eF-site ID 4qo8-ABCD
PDB Code 4qo8
Chain A, B, C, D

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Title Lactate Dehydrogenase A in complex with substituted 3-Hydroxy-2-mercaptocyclohex-2-enone compound 104
Classification oxidoreductase/oxidoreductase inhibitor
Compound L-lactate dehydrogenase A chain
Source Homo sapiens (Human) (LDHA_HUMAN)
Sequence A:  ATLKDQLIYNLLKEEQTPQNKITVVGVGAVGMACAISILM
KDLADELALVDVIEDKLKGEMMDLQHGSLFLRTPKIVSGK
DYNVTANSKLVIITAGARQQEGESRLNLVQRNVNIFKFII
PNVVKYSPNCKLLIVSNPVDILTYVAWKISGFPKNRVIGS
GCNLDSARFRYLMGERLGVHPLSCHGWVLGEHGDSSVPVW
SGMNVAGVSLKTLHPDLGTDKDKEQWKEVHKQVVESAYEV
IKLKGYTSWAIGLSVADLAESIMKNLRRVHPVSTMIKGLY
GIKDDVFLSVPCILGQNGISDLVKVTLTSEEEARLKKSAD
TLWGIQKELQF
B:  ATLKDQLIYNLLKEEQTPQNKITVVGVGAVGMACAISILM
KDLADELALVDVIEDKLKGEMMDLQHGSLFLRTPKIVSGK
DYNVTANSKLVIITAGARQQEGESRLNLVQRNVNIFKFII
PNVVKYSPNCKLLIVSNPVDILTYVAWKISGFPKNRVIGS
GCNLDSARFRYLMGERLGVHPLSCHGWVLGEHGDSSVPVW
SGMNVAGVSLKTLHPDLGTDKDKEQWKEVHKQVVESAYEV
IKLKGYTSWAIGLSVADLAESIMKNLRRVHPVSTMIKGLY
GIKDDVFLSVPCILGQNGISDLVKVTLTSEEEARLKKSAD
TLWGIQKELQF
C:  ATLKDQLIYNLLKEEQTPQNKITVVGVGAVGMACAISILM
KDLADELALVDVIEDKLKGEMMDLQHGSLFLRTPKIVSGK
DYNVTANSKLVIITAGARQQEGESRLNLVQRNVNIFKFII
PNVVKYSPNCKLLIVSNPVDILTYVAWKISGFPKNRVIGS
GCNLDSARFRYLMGERLGVHPLSCHGWVLGEHGDSSVPVW
SGMNVAGVSLKTLHPDLGTDKDKEQWKEVHKQVVESAYEV
IKLKGYTSWAIGLSVADLAESIMKNLRRVHPVSTMIKGLY
GIKDDVFLSVPCILGQNGISDLVKVTLTSEEEARLKKSAD
TLWGIQKELQF
D:  ATLKDQLIYNLLKEEQTPQNKITVVGVGAVGMACAISILM
KDLADELALVDVIEDKLKGEMMDLQHGSLFLRTPKIVSGK
DYNVTANSKLVIITAGARQQEGESRLNLVQRNVNIFKFII
PNVVKYSPNCKLLIVSNPVDILTYVAWKISGFPKNRVIGS
GCNLDSARFRYLMGERLGVHPLSCHGWVLGEHGDSSVPVW
SGMNVAGVSLKTLHPDLGTDKDKEQWKEVHKQVVESAYEV
IKLKGYTSWAIGLSVADLAESIMKNLRRVHPVSTMIKGLY
GIKDDVFLSVPCILGQNGISDLVKVTLTSEEEARLKKSAD
TLWGIQKELQF
Description


Functional site

1) chain A
residue 28
type
sequence G
description BINDING SITE FOR RESIDUE NAI A 801
source : AC1

2) chain A
residue 29
type
sequence A
description BINDING SITE FOR RESIDUE NAI A 801
source : AC1

3) chain A
residue 30
type
sequence V
description BINDING SITE FOR RESIDUE NAI A 801
source : AC1

4) chain A
residue 51
type
sequence D
description BINDING SITE FOR RESIDUE NAI A 801
source : AC1

5) chain A
residue 52
type
sequence V
description BINDING SITE FOR RESIDUE NAI A 801
source : AC1

6) chain A
residue 53
type
sequence I
description BINDING SITE FOR RESIDUE NAI A 801
source : AC1

7) chain A
residue 94
type
sequence T
description BINDING SITE FOR RESIDUE NAI A 801
source : AC1

8) chain A
residue 95
type
sequence A
description BINDING SITE FOR RESIDUE NAI A 801
source : AC1

9) chain A
residue 96
type
sequence G
description BINDING SITE FOR RESIDUE NAI A 801
source : AC1

10) chain A
residue 98
type
sequence R
description BINDING SITE FOR RESIDUE NAI A 801
source : AC1

11) chain A
residue 115
type
sequence I
description BINDING SITE FOR RESIDUE NAI A 801
source : AC1

12) chain A
residue 119
type
sequence I
description BINDING SITE FOR RESIDUE NAI A 801
source : AC1

13) chain A
residue 135
type
sequence V
description BINDING SITE FOR RESIDUE NAI A 801
source : AC1

14) chain A
residue 136
type
sequence S
description BINDING SITE FOR RESIDUE NAI A 801
source : AC1

15) chain A
residue 137
type
sequence N
description BINDING SITE FOR RESIDUE NAI A 801
source : AC1

16) chain A
residue 160
type
sequence S
description BINDING SITE FOR RESIDUE NAI A 801
source : AC1

17) chain A
residue 192
type
sequence H
description BINDING SITE FOR RESIDUE NAI A 801
source : AC1

18) chain A
residue 247
type
sequence T
description BINDING SITE FOR RESIDUE NAI A 801
source : AC1

19) chain A
residue 251
type
sequence I
description BINDING SITE FOR RESIDUE NAI A 801
source : AC1

20) chain A
residue 147
type
sequence W
description BINDING SITE FOR RESIDUE EPE A 802
source : AC2

21) chain A
residue 151
type
sequence G
description BINDING SITE FOR RESIDUE EPE A 802
source : AC2

22) chain A
residue 152
type
sequence F
description BINDING SITE FOR RESIDUE EPE A 802
source : AC2

23) chain A
residue 154
type
sequence K
description BINDING SITE FOR RESIDUE EPE A 802
source : AC2

24) chain A
residue 170
type
sequence R
description BINDING SITE FOR RESIDUE SO4 A 803
source : AC3

25) chain A
residue 185
type
sequence H
description BINDING SITE FOR RESIDUE SO4 A 803
source : AC3

26) chain C
residue 185
type
sequence H
description BINDING SITE FOR RESIDUE SO4 A 803
source : AC3

27) chain A
residue 137
type
sequence N
description BINDING SITE FOR RESIDUE 36U A 804
source : AC4

28) chain A
residue 165
type
sequence D
description BINDING SITE FOR RESIDUE 36U A 804
source : AC4

29) chain A
residue 168
type
sequence R
description BINDING SITE FOR RESIDUE 36U A 804
source : AC4

30) chain A
residue 192
type
sequence H
description BINDING SITE FOR RESIDUE 36U A 804
source : AC4

31) chain A
residue 193
type
sequence G
description BINDING SITE FOR RESIDUE 36U A 804
source : AC4

32) chain A
residue 237
type
sequence A
description BINDING SITE FOR RESIDUE 36U A 804
source : AC4

33) chain A
residue 238
type
sequence Y
description BINDING SITE FOR RESIDUE 36U A 804
source : AC4

34) chain A
residue 241
type
sequence I
description BINDING SITE FOR RESIDUE 36U A 804
source : AC4

35) chain A
residue 247
type
sequence T
description BINDING SITE FOR RESIDUE 36U A 804
source : AC4

36) chain B
residue 28
type
sequence G
description BINDING SITE FOR RESIDUE NAI B 801
source : AC5

37) chain B
residue 29
type
sequence A
description BINDING SITE FOR RESIDUE NAI B 801
source : AC5

38) chain B
residue 30
type
sequence V
description BINDING SITE FOR RESIDUE NAI B 801
source : AC5

39) chain B
residue 51
type
sequence D
description BINDING SITE FOR RESIDUE NAI B 801
source : AC5

40) chain B
residue 52
type
sequence V
description BINDING SITE FOR RESIDUE NAI B 801
source : AC5

41) chain B
residue 53
type
sequence I
description BINDING SITE FOR RESIDUE NAI B 801
source : AC5

42) chain B
residue 56
type
sequence K
description BINDING SITE FOR RESIDUE NAI B 801
source : AC5

43) chain B
residue 94
type
sequence T
description BINDING SITE FOR RESIDUE NAI B 801
source : AC5

44) chain B
residue 95
type
sequence A
description BINDING SITE FOR RESIDUE NAI B 801
source : AC5

45) chain B
residue 96
type
sequence G
description BINDING SITE FOR RESIDUE NAI B 801
source : AC5

46) chain B
residue 97
type
sequence A
description BINDING SITE FOR RESIDUE NAI B 801
source : AC5

47) chain B
residue 98
type
sequence R
description BINDING SITE FOR RESIDUE NAI B 801
source : AC5

48) chain B
residue 99
type
sequence Q
description BINDING SITE FOR RESIDUE NAI B 801
source : AC5

49) chain B
residue 115
type
sequence I
description BINDING SITE FOR RESIDUE NAI B 801
source : AC5

50) chain B
residue 119
type
sequence I
description BINDING SITE FOR RESIDUE NAI B 801
source : AC5

51) chain B
residue 135
type
sequence V
description BINDING SITE FOR RESIDUE NAI B 801
source : AC5

52) chain B
residue 137
type
sequence N
description BINDING SITE FOR RESIDUE NAI B 801
source : AC5

53) chain B
residue 160
type
sequence S
description BINDING SITE FOR RESIDUE NAI B 801
source : AC5

54) chain B
residue 164
type
sequence L
description BINDING SITE FOR RESIDUE NAI B 801
source : AC5

55) chain B
residue 192
type
sequence H
description BINDING SITE FOR RESIDUE NAI B 801
source : AC5

56) chain B
residue 247
type
sequence T
description BINDING SITE FOR RESIDUE NAI B 801
source : AC5

57) chain B
residue 251
type
sequence I
description BINDING SITE FOR RESIDUE NAI B 801
source : AC5

58) chain A
residue 283
type
sequence K
description BINDING SITE FOR RESIDUE EPE B 802
source : AC6

59) chain B
residue 147
type
sequence W
description BINDING SITE FOR RESIDUE EPE B 802
source : AC6

60) chain B
residue 151
type
sequence G
description BINDING SITE FOR RESIDUE EPE B 802
source : AC6

61) chain B
residue 153
type
sequence P
description BINDING SITE FOR RESIDUE EPE B 802
source : AC6

62) chain B
residue 154
type
sequence K
description BINDING SITE FOR RESIDUE EPE B 802
source : AC6

63) chain B
residue 99
type
sequence Q
description BINDING SITE FOR RESIDUE LAC B 803
source : AC7

64) chain B
residue 105
type
sequence R
description BINDING SITE FOR RESIDUE LAC B 803
source : AC7

65) chain B
residue 137
type
sequence N
description BINDING SITE FOR RESIDUE LAC B 803
source : AC7

66) chain B
residue 168
type
sequence R
description BINDING SITE FOR RESIDUE LAC B 803
source : AC7

67) chain B
residue 192
type
sequence H
description BINDING SITE FOR RESIDUE LAC B 803
source : AC7

68) chain B
residue 237
type
sequence A
description BINDING SITE FOR RESIDUE LAC B 803
source : AC7

69) chain B
residue 247
type
sequence T
description BINDING SITE FOR RESIDUE LAC B 803
source : AC7

70) chain B
residue 170
type
sequence R
description BINDING SITE FOR RESIDUE SO4 B 804
source : AC8

71) chain B
residue 185
type
sequence H
description BINDING SITE FOR RESIDUE SO4 B 804
source : AC8

72) chain D
residue 185
type
sequence H
description BINDING SITE FOR RESIDUE SO4 B 804
source : AC8

73) chain C
residue 28
type
sequence G
description BINDING SITE FOR RESIDUE NAI C 801
source : AC9

74) chain C
residue 29
type
sequence A
description BINDING SITE FOR RESIDUE NAI C 801
source : AC9

75) chain C
residue 30
type
sequence V
description BINDING SITE FOR RESIDUE NAI C 801
source : AC9

76) chain C
residue 51
type
sequence D
description BINDING SITE FOR RESIDUE NAI C 801
source : AC9

77) chain C
residue 52
type
sequence V
description BINDING SITE FOR RESIDUE NAI C 801
source : AC9

78) chain C
residue 53
type
sequence I
description BINDING SITE FOR RESIDUE NAI C 801
source : AC9

79) chain C
residue 94
type
sequence T
description BINDING SITE FOR RESIDUE NAI C 801
source : AC9

80) chain C
residue 95
type
sequence A
description BINDING SITE FOR RESIDUE NAI C 801
source : AC9

81) chain C
residue 96
type
sequence G
description BINDING SITE FOR RESIDUE NAI C 801
source : AC9

82) chain C
residue 115
type
sequence I
description BINDING SITE FOR RESIDUE NAI C 801
source : AC9

83) chain C
residue 135
type
sequence V
description BINDING SITE FOR RESIDUE NAI C 801
source : AC9

84) chain C
residue 136
type
sequence S
description BINDING SITE FOR RESIDUE NAI C 801
source : AC9

85) chain C
residue 137
type
sequence N
description BINDING SITE FOR RESIDUE NAI C 801
source : AC9

86) chain C
residue 192
type
sequence H
description BINDING SITE FOR RESIDUE NAI C 801
source : AC9

87) chain C
residue 247
type
sequence T
description BINDING SITE FOR RESIDUE NAI C 801
source : AC9

88) chain C
residue 147
type
sequence W
description BINDING SITE FOR RESIDUE EPE C 802
source : BC1

89) chain C
residue 151
type
sequence G
description BINDING SITE FOR RESIDUE EPE C 802
source : BC1

90) chain C
residue 152
type
sequence F
description BINDING SITE FOR RESIDUE EPE C 802
source : BC1

91) chain C
residue 153
type
sequence P
description BINDING SITE FOR RESIDUE EPE C 802
source : BC1

92) chain C
residue 154
type
sequence K
description BINDING SITE FOR RESIDUE EPE C 802
source : BC1

93) chain A
residue 182
type
sequence L
description BINDING SITE FOR RESIDUE SO4 C 803
source : BC2

94) chain A
residue 185
type
sequence H
description BINDING SITE FOR RESIDUE SO4 C 803
source : BC2

95) chain C
residue 170
type
sequence R
description BINDING SITE FOR RESIDUE SO4 C 803
source : BC2

96) chain C
residue 185
type
sequence H
description BINDING SITE FOR RESIDUE SO4 C 803
source : BC2

97) chain C
residue 137
type
sequence N
description BINDING SITE FOR RESIDUE 36U C 804
source : BC3

98) chain C
residue 165
type
sequence D
description BINDING SITE FOR RESIDUE 36U C 804
source : BC3

99) chain C
residue 168
type
sequence R
description BINDING SITE FOR RESIDUE 36U C 804
source : BC3

100) chain C
residue 192
type
sequence H
description BINDING SITE FOR RESIDUE 36U C 804
source : BC3

101) chain C
residue 193
type
sequence G
description BINDING SITE FOR RESIDUE 36U C 804
source : BC3

102) chain C
residue 237
type
sequence A
description BINDING SITE FOR RESIDUE 36U C 804
source : BC3

103) chain C
residue 238
type
sequence Y
description BINDING SITE FOR RESIDUE 36U C 804
source : BC3

104) chain C
residue 101
type
sequence E
description BINDING SITE FOR RESIDUE NAI D 801
source : BC4

105) chain D
residue 28
type
sequence G
description BINDING SITE FOR RESIDUE NAI D 801
source : BC4

106) chain D
residue 29
type
sequence A
description BINDING SITE FOR RESIDUE NAI D 801
source : BC4

107) chain D
residue 30
type
sequence V
description BINDING SITE FOR RESIDUE NAI D 801
source : BC4

108) chain D
residue 51
type
sequence D
description BINDING SITE FOR RESIDUE NAI D 801
source : BC4

109) chain D
residue 52
type
sequence V
description BINDING SITE FOR RESIDUE NAI D 801
source : BC4

110) chain D
residue 53
type
sequence I
description BINDING SITE FOR RESIDUE NAI D 801
source : BC4

111) chain D
residue 94
type
sequence T
description BINDING SITE FOR RESIDUE NAI D 801
source : BC4

112) chain D
residue 95
type
sequence A
description BINDING SITE FOR RESIDUE NAI D 801
source : BC4

113) chain D
residue 115
type
sequence I
description BINDING SITE FOR RESIDUE NAI D 801
source : BC4

114) chain D
residue 119
type
sequence I
description BINDING SITE FOR RESIDUE NAI D 801
source : BC4

115) chain D
residue 135
type
sequence V
description BINDING SITE FOR RESIDUE NAI D 801
source : BC4

116) chain D
residue 137
type
sequence N
description BINDING SITE FOR RESIDUE NAI D 801
source : BC4

117) chain D
residue 160
type
sequence S
description BINDING SITE FOR RESIDUE NAI D 801
source : BC4

118) chain D
residue 192
type
sequence H
description BINDING SITE FOR RESIDUE NAI D 801
source : BC4

119) chain D
residue 247
type
sequence T
description BINDING SITE FOR RESIDUE NAI D 801
source : BC4

120) chain B
residue 185
type
sequence H
description BINDING SITE FOR RESIDUE SO4 D 802
source : BC5

121) chain D
residue 170
type
sequence R
description BINDING SITE FOR RESIDUE SO4 D 802
source : BC5

122) chain D
residue 185
type
sequence H
description BINDING SITE FOR RESIDUE SO4 D 802
source : BC5

123) chain D
residue 137
type
sequence N
description BINDING SITE FOR RESIDUE 36U D 803
source : BC6

124) chain D
residue 165
type
sequence D
description BINDING SITE FOR RESIDUE 36U D 803
source : BC6

125) chain D
residue 168
type
sequence R
description BINDING SITE FOR RESIDUE 36U D 803
source : BC6

126) chain D
residue 192
type
sequence H
description BINDING SITE FOR RESIDUE 36U D 803
source : BC6

127) chain D
residue 193
type
sequence G
description BINDING SITE FOR RESIDUE 36U D 803
source : BC6

128) chain D
residue 237
type
sequence A
description BINDING SITE FOR RESIDUE 36U D 803
source : BC6

129) chain D
residue 238
type
sequence Y
description BINDING SITE FOR RESIDUE 36U D 803
source : BC6

130) chain D
residue 241
type
sequence I
description BINDING SITE FOR RESIDUE 36U D 803
source : BC6

131) chain D
residue 247
type
sequence T
description BINDING SITE FOR RESIDUE 36U D 803
source : BC6

132) chain A
residue 192
type ACT_SITE
sequence H
description Proton acceptor
source Swiss-Prot : SWS_FT_FI1

133) chain B
residue 192
type ACT_SITE
sequence H
description Proton acceptor
source Swiss-Prot : SWS_FT_FI1

134) chain C
residue 192
type ACT_SITE
sequence H
description Proton acceptor
source Swiss-Prot : SWS_FT_FI1

135) chain D
residue 192
type ACT_SITE
sequence H
description Proton acceptor
source Swiss-Prot : SWS_FT_FI1

136) chain A
residue 223
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P06151
source Swiss-Prot : SWS_FT_FI10

137) chain D
residue 223
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P06151
source Swiss-Prot : SWS_FT_FI10

138) chain D
residue 231
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P06151
source Swiss-Prot : SWS_FT_FI10

139) chain D
residue 242
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P06151
source Swiss-Prot : SWS_FT_FI10

140) chain A
residue 231
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P06151
source Swiss-Prot : SWS_FT_FI10

141) chain A
residue 242
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P06151
source Swiss-Prot : SWS_FT_FI10

142) chain B
residue 223
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P06151
source Swiss-Prot : SWS_FT_FI10

143) chain B
residue 231
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P06151
source Swiss-Prot : SWS_FT_FI10

144) chain B
residue 242
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P06151
source Swiss-Prot : SWS_FT_FI10

145) chain C
residue 223
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P06151
source Swiss-Prot : SWS_FT_FI10

146) chain C
residue 231
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P06151
source Swiss-Prot : SWS_FT_FI10

147) chain C
residue 242
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P06151
source Swiss-Prot : SWS_FT_FI10

148) chain A
residue 238
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:P06151
source Swiss-Prot : SWS_FT_FI11

149) chain B
residue 238
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:P06151
source Swiss-Prot : SWS_FT_FI11

150) chain C
residue 238
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:P06151
source Swiss-Prot : SWS_FT_FI11

151) chain D
residue 238
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:P06151
source Swiss-Prot : SWS_FT_FI11

152) chain A
residue 28
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:11276087
source Swiss-Prot : SWS_FT_FI2

153) chain A
residue 98
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:11276087
source Swiss-Prot : SWS_FT_FI2

154) chain B
residue 28
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:11276087
source Swiss-Prot : SWS_FT_FI2

155) chain B
residue 98
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:11276087
source Swiss-Prot : SWS_FT_FI2

156) chain C
residue 28
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:11276087
source Swiss-Prot : SWS_FT_FI2

157) chain C
residue 98
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:11276087
source Swiss-Prot : SWS_FT_FI2

158) chain D
residue 28
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:11276087
source Swiss-Prot : SWS_FT_FI2

159) chain D
residue 98
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:11276087
source Swiss-Prot : SWS_FT_FI2

160) chain A
residue 105
type BINDING
sequence R
description
source Swiss-Prot : SWS_FT_FI3

161) chain C
residue 137
type BINDING
sequence N
description
source Swiss-Prot : SWS_FT_FI3

162) chain C
residue 168
type BINDING
sequence R
description
source Swiss-Prot : SWS_FT_FI3

163) chain C
residue 247
type BINDING
sequence T
description
source Swiss-Prot : SWS_FT_FI3

164) chain D
residue 105
type BINDING
sequence R
description
source Swiss-Prot : SWS_FT_FI3

165) chain D
residue 137
type BINDING
sequence N
description
source Swiss-Prot : SWS_FT_FI3

166) chain D
residue 168
type BINDING
sequence R
description
source Swiss-Prot : SWS_FT_FI3

167) chain D
residue 247
type BINDING
sequence T
description
source Swiss-Prot : SWS_FT_FI3

168) chain A
residue 137
type BINDING
sequence N
description
source Swiss-Prot : SWS_FT_FI3

169) chain A
residue 168
type BINDING
sequence R
description
source Swiss-Prot : SWS_FT_FI3

170) chain A
residue 247
type BINDING
sequence T
description
source Swiss-Prot : SWS_FT_FI3

171) chain B
residue 105
type BINDING
sequence R
description
source Swiss-Prot : SWS_FT_FI3

172) chain B
residue 137
type BINDING
sequence N
description
source Swiss-Prot : SWS_FT_FI3

173) chain B
residue 168
type BINDING
sequence R
description
source Swiss-Prot : SWS_FT_FI3

174) chain B
residue 247
type BINDING
sequence T
description
source Swiss-Prot : SWS_FT_FI3

175) chain C
residue 105
type BINDING
sequence R
description
source Swiss-Prot : SWS_FT_FI3

176) chain A
residue 1
type MOD_RES
sequence A
description N-acetylalanine => ECO:0000269|Ref.10, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895
source Swiss-Prot : SWS_FT_FI4

177) chain B
residue 1
type MOD_RES
sequence A
description N-acetylalanine => ECO:0000269|Ref.10, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895
source Swiss-Prot : SWS_FT_FI4

178) chain C
residue 1
type MOD_RES
sequence A
description N-acetylalanine => ECO:0000269|Ref.10, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895
source Swiss-Prot : SWS_FT_FI4

179) chain D
residue 1
type MOD_RES
sequence A
description N-acetylalanine => ECO:0000269|Ref.10, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895
source Swiss-Prot : SWS_FT_FI4

180) chain A
residue 308
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:P04642
source Swiss-Prot : SWS_FT_FI12

181) chain A
residue 321
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:P04642
source Swiss-Prot : SWS_FT_FI12

182) chain B
residue 308
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:P04642
source Swiss-Prot : SWS_FT_FI12

183) chain B
residue 321
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:P04642
source Swiss-Prot : SWS_FT_FI12

184) chain C
residue 308
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:P04642
source Swiss-Prot : SWS_FT_FI12

185) chain C
residue 321
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:P04642
source Swiss-Prot : SWS_FT_FI12

186) chain D
residue 308
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:P04642
source Swiss-Prot : SWS_FT_FI12

187) chain D
residue 321
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:P04642
source Swiss-Prot : SWS_FT_FI12

188) chain A
residue 189-195
type prosite
sequence LGEHGDS
description L_LDH L-lactate dehydrogenase active site. LGEHGDS
source prosite : PS00064

189) chain A
residue 309
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI13

190) chain B
residue 309
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI13

191) chain C
residue 309
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI13

192) chain D
residue 309
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI13

193) chain A
residue 56
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
source Swiss-Prot : SWS_FT_FI14

194) chain B
residue 56
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
source Swiss-Prot : SWS_FT_FI14

195) chain C
residue 56
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
source Swiss-Prot : SWS_FT_FI14

196) chain D
residue 56
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
source Swiss-Prot : SWS_FT_FI14

197) chain A
residue 56
type MOD_RES
sequence K
description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI9

198) chain B
residue 56
type MOD_RES
sequence K
description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI9

199) chain C
residue 56
type MOD_RES
sequence K
description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI9

200) chain D
residue 56
type MOD_RES
sequence K
description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI9

201) chain A
residue 4
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151
source Swiss-Prot : SWS_FT_FI5

202) chain D
residue 4
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151
source Swiss-Prot : SWS_FT_FI5

203) chain D
residue 117
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151
source Swiss-Prot : SWS_FT_FI5

204) chain D
residue 317
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151
source Swiss-Prot : SWS_FT_FI5

205) chain A
residue 117
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151
source Swiss-Prot : SWS_FT_FI5

206) chain A
residue 317
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151
source Swiss-Prot : SWS_FT_FI5

207) chain B
residue 4
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151
source Swiss-Prot : SWS_FT_FI5

208) chain B
residue 117
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151
source Swiss-Prot : SWS_FT_FI5

209) chain B
residue 317
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151
source Swiss-Prot : SWS_FT_FI5

210) chain C
residue 4
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151
source Swiss-Prot : SWS_FT_FI5

211) chain C
residue 117
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151
source Swiss-Prot : SWS_FT_FI5

212) chain C
residue 317
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06151
source Swiss-Prot : SWS_FT_FI5

213) chain A
residue 9
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI6

214) chain B
residue 9
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI6

215) chain C
residue 9
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI6

216) chain D
residue 9
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI6

217) chain A
residue 13
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI7

218) chain D
residue 13
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI7

219) chain D
residue 80
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI7

220) chain D
residue 125
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI7

221) chain A
residue 80
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI7

222) chain A
residue 125
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI7

223) chain B
residue 13
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI7

224) chain B
residue 80
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI7

225) chain B
residue 125
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI7

226) chain C
residue 13
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI7

227) chain C
residue 80
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI7

228) chain C
residue 125
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI7

229) chain A
residue 17
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI8

230) chain B
residue 17
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI8

231) chain C
residue 17
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI8

232) chain D
residue 17
type MOD_RES
sequence T
description Phosphothreonine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI8


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