eF-site ID 1j1z-ABCD
PDB Code 1j1z
Chain A, B, C, D

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Title Crystal Structure of Thermus thermophilus HB8 Argininosuccinate Synthetase in complex with substrate
Classification LIGASE
Compound Argininosuccinate Synthetase
Source Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) (ASSY_THET8)
Sequence A:  MKIVLAYSGGLDTSIILKWLKETYRAEVIAFTADIGQGEE
VEEAREKALRTGASKAIALDLKEEFVRDFVFPMMRAGAVY
EGYYLLGTSIARPLIAKHLVRIAEEEGAEAIAHGATGKGN
DQVRFELTAYALKPDIKVIAPWREWSFQGRKEMIAYAEAH
GIPVPPYSMDANLLHISYEGGVLEDPWAEPPKGMFRMTQD
PEEAPDAPEYVEVEFFEGDPVAVNGERLSPAALLQRLNEI
GGRHGVGRVDIVENRFVGMKSRGVYETPGGTILYHARRAV
ESLTLDREVLHQRDMLSPKYAELVYYGFWYAPEREALQAY
FDHVARSVTGVARLKLYKGNVYVVGRKAPKSLYRQDLVSF
GYDQKDAEGFIKIQALRLRVRALVER
B:  MKIVLAYSGGLDTSIILKWLKETYRAEVIAFTADIGQGEE
VEEAREKALRTGASKAIALDLKEEFVRDFVFPMMRAGAVY
EGYYLLGTSIARPLIAKHLVRIAEEEGAEAIAHGATGKGN
DQVRFELTAYALKPDIKVIAPWREWSFQGRKEMIAYAEAH
GIPVPPYSMDANLLHISYEGGVLEDPWAEPPKGMFRMTQD
PEEAPDAPEYVEVEFFEGDPVAVNGERLSPAALLQRLNEI
GGRHGVGRVDIVENRFVGMKSRGVYETPGGTILYHARRAV
ESLTLDREVLHQRDMLSPKYAELVYYGFWYAPEREALQAY
FDHVARSVTGVARLKLYKGNVYVVGRKAPKSLYRQDLVSF
GYDQKDAEGFIKIQALRLRVRALVER
C:  MKIVLAYSGGLDTSIILKWLKETYRAEVIAFTADIGQGEE
VEEAREKALRTGASKAIALDLKEEFVRDFVFPMMRAGAVY
EGYYLLGTSIARPLIAKHLVRIAEEEGAEAIAHGATGKGN
DQVRFELTAYALKPDIKVIAPWREWSFQGRKEMIAYAEAH
GIPVPPYSMDANLLHISYEGGVLEDPWAEPPKGMFRMTQD
PEEAPDAPEYVEVEFFEGDPVAVNGERLSPAALLQRLNEI
GGRHGVGRVDIVENRFVGMKSRGVYETPGGTILYHARRAV
ESLTLDREVLHQRDMLSPKYAELVYYGFWYAPEREALQAY
FDHVARSVTGVARLKLYKGNVYVVGRKAPKSLYRQDLVSF
GYDQKDAEGFIKIQALRLRVRALVER
D:  MKIVLAYSGGLDTSIILKWLKETYRAEVIAFTADIGQGEE
VEEAREKALRTGASKAIALDLKEEFVRDFVFPMMRAGAVY
EGYYLLGTSIARPLIAKHLVRIAEEEGAEAIAHGATGKGN
DQVRFELTAYALKPDIKVIAPWREWSFQGRKEMIAYAEAH
GIPVPPYSMDANLLHISYEGGVLEDPWAEPPKGMFRMTQD
PEEAPDAPEYVEVEFFEGDPVAVNGERLSPAALLQRLNEI
GGRHGVGRVDIVENRFVGMKSRGVYETPGGTILYHARRAV
ESLTLDREVLHQRDMLSPKYAELVYYGFWYAPEREALQAY
FDHVARSVTGVARLKLYKGNVYVVGRKAPKSLYRQDLVSF
GYDQKDAEGFIKIQALRLRVRALVER
Description


Functional site

1) chain A
residue 6
type
sequence A
description BINDING SITE FOR RESIDUE ATP A 510
source : AC1

2) chain A
residue 8
type
sequence S
description BINDING SITE FOR RESIDUE ATP A 510
source : AC1

3) chain A
residue 12
type
sequence D
description BINDING SITE FOR RESIDUE ATP A 510
source : AC1

4) chain A
residue 13
type
sequence T
description BINDING SITE FOR RESIDUE ATP A 510
source : AC1

5) chain A
residue 31
type
sequence F
description BINDING SITE FOR RESIDUE ATP A 510
source : AC1

6) chain A
residue 32
type
sequence T
description BINDING SITE FOR RESIDUE ATP A 510
source : AC1

7) chain A
residue 33
type
sequence A
description BINDING SITE FOR RESIDUE ATP A 510
source : AC1

8) chain A
residue 37
type
sequence Q
description BINDING SITE FOR RESIDUE ATP A 510
source : AC1

9) chain A
residue 92
type
sequence R
description BINDING SITE FOR RESIDUE ATP A 510
source : AC1

10) chain A
residue 113
type
sequence H
description BINDING SITE FOR RESIDUE ATP A 510
source : AC1

11) chain A
residue 114
type
sequence G
description BINDING SITE FOR RESIDUE ATP A 510
source : AC1

12) chain A
residue 125
type
sequence F
description BINDING SITE FOR RESIDUE ATP A 510
source : AC1

13) chain A
residue 173
type
sequence S
description BINDING SITE FOR RESIDUE ATP A 510
source : AC1

14) chain A
residue 175
type
sequence D
description BINDING SITE FOR RESIDUE ATP A 510
source : AC1

15) chain B
residue 6
type
sequence A
description BINDING SITE FOR RESIDUE ATP B 2510
source : AC2

16) chain B
residue 7
type
sequence Y
description BINDING SITE FOR RESIDUE ATP B 2510
source : AC2

17) chain B
residue 8
type
sequence S
description BINDING SITE FOR RESIDUE ATP B 2510
source : AC2

18) chain B
residue 10
type
sequence G
description BINDING SITE FOR RESIDUE ATP B 2510
source : AC2

19) chain B
residue 12
type
sequence D
description BINDING SITE FOR RESIDUE ATP B 2510
source : AC2

20) chain B
residue 13
type
sequence T
description BINDING SITE FOR RESIDUE ATP B 2510
source : AC2

21) chain B
residue 31
type
sequence F
description BINDING SITE FOR RESIDUE ATP B 2510
source : AC2

22) chain B
residue 32
type
sequence T
description BINDING SITE FOR RESIDUE ATP B 2510
source : AC2

23) chain B
residue 33
type
sequence A
description BINDING SITE FOR RESIDUE ATP B 2510
source : AC2

24) chain B
residue 37
type
sequence Q
description BINDING SITE FOR RESIDUE ATP B 2510
source : AC2

25) chain B
residue 92
type
sequence R
description BINDING SITE FOR RESIDUE ATP B 2510
source : AC2

26) chain B
residue 113
type
sequence H
description BINDING SITE FOR RESIDUE ATP B 2510
source : AC2

27) chain B
residue 114
type
sequence G
description BINDING SITE FOR RESIDUE ATP B 2510
source : AC2

28) chain B
residue 125
type
sequence F
description BINDING SITE FOR RESIDUE ATP B 2510
source : AC2

29) chain C
residue 6
type
sequence A
description BINDING SITE FOR RESIDUE ATP C 3510
source : AC3

30) chain C
residue 8
type
sequence S
description BINDING SITE FOR RESIDUE ATP C 3510
source : AC3

31) chain C
residue 12
type
sequence D
description BINDING SITE FOR RESIDUE ATP C 3510
source : AC3

32) chain C
residue 13
type
sequence T
description BINDING SITE FOR RESIDUE ATP C 3510
source : AC3

33) chain C
residue 31
type
sequence F
description BINDING SITE FOR RESIDUE ATP C 3510
source : AC3

34) chain C
residue 32
type
sequence T
description BINDING SITE FOR RESIDUE ATP C 3510
source : AC3

35) chain C
residue 33
type
sequence A
description BINDING SITE FOR RESIDUE ATP C 3510
source : AC3

36) chain C
residue 37
type
sequence Q
description BINDING SITE FOR RESIDUE ATP C 3510
source : AC3

37) chain C
residue 92
type
sequence R
description BINDING SITE FOR RESIDUE ATP C 3510
source : AC3

38) chain C
residue 95
type
sequence I
description BINDING SITE FOR RESIDUE ATP C 3510
source : AC3

39) chain C
residue 113
type
sequence H
description BINDING SITE FOR RESIDUE ATP C 3510
source : AC3

40) chain C
residue 114
type
sequence G
description BINDING SITE FOR RESIDUE ATP C 3510
source : AC3

41) chain C
residue 115
type
sequence A
description BINDING SITE FOR RESIDUE ATP C 3510
source : AC3

42) chain C
residue 125
type
sequence F
description BINDING SITE FOR RESIDUE ATP C 3510
source : AC3

43) chain C
residue 173
type
sequence S
description BINDING SITE FOR RESIDUE ATP C 3510
source : AC3

44) chain C
residue 175
type
sequence D
description BINDING SITE FOR RESIDUE ATP C 3510
source : AC3

45) chain D
residue 6
type
sequence A
description BINDING SITE FOR RESIDUE ATP D 4510
source : AC4

46) chain D
residue 7
type
sequence Y
description BINDING SITE FOR RESIDUE ATP D 4510
source : AC4

47) chain D
residue 8
type
sequence S
description BINDING SITE FOR RESIDUE ATP D 4510
source : AC4

48) chain D
residue 10
type
sequence G
description BINDING SITE FOR RESIDUE ATP D 4510
source : AC4

49) chain D
residue 11
type
sequence L
description BINDING SITE FOR RESIDUE ATP D 4510
source : AC4

50) chain D
residue 12
type
sequence D
description BINDING SITE FOR RESIDUE ATP D 4510
source : AC4

51) chain D
residue 13
type
sequence T
description BINDING SITE FOR RESIDUE ATP D 4510
source : AC4

52) chain D
residue 31
type
sequence F
description BINDING SITE FOR RESIDUE ATP D 4510
source : AC4

53) chain D
residue 33
type
sequence A
description BINDING SITE FOR RESIDUE ATP D 4510
source : AC4

54) chain D
residue 37
type
sequence Q
description BINDING SITE FOR RESIDUE ATP D 4510
source : AC4

55) chain D
residue 92
type
sequence R
description BINDING SITE FOR RESIDUE ATP D 4510
source : AC4

56) chain D
residue 113
type
sequence H
description BINDING SITE FOR RESIDUE ATP D 4510
source : AC4

57) chain D
residue 114
type
sequence G
description BINDING SITE FOR RESIDUE ATP D 4510
source : AC4

58) chain D
residue 125
type
sequence F
description BINDING SITE FOR RESIDUE ATP D 4510
source : AC4

59) chain A
residue 84
type
sequence Y
description BINDING SITE FOR RESIDUE CIR A 520
source : AC5

60) chain A
residue 88
type
sequence T
description BINDING SITE FOR RESIDUE CIR A 520
source : AC5

61) chain A
residue 89
type
sequence S
description BINDING SITE FOR RESIDUE CIR A 520
source : AC5

62) chain A
residue 120
type
sequence N
description BINDING SITE FOR RESIDUE CIR A 520
source : AC5

63) chain A
residue 124
type
sequence R
description BINDING SITE FOR RESIDUE CIR A 520
source : AC5

64) chain A
residue 173
type
sequence S
description BINDING SITE FOR RESIDUE CIR A 520
source : AC5

65) chain A
residue 174
type
sequence M
description BINDING SITE FOR RESIDUE CIR A 520
source : AC5

66) chain A
residue 182
type
sequence S
description BINDING SITE FOR RESIDUE CIR A 520
source : AC5

67) chain A
residue 184
type
sequence E
description BINDING SITE FOR RESIDUE CIR A 520
source : AC5

68) chain A
residue 258
type
sequence E
description BINDING SITE FOR RESIDUE CIR A 520
source : AC5

69) chain A
residue 270
type
sequence Y
description BINDING SITE FOR RESIDUE CIR A 520
source : AC5

70) chain A
residue 310
type
sequence Y
description BINDING SITE FOR RESIDUE CIR A 520
source : AC5

71) chain B
residue 84
type
sequence Y
description BINDING SITE FOR RESIDUE CIR B 2520
source : AC6

72) chain B
residue 88
type
sequence T
description BINDING SITE FOR RESIDUE CIR B 2520
source : AC6

73) chain B
residue 89
type
sequence S
description BINDING SITE FOR RESIDUE CIR B 2520
source : AC6

74) chain B
residue 120
type
sequence N
description BINDING SITE FOR RESIDUE CIR B 2520
source : AC6

75) chain B
residue 124
type
sequence R
description BINDING SITE FOR RESIDUE CIR B 2520
source : AC6

76) chain B
residue 173
type
sequence S
description BINDING SITE FOR RESIDUE CIR B 2520
source : AC6

77) chain B
residue 174
type
sequence M
description BINDING SITE FOR RESIDUE CIR B 2520
source : AC6

78) chain B
residue 175
type
sequence D
description BINDING SITE FOR RESIDUE CIR B 2520
source : AC6

79) chain B
residue 182
type
sequence S
description BINDING SITE FOR RESIDUE CIR B 2520
source : AC6

80) chain B
residue 184
type
sequence E
description BINDING SITE FOR RESIDUE CIR B 2520
source : AC6

81) chain B
residue 258
type
sequence E
description BINDING SITE FOR RESIDUE CIR B 2520
source : AC6

82) chain B
residue 270
type
sequence Y
description BINDING SITE FOR RESIDUE CIR B 2520
source : AC6

83) chain B
residue 310
type
sequence Y
description BINDING SITE FOR RESIDUE CIR B 2520
source : AC6

84) chain C
residue 84
type
sequence Y
description BINDING SITE FOR RESIDUE CIR C 3520
source : AC7

85) chain C
residue 88
type
sequence T
description BINDING SITE FOR RESIDUE CIR C 3520
source : AC7

86) chain C
residue 89
type
sequence S
description BINDING SITE FOR RESIDUE CIR C 3520
source : AC7

87) chain C
residue 120
type
sequence N
description BINDING SITE FOR RESIDUE CIR C 3520
source : AC7

88) chain C
residue 121
type
sequence D
description BINDING SITE FOR RESIDUE CIR C 3520
source : AC7

89) chain C
residue 124
type
sequence R
description BINDING SITE FOR RESIDUE CIR C 3520
source : AC7

90) chain C
residue 173
type
sequence S
description BINDING SITE FOR RESIDUE CIR C 3520
source : AC7

91) chain C
residue 174
type
sequence M
description BINDING SITE FOR RESIDUE CIR C 3520
source : AC7

92) chain C
residue 182
type
sequence S
description BINDING SITE FOR RESIDUE CIR C 3520
source : AC7

93) chain C
residue 184
type
sequence E
description BINDING SITE FOR RESIDUE CIR C 3520
source : AC7

94) chain C
residue 258
type
sequence E
description BINDING SITE FOR RESIDUE CIR C 3520
source : AC7

95) chain C
residue 270
type
sequence Y
description BINDING SITE FOR RESIDUE CIR C 3520
source : AC7

96) chain C
residue 310
type
sequence Y
description BINDING SITE FOR RESIDUE CIR C 3520
source : AC7

97) chain D
residue 84
type
sequence Y
description BINDING SITE FOR RESIDUE CIR D 4520
source : AC8

98) chain D
residue 88
type
sequence T
description BINDING SITE FOR RESIDUE CIR D 4520
source : AC8

99) chain D
residue 89
type
sequence S
description BINDING SITE FOR RESIDUE CIR D 4520
source : AC8

100) chain D
residue 120
type
sequence N
description BINDING SITE FOR RESIDUE CIR D 4520
source : AC8

101) chain D
residue 124
type
sequence R
description BINDING SITE FOR RESIDUE CIR D 4520
source : AC8

102) chain D
residue 173
type
sequence S
description BINDING SITE FOR RESIDUE CIR D 4520
source : AC8

103) chain D
residue 174
type
sequence M
description BINDING SITE FOR RESIDUE CIR D 4520
source : AC8

104) chain D
residue 175
type
sequence D
description BINDING SITE FOR RESIDUE CIR D 4520
source : AC8

105) chain D
residue 182
type
sequence S
description BINDING SITE FOR RESIDUE CIR D 4520
source : AC8

106) chain D
residue 184
type
sequence E
description BINDING SITE FOR RESIDUE CIR D 4520
source : AC8

107) chain D
residue 258
type
sequence E
description BINDING SITE FOR RESIDUE CIR D 4520
source : AC8

108) chain D
residue 270
type
sequence Y
description BINDING SITE FOR RESIDUE CIR D 4520
source : AC8

109) chain D
residue 310
type
sequence Y
description BINDING SITE FOR RESIDUE CIR D 4520
source : AC8

110) chain A
residue 115
type
sequence A
description BINDING SITE FOR RESIDUE ASP A 530
source : AC9

111) chain A
residue 116
type
sequence T
description BINDING SITE FOR RESIDUE ASP A 530
source : AC9

112) chain A
residue 119
type
sequence G
description BINDING SITE FOR RESIDUE ASP A 530
source : AC9

113) chain A
residue 120
type
sequence N
description BINDING SITE FOR RESIDUE ASP A 530
source : AC9

114) chain A
residue 121
type
sequence D
description BINDING SITE FOR RESIDUE ASP A 530
source : AC9

115) chain B
residue 115
type
sequence A
description BINDING SITE FOR RESIDUE ASP A 2530
source : BC1

116) chain B
residue 116
type
sequence T
description BINDING SITE FOR RESIDUE ASP A 2530
source : BC1

117) chain B
residue 119
type
sequence G
description BINDING SITE FOR RESIDUE ASP A 2530
source : BC1

118) chain B
residue 120
type
sequence N
description BINDING SITE FOR RESIDUE ASP A 2530
source : BC1

119) chain B
residue 121
type
sequence D
description BINDING SITE FOR RESIDUE ASP A 2530
source : BC1

120) chain C
residue 115
type
sequence A
description BINDING SITE FOR RESIDUE ASP A 3530
source : BC2

121) chain C
residue 116
type
sequence T
description BINDING SITE FOR RESIDUE ASP A 3530
source : BC2

122) chain C
residue 119
type
sequence G
description BINDING SITE FOR RESIDUE ASP A 3530
source : BC2

123) chain C
residue 120
type
sequence N
description BINDING SITE FOR RESIDUE ASP A 3530
source : BC2

124) chain C
residue 121
type
sequence D
description BINDING SITE FOR RESIDUE ASP A 3530
source : BC2

125) chain D
residue 115
type
sequence A
description BINDING SITE FOR RESIDUE ASP A 4530
source : BC3

126) chain D
residue 116
type
sequence T
description BINDING SITE FOR RESIDUE ASP A 4530
source : BC3

127) chain D
residue 119
type
sequence G
description BINDING SITE FOR RESIDUE ASP A 4530
source : BC3

128) chain D
residue 120
type
sequence N
description BINDING SITE FOR RESIDUE ASP A 4530
source : BC3

129) chain D
residue 121
type
sequence D
description BINDING SITE FOR RESIDUE ASP A 4530
source : BC3

130) chain D
residue 184
type
sequence E
description BINDING SITE FOR RESIDUE ASP A 4530
source : BC3

131) chain A
residue 12
type catalytic
sequence D
description 316
source MCSA : MCSA1

132) chain A
residue 92
type catalytic
sequence R
description 316
source MCSA : MCSA1

133) chain A
residue 121
type catalytic
sequence D
description 316
source MCSA : MCSA1

134) chain A
residue 173
type catalytic
sequence S
description 316
source MCSA : MCSA1

135) chain B
residue 12
type catalytic
sequence D
description 316
source MCSA : MCSA2

136) chain B
residue 92
type catalytic
sequence R
description 316
source MCSA : MCSA2

137) chain B
residue 121
type catalytic
sequence D
description 316
source MCSA : MCSA2

138) chain B
residue 173
type catalytic
sequence S
description 316
source MCSA : MCSA2

139) chain C
residue 12
type catalytic
sequence D
description 316
source MCSA : MCSA3

140) chain C
residue 92
type catalytic
sequence R
description 316
source MCSA : MCSA3

141) chain C
residue 121
type catalytic
sequence D
description 316
source MCSA : MCSA3

142) chain C
residue 173
type catalytic
sequence S
description 316
source MCSA : MCSA3

143) chain D
residue 12
type catalytic
sequence D
description 316
source MCSA : MCSA4

144) chain D
residue 92
type catalytic
sequence R
description 316
source MCSA : MCSA4

145) chain D
residue 121
type catalytic
sequence D
description 316
source MCSA : MCSA4

146) chain D
residue 173
type catalytic
sequence S
description 316
source MCSA : MCSA4

147) chain A
residue 6
type BINDING
sequence A
description BINDING => ECO:0000255|HAMAP-Rule:MF_00005, ECO:0000269|PubMed:11844799, ECO:0000269|PubMed:12684518
source Swiss-Prot : SWS_FT_FI1

148) chain D
residue 6
type BINDING
sequence A
description BINDING => ECO:0000255|HAMAP-Rule:MF_00005, ECO:0000269|PubMed:11844799, ECO:0000269|PubMed:12684518
source Swiss-Prot : SWS_FT_FI1

149) chain D
residue 33
type BINDING
sequence A
description BINDING => ECO:0000255|HAMAP-Rule:MF_00005, ECO:0000269|PubMed:11844799, ECO:0000269|PubMed:12684518
source Swiss-Prot : SWS_FT_FI1

150) chain D
residue 114
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_00005, ECO:0000269|PubMed:11844799, ECO:0000269|PubMed:12684518
source Swiss-Prot : SWS_FT_FI1

151) chain A
residue 33
type BINDING
sequence A
description BINDING => ECO:0000255|HAMAP-Rule:MF_00005, ECO:0000269|PubMed:11844799, ECO:0000269|PubMed:12684518
source Swiss-Prot : SWS_FT_FI1

152) chain A
residue 114
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_00005, ECO:0000269|PubMed:11844799, ECO:0000269|PubMed:12684518
source Swiss-Prot : SWS_FT_FI1

153) chain B
residue 6
type BINDING
sequence A
description BINDING => ECO:0000255|HAMAP-Rule:MF_00005, ECO:0000269|PubMed:11844799, ECO:0000269|PubMed:12684518
source Swiss-Prot : SWS_FT_FI1

154) chain B
residue 33
type BINDING
sequence A
description BINDING => ECO:0000255|HAMAP-Rule:MF_00005, ECO:0000269|PubMed:11844799, ECO:0000269|PubMed:12684518
source Swiss-Prot : SWS_FT_FI1

155) chain B
residue 114
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_00005, ECO:0000269|PubMed:11844799, ECO:0000269|PubMed:12684518
source Swiss-Prot : SWS_FT_FI1

156) chain C
residue 6
type BINDING
sequence A
description BINDING => ECO:0000255|HAMAP-Rule:MF_00005, ECO:0000269|PubMed:11844799, ECO:0000269|PubMed:12684518
source Swiss-Prot : SWS_FT_FI1

157) chain C
residue 33
type BINDING
sequence A
description BINDING => ECO:0000255|HAMAP-Rule:MF_00005, ECO:0000269|PubMed:11844799, ECO:0000269|PubMed:12684518
source Swiss-Prot : SWS_FT_FI1

158) chain C
residue 114
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_00005, ECO:0000269|PubMed:11844799, ECO:0000269|PubMed:12684518
source Swiss-Prot : SWS_FT_FI1

159) chain A
residue 84
type BINDING
sequence Y
description
source Swiss-Prot : SWS_FT_FI2

160) chain A
residue 270
type BINDING
sequence Y
description
source Swiss-Prot : SWS_FT_FI2

161) chain B
residue 84
type BINDING
sequence Y
description
source Swiss-Prot : SWS_FT_FI2

162) chain B
residue 89
type BINDING
sequence S
description
source Swiss-Prot : SWS_FT_FI2

163) chain B
residue 116
type BINDING
sequence T
description
source Swiss-Prot : SWS_FT_FI2

164) chain B
residue 120
type BINDING
sequence N
description
source Swiss-Prot : SWS_FT_FI2

165) chain B
residue 121
type BINDING
sequence D
description
source Swiss-Prot : SWS_FT_FI2

166) chain B
residue 124
type BINDING
sequence R
description
source Swiss-Prot : SWS_FT_FI2

167) chain B
residue 173
type BINDING
sequence S
description
source Swiss-Prot : SWS_FT_FI2

168) chain B
residue 182
type BINDING
sequence S
description
source Swiss-Prot : SWS_FT_FI2

169) chain B
residue 258
type BINDING
sequence E
description
source Swiss-Prot : SWS_FT_FI2

170) chain A
residue 89
type BINDING
sequence S
description
source Swiss-Prot : SWS_FT_FI2

171) chain B
residue 270
type BINDING
sequence Y
description
source Swiss-Prot : SWS_FT_FI2

172) chain C
residue 84
type BINDING
sequence Y
description
source Swiss-Prot : SWS_FT_FI2

173) chain C
residue 89
type BINDING
sequence S
description
source Swiss-Prot : SWS_FT_FI2

174) chain C
residue 116
type BINDING
sequence T
description
source Swiss-Prot : SWS_FT_FI2

175) chain C
residue 120
type BINDING
sequence N
description
source Swiss-Prot : SWS_FT_FI2

176) chain C
residue 121
type BINDING
sequence D
description
source Swiss-Prot : SWS_FT_FI2

177) chain C
residue 124
type BINDING
sequence R
description
source Swiss-Prot : SWS_FT_FI2

178) chain C
residue 173
type BINDING
sequence S
description
source Swiss-Prot : SWS_FT_FI2

179) chain C
residue 182
type BINDING
sequence S
description
source Swiss-Prot : SWS_FT_FI2

180) chain C
residue 258
type BINDING
sequence E
description
source Swiss-Prot : SWS_FT_FI2

181) chain A
residue 116
type BINDING
sequence T
description
source Swiss-Prot : SWS_FT_FI2

182) chain C
residue 270
type BINDING
sequence Y
description
source Swiss-Prot : SWS_FT_FI2

183) chain D
residue 84
type BINDING
sequence Y
description
source Swiss-Prot : SWS_FT_FI2

184) chain D
residue 89
type BINDING
sequence S
description
source Swiss-Prot : SWS_FT_FI2

185) chain D
residue 116
type BINDING
sequence T
description
source Swiss-Prot : SWS_FT_FI2

186) chain D
residue 120
type BINDING
sequence N
description
source Swiss-Prot : SWS_FT_FI2

187) chain D
residue 121
type BINDING
sequence D
description
source Swiss-Prot : SWS_FT_FI2

188) chain D
residue 124
type BINDING
sequence R
description
source Swiss-Prot : SWS_FT_FI2

189) chain D
residue 173
type BINDING
sequence S
description
source Swiss-Prot : SWS_FT_FI2

190) chain D
residue 182
type BINDING
sequence S
description
source Swiss-Prot : SWS_FT_FI2

191) chain D
residue 258
type BINDING
sequence E
description
source Swiss-Prot : SWS_FT_FI2

192) chain A
residue 120
type BINDING
sequence N
description
source Swiss-Prot : SWS_FT_FI2

193) chain D
residue 270
type BINDING
sequence Y
description
source Swiss-Prot : SWS_FT_FI2

194) chain A
residue 121
type BINDING
sequence D
description
source Swiss-Prot : SWS_FT_FI2

195) chain A
residue 124
type BINDING
sequence R
description
source Swiss-Prot : SWS_FT_FI2

196) chain A
residue 173
type BINDING
sequence S
description
source Swiss-Prot : SWS_FT_FI2

197) chain A
residue 182
type BINDING
sequence S
description
source Swiss-Prot : SWS_FT_FI2

198) chain A
residue 258
type BINDING
sequence E
description
source Swiss-Prot : SWS_FT_FI2

199) chain A
residue 6-14
type prosite
sequence AYSGGLDTS
description ARGININOSUCCIN_SYN_1 Argininosuccinate synthase signature 1. AYSGGLDTS
source prosite : PS00564

200) chain A
residue 114-125
type prosite
sequence GATGKGNDQVRF
description ARGININOSUCCIN_SYN_2 Argininosuccinate synthase signature 2. GaTgKGNDqvRF
source prosite : PS00565


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