donor/acceptor => ECO:0000269|PubMed:10521255, ECO:0000269|PubMed:9705294
source Swiss-Prot : SWS_FT_FI1

144) chain C
residue 173
type ACT_SITE
sequence I
description Proton donor/acceptor => ECO:0000269|PubMed:10521255, ECO:0000269|PubMed:9705294
source Swiss-Prot : SWS_FT_FI1

145) chain D
residue 173
type ACT_SITE
sequence I
description Proton donor/acceptor => ECO:0000269|PubMed:10521255, ECO:0000269|PubMed:9705294
source Swiss-Prot : SWS_FT_FI1

146) chain A
residue 148
type MOD_RES
sequence F
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CPU0
source Swiss-Prot : SWS_FT_FI10

147) chain B
residue 148
type MOD_RES
sequence F
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CPU0
source Swiss-Prot : SWS_FT_FI10

148) chain C
residue 148
type MOD_RES
sequence F
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CPU0
source Swiss-Prot : SWS_FT_FI10

149) chain D
residue 148
type MOD_RES
sequence F
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CPU0
source Swiss-Prot : SWS_FT_FI10

150) chain A
residue 34
type catalytic
sequence T
description 32
source MCSA : MCSA1

151) chain A
residue 100
type catalytic
sequence L
description 32
source MCSA : MCSA1

152) chain A
residue 127
type catalytic
sequence I
description 32
source MCSA : MCSA1

153) chain A
residue 173
type catalytic
sequence I
description 32
source MCSA : MCSA1

154) chain B
residue 34
type catalytic
sequence T
description 32
source MCSA : MCSA2

155) chain B
residue 100
type catalytic
sequence L
description 32
source MCSA : MCSA2

156) chain B
residue 127
type catalytic
sequence I
description 32
source MCSA : MCSA2

157) chain B
residue 173
type catalytic
sequence I
description 32
source MCSA : MCSA2

158) chain C
residue 34
type catalytic
sequence T
description 32
source MCSA : MCSA3

159) chain C
residue 100
type catalytic
sequence L
description 32
source MCSA : MCSA3

160) chain C
residue 127
type catalytic
sequence I
description 32
source MCSA : MCSA3

161) chain C
residue 173
type catalytic
sequence I
description 32
source MCSA : MCSA3

162) chain D
residue 34
type catalytic
sequence T
description 32
source MCSA : MCSA4

163) chain D
residue 100
type catalytic
sequence L
description 32
source MCSA : MCSA4

164) chain D
residue 127
type catalytic
sequence I
description 32
source MCSA : MCSA4

165) chain D
residue 173
type catalytic
sequence I
description 32
source MCSA : MCSA4

166) chain A
residue 88
type MOD_RES
sequence I
description N6-succinyllysine => ECO:0000250|UniProtKB:Q9CPU0
source Swiss-Prot : SWS_FT_FI7

167) chain B
residue 88
type MOD_RES
sequence I
description N6-succinyllysine => ECO:0000250|UniProtKB:Q9CPU0
source Swiss-Prot : SWS_FT_FI7

168) chain C
residue 88
type MOD_RES
sequence I
description N6-succinyllysine => ECO:0000250|UniProtKB:Q9CPU0
source Swiss-Prot : SWS_FT_FI7

169) chain D
residue 88
type MOD_RES
sequence I
description N6-succinyllysine => ECO:0000250|UniProtKB:Q9CPU0
source Swiss-Prot : SWS_FT_FI7

170) chain A
residue 139
type MOD_RES
sequence K
description S-glutathionyl cysteine; alternate => ECO:0000269|PubMed:20454679
source Swiss-Prot : SWS_FT_FI9

171) chain B
residue 139
type MOD_RES
sequence K
description S-glutathionyl cysteine; alternate => ECO:0000269|PubMed:20454679
source Swiss-Prot : SWS_FT_FI9

172) chain C
residue 139
type MOD_RES
sequence K
description S-glutathionyl cysteine; alternate => ECO:0000269|PubMed:20454679
source Swiss-Prot : SWS_FT_FI9

173) chain D
residue 139
type MOD_RES
sequence K
description S-glutathionyl cysteine; alternate => ECO:0000269|PubMed:20454679
source Swiss-Prot : SWS_FT_FI9

174) chain A
residue 34
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294
source Swiss-Prot : SWS_FT_FI2

175) chain A
residue 100
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294
source Swiss-Prot : SWS_FT_FI2

176) chain B
residue 34
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294
source Swiss-Prot : SWS_FT_FI2

177) chain B
residue 100
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294
source Swiss-Prot : SWS_FT_FI2

178) chain C
residue 34
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294
source Swiss-Prot : SWS_FT_FI2

179) chain C
residue 100
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294
source Swiss-Prot : SWS_FT_FI2

180) chain D
residue 34
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294
source Swiss-Prot : SWS_FT_FI2

181) chain D
residue 100
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294
source Swiss-Prot : SWS_FT_FI2

182) chain A
residue 38
type BINDING
sequence V
description
source Swiss-Prot : SWS_FT_FI3

183) chain A
residue 104
type BINDING
sequence W
description
source Swiss-Prot : SWS_FT_FI3

184) chain B
residue 38
type BINDING
sequence V
description
source Swiss-Prot : SWS_FT_FI3

185) chain B
residue 104
type BINDING
sequence W
description
source Swiss-Prot : SWS_FT_FI3

186) chain C
residue 38
type BINDING
sequence V
description
source Swiss-Prot : SWS_FT_FI3

187) chain C
residue 104
type BINDING
sequence W
description
source Swiss-Prot : SWS_FT_FI3

188) chain D
residue 38
type BINDING
sequence V
description
source Swiss-Prot : SWS_FT_FI3

189) chain D
residue 104
type BINDING
sequence W
description
source Swiss-Prot : SWS_FT_FI3

190) chain A
residue 123
type BINDING
sequence G
description in other chain
source Swiss-Prot : SWS_FT_FI4

191) chain A
residue 157
type BINDING
sequence M
description in other chain
source Swiss-Prot : SWS_FT_FI4

192) chain B
residue 123
type BINDING
sequence G
description in other chain
source Swiss-Prot : SWS_FT_FI4

193) chain B
residue 157
type BINDING
sequence M
description in other chain
source Swiss-Prot : SWS_FT_FI4

194) chain C
residue 123
type BINDING
sequence G
description in other chain
source Swiss-Prot : SWS_FT_FI4

195) chain C
residue 157
type BINDING
sequence M
description in other chain
source Swiss-Prot : SWS_FT_FI4

196) chain D
residue 123
type BINDING
sequence G
description in other chain
source Swiss-Prot : SWS_FT_FI4

197) chain D
residue 157
type BINDING
sequence M
description in other chain
source Swiss-Prot : SWS_FT_FI4

198) chain A
residue 117-133
type prosite
sequence GNSDPRGFGHIGIAVPD
description GLYOXALASE_I_2 Glyoxalase I signature 2. GNsdpr.GFGHIGiAvpD
source prosite : PS00935

199) chain A
residue 127
type BINDING
sequence I
description in other chain => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294
source Swiss-Prot : SWS_FT_FI5

200) chain A
residue 173
type BINDING
sequence I
description in other chain => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294
source Swiss-Prot : SWS_FT_FI5

201) chain B
residue 127
type BINDING
sequence I
description in other chain => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294
source Swiss-Prot : SWS_FT_FI5

202) chain B
residue 173
type BINDING
sequence I
description in other chain => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294
source Swiss-Prot : SWS_FT_FI5

203) chain C
residue 127
type BINDING
sequence I
description in other chain => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294
source Swiss-Prot : SWS_FT_FI5

204) chain C
residue 173
type BINDING
sequence I
description in other chain => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294
source Swiss-Prot : SWS_FT_FI5

205) chain D
residue 127
type BINDING
sequence I
description in other chain => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294
source Swiss-Prot : SWS_FT_FI5

206) chain D
residue 173
type BINDING
sequence I
description in other chain => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294
source Swiss-Prot : SWS_FT_FI5

207) chain B
residue 2
type MOD_RES
sequence E
description N-acetylalanine => ECO:0000269|PubMed:20454679, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:25944712
source Swiss-Prot : SWS_FT_FI6

208) chain D
residue 2
type MOD_RES
sequence E
description N-acetylalanine => ECO:0000269|PubMed:20454679, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:25944712
source Swiss-Prot : SWS_FT_FI6

209) chain A
residue 107
type MOD_RES
sequence E
description Phosphothreonine => ECO:0000269|PubMed:19199007
source Swiss-Prot : SWS_FT_FI8

210) chain B
residue 107
type MOD_RES
sequence E
description Phosphothreonine => ECO:0000269|PubMed:19199007
source Swiss-Prot : SWS_FT_FI8

211) chain C
residue 107
type MOD_RES
sequence E
description Phosphothreonine => ECO:0000269|PubMed:19199007
source Swiss-Prot : SWS_FT_FI8

212) chain D
residue 107
type MOD_RES
sequence E
description Phosphothreonine => ECO:0000269|PubMed:19199007
source Swiss-Prot : SWS_FT_FI8


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