eF-site ID 5qjl-ABCD
PDB Code 5qjl
Chain A, B, C, D

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Title PanDDA analysis group deposition of models with modelled events (e.g. bound ligands) -- Crystal Structure of NUDT5 in complex with Z56983806
Classification HYDROLASE
Compound ADP-sugar pyrophosphatase
Source (NUDT5_HUMAN)
Sequence A:  KQYIISEELISEGKWVKLEKTTYMDPTGKTRTWESVKRTT
RKEQTADGVAVIPVLQRTLHYECIVLVKQFRPPMGGYCIE
FPAGLIDDGETPEAAALRELEEETGYKGDIAECSPAVCMD
PGLSNCTIHIVTVTINGDDAENARPKPKPGDGEFVEVISL
PKNDLLQRLDALVAEEHLTVDARVYSYALALKHA
B:  KQYIISEELISEGKWVKLEKTTYMDPTGKTRTWESVKRTT
RKQTADGVAVIPVLQRTLHYECIVLVKQFRPPMGGYCIEF
PAGLIDDGETPEAAALRELEEETGYKGDIAECSPAVCMDP
GLSNCTIHIVTVTINGDDAENARPKPKPGDGEFVEVISLP
KNDLLQRLDALVAEEHLTVDARVYSYALALKHAN
C:  QYIISEELISEGKWVKLEKTTYMDPTGKTRTWESVKRTTR
KQTADGVAVIPVLQRTLHYECIVLVKQFRPPMGGYCIEFP
AGLIDDGETPEAAALRELEEETGYKGDIAECSPAVCMDPG
LSNCTIHIVTVTINGDDAENARPKPKPGDGEFVEVISLPK
NDLLQRLDALVAEEHLTVDARVYSYALALKHA
D:  KQYIISEELISEGKWVKLEKTTYMDPTGKTRTWESVKRTT
ADGVAVIPVLQRTLHYECIVLVKQFRPPMGGYCIEFPAGL
IDDGETPEAAALRELEEETGYKGDIAECSPAVCMDPGLSN
CTIHIVTVTINGDDAENARPKPKPGDGEFVEVISLPKNDL
LQRLDALVAEEHLTVDARVYSYALALKHAN
Description


Functional site

1) chain A
residue 96
type
sequence A
description binding site for residue MG A 301
source : AC1

2) chain A
residue 116
type
sequence E
description binding site for residue MG A 301
source : AC1

3) chain A
residue 112
type
sequence E
description binding site for residue MG A 302
source : AC2

4) chain A
residue 116
type
sequence E
description binding site for residue MG A 302
source : AC2

5) chain A
residue 166
type
sequence E
description binding site for residue MG A 302
source : AC2

6) chain A
residue 51
type
sequence R
description binding site for residue EDO A 304
source : AC3

7) chain A
residue 132
type
sequence M
description binding site for residue EDO A 304
source : AC3

8) chain A
residue 139
type
sequence C
description binding site for residue EDO A 304
source : AC3

9) chain B
residue 133
type
sequence D
description binding site for residue EDO A 304
source : AC3

10) chain A
residue 176
type
sequence N
description binding site for residue EDO A 305
source : AC4

11) chain A
residue 177
type
sequence D
description binding site for residue EDO A 305
source : AC4

12) chain A
residue 179
type
sequence L
description binding site for residue EDO A 305
source : AC4

13) chain A
residue 180
type
sequence Q
description binding site for residue EDO A 305
source : AC4

14) chain A
residue 205
type
sequence K
description binding site for residue EDO A 305
source : AC4

15) chain B
residue 69
type
sequence Q
description binding site for residue EDO B 301
source : AC5

16) chain B
residue 149
type
sequence N
description binding site for residue EDO B 301
source : AC5

17) chain B
residue 151
type
sequence D
description binding site for residue EDO B 301
source : AC5

18) chain B
residue 96
type
sequence A
description binding site for residue MG B 302
source : AC6

19) chain B
residue 116
type
sequence E
description binding site for residue MG B 302
source : AC6

20) chain B
residue 112
type
sequence E
description binding site for residue MG B 303
source : AC7

21) chain B
residue 115
type
sequence E
description binding site for residue MG B 303
source : AC7

22) chain B
residue 116
type
sequence E
description binding site for residue MG B 303
source : AC7

23) chain B
residue 166
type
sequence E
description binding site for residue MG B 303
source : AC7

24) chain A
residue 28
type
sequence W
description binding site for residue JJM B 304
source : AC8

25) chain A
residue 29
type
sequence V
description binding site for residue JJM B 304
source : AC8

26) chain A
residue 51
type
sequence R
description binding site for residue JJM B 304
source : AC8

27) chain A
residue 164
type
sequence D
description binding site for residue JJM B 304
source : AC8

28) chain A
residue 166
type
sequence E
description binding site for residue JJM B 304
source : AC8

29) chain B
residue 46
type
sequence W
description binding site for residue JJM B 304
source : AC8

30) chain B
residue 47
type
sequence E
description binding site for residue JJM B 304
source : AC8

31) chain B
residue 135
type
sequence G
description binding site for residue JJM B 304
source : AC8

32) chain A
residue 46
type
sequence W
description binding site for residue JJM B 305
source : AC9

33) chain A
residue 47
type
sequence E
description binding site for residue JJM B 305
source : AC9

34) chain A
residue 135
type
sequence G
description binding site for residue JJM B 305
source : AC9

35) chain B
residue 28
type
sequence W
description binding site for residue JJM B 305
source : AC9

36) chain B
residue 29
type
sequence V
description binding site for residue JJM B 305
source : AC9

37) chain B
residue 51
type
sequence R
description binding site for residue JJM B 305
source : AC9

38) chain B
residue 164
type
sequence D
description binding site for residue JJM B 305
source : AC9

39) chain B
residue 166
type
sequence E
description binding site for residue JJM B 305
source : AC9

40) chain A
residue 133
type
sequence D
description binding site for residue EDO B 306
source : AD1

41) chain B
residue 51
type
sequence R
description binding site for residue EDO B 306
source : AD1

42) chain B
residue 132
type
sequence M
description binding site for residue EDO B 306
source : AD1

43) chain B
residue 139
type
sequence C
description binding site for residue EDO B 306
source : AD1

44) chain C
residue 122
type
sequence D
description binding site for residue EDO C 301
source : AD2

45) chain C
residue 152
type
sequence D
description binding site for residue EDO C 301
source : AD2

46) chain C
residue 154
type
sequence E
description binding site for residue EDO C 301
source : AD2

47) chain C
residue 155
type
sequence N
description binding site for residue EDO C 301
source : AD2

48) chain C
residue 96
type
sequence A
description binding site for residue MG C 302
source : AD3

49) chain C
residue 97
type
sequence G
description binding site for residue MG C 302
source : AD3

50) chain C
residue 112
type
sequence E
description binding site for residue MG C 302
source : AD3

51) chain C
residue 116
type
sequence E
description binding site for residue MG C 302
source : AD3

52) chain C
residue 166
type
sequence E
description binding site for residue MG C 302
source : AD3

53) chain C
residue 96
type
sequence A
description binding site for residue MG C 303
source : AD4

54) chain C
residue 116
type
sequence E
description binding site for residue MG C 303
source : AD4

55) chain C
residue 166
type
sequence E
description binding site for residue MG C 303
source : AD4

56) chain C
residue 46
type
sequence W
description binding site for residue JJM C 304
source : AD5

57) chain C
residue 47
type
sequence E
description binding site for residue JJM C 304
source : AD5

58) chain C
residue 135
type
sequence G
description binding site for residue JJM C 304
source : AD5

59) chain D
residue 28
type
sequence W
description binding site for residue JJM C 304
source : AD5

60) chain D
residue 29
type
sequence V
description binding site for residue JJM C 304
source : AD5

61) chain D
residue 51
type
sequence R
description binding site for residue JJM C 304
source : AD5

62) chain C
residue 133
type
sequence D
description binding site for residue EDO C 305
source : AD6

63) chain D
residue 51
type
sequence R
description binding site for residue EDO C 305
source : AD6

64) chain D
residue 132
type
sequence M
description binding site for residue EDO C 305
source : AD6

65) chain D
residue 139
type
sequence C
description binding site for residue EDO C 305
source : AD6

66) chain D
residue 96
type
sequence A
description binding site for residue MG D 301
source : AD7

67) chain D
residue 116
type
sequence E
description binding site for residue MG D 301
source : AD7

68) chain D
residue 96
type
sequence A
description binding site for residue MG D 302
source : AD8

69) chain D
residue 97
type
sequence G
description binding site for residue MG D 302
source : AD8

70) chain D
residue 112
type
sequence E
description binding site for residue MG D 302
source : AD8

71) chain D
residue 116
type
sequence E
description binding site for residue MG D 302
source : AD8

72) chain D
residue 166
type
sequence E
description binding site for residue MG D 302
source : AD8

73) chain C
residue 28
type
sequence W
description binding site for residue JJM D 303
source : AD9

74) chain C
residue 51
type
sequence R
description binding site for residue JJM D 303
source : AD9

75) chain C
residue 164
type
sequence D
description binding site for residue JJM D 303
source : AD9

76) chain D
residue 46
type
sequence W
description binding site for residue JJM D 303
source : AD9

77) chain D
residue 47
type
sequence E
description binding site for residue JJM D 303
source : AD9

78) chain C
residue 51
type
sequence R
description binding site for residue EDO D 304
source : AE1

79) chain C
residue 132
type
sequence M
description binding site for residue EDO D 304
source : AE1

80) chain C
residue 139
type
sequence C
description binding site for residue EDO D 304
source : AE1

81) chain D
residue 133
type
sequence D
description binding site for residue EDO D 304
source : AE1

82) chain A
residue 28
type BINDING
sequence W
description in other chain => ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126
source Swiss-Prot : SWS_FT_FI1

83) chain A
residue 84
type BINDING
sequence R
description in other chain => ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126
source Swiss-Prot : SWS_FT_FI1

84) chain B
residue 28
type BINDING
sequence W
description in other chain => ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126
source Swiss-Prot : SWS_FT_FI1

85) chain B
residue 84
type BINDING
sequence R
description in other chain => ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126
source Swiss-Prot : SWS_FT_FI1

86) chain C
residue 28
type BINDING
sequence W
description in other chain => ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126
source Swiss-Prot : SWS_FT_FI1

87) chain C
residue 84
type BINDING
sequence R
description in other chain => ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126
source Swiss-Prot : SWS_FT_FI1

88) chain D
residue 28
type BINDING
sequence W
description in other chain => ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126
source Swiss-Prot : SWS_FT_FI1

89) chain D
residue 84
type BINDING
sequence R
description in other chain => ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126
source Swiss-Prot : SWS_FT_FI1

90) chain A
residue 46
type BINDING
sequence W
description BINDING => ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126
source Swiss-Prot : SWS_FT_FI2

91) chain B
residue 112
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126
source Swiss-Prot : SWS_FT_FI2

92) chain B
residue 116
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126
source Swiss-Prot : SWS_FT_FI2

93) chain B
residue 166
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126
source Swiss-Prot : SWS_FT_FI2

94) chain C
residue 46
type BINDING
sequence W
description BINDING => ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126
source Swiss-Prot : SWS_FT_FI2

95) chain C
residue 51
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126
source Swiss-Prot : SWS_FT_FI2

96) chain C
residue 96
type BINDING
sequence A
description BINDING => ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126
source Swiss-Prot : SWS_FT_FI2

97) chain C
residue 112
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126
source Swiss-Prot : SWS_FT_FI2

98) chain C
residue 116
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126
source Swiss-Prot : SWS_FT_FI2

99) chain C
residue 166
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126
source Swiss-Prot : SWS_FT_FI2

100) chain D
residue 46
type BINDING
sequence W
description BINDING => ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126
source Swiss-Prot : SWS_FT_FI2

101) chain A
residue 51
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126
source Swiss-Prot : SWS_FT_FI2

102) chain D
residue 51
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126
source Swiss-Prot : SWS_FT_FI2

103) chain D
residue 96
type BINDING
sequence A
description BINDING => ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126
source Swiss-Prot : SWS_FT_FI2

104) chain D
residue 112
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126
source Swiss-Prot : SWS_FT_FI2

105) chain D
residue 116
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126
source Swiss-Prot : SWS_FT_FI2

106) chain D
residue 166
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126
source Swiss-Prot : SWS_FT_FI2

107) chain A
residue 96
type BINDING
sequence A
description BINDING => ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126
source Swiss-Prot : SWS_FT_FI2

108) chain A
residue 112
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126
source Swiss-Prot : SWS_FT_FI2

109) chain A
residue 116
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126
source Swiss-Prot : SWS_FT_FI2

110) chain A
residue 166
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126
source Swiss-Prot : SWS_FT_FI2

111) chain B
residue 46
type BINDING
sequence W
description BINDING => ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126
source Swiss-Prot : SWS_FT_FI2

112) chain B
residue 51
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126
source Swiss-Prot : SWS_FT_FI2

113) chain B
residue 96
type BINDING
sequence A
description BINDING => ECO:0000269|PubMed:17052728, ECO:0000269|PubMed:18462755, ECO:0000269|PubMed:21768126
source Swiss-Prot : SWS_FT_FI2

114) chain A
residue 45
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000269|PubMed:27257257
source Swiss-Prot : SWS_FT_FI7

115) chain B
residue 45
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000269|PubMed:27257257
source Swiss-Prot : SWS_FT_FI7

116) chain C
residue 45
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000269|PubMed:27257257
source Swiss-Prot : SWS_FT_FI7

117) chain D
residue 45
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000269|PubMed:27257257
source Swiss-Prot : SWS_FT_FI7

118) chain A
residue 74
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:15592455
source Swiss-Prot : SWS_FT_FI8

119) chain B
residue 74
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:15592455
source Swiss-Prot : SWS_FT_FI8

120) chain C
residue 74
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:15592455
source Swiss-Prot : SWS_FT_FI8

121) chain D
residue 74
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:15592455
source Swiss-Prot : SWS_FT_FI8

122) chain A
residue 42
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
source Swiss-Prot : SWS_FT_FI9

123) chain B
residue 42
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
source Swiss-Prot : SWS_FT_FI9

124) chain C
residue 42
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
source Swiss-Prot : SWS_FT_FI9

125) chain D
residue 42
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
source Swiss-Prot : SWS_FT_FI9

126) chain A
residue 97-118
type prosite
sequence GLIDDGETPEAAALRELEEETG
description NUDIX_BOX Nudix box signature. GliddgEtpeaAAlRELeEEtG
source prosite : PS00893

127) chain A
residue 98
type BINDING
sequence L
description in other chain => ECO:0000269|PubMed:17052728
source Swiss-Prot : SWS_FT_FI3

128) chain A
residue 133
type BINDING
sequence D
description in other chain => ECO:0000269|PubMed:17052728
source Swiss-Prot : SWS_FT_FI3

129) chain B
residue 98
type BINDING
sequence L
description in other chain => ECO:0000269|PubMed:17052728
source Swiss-Prot : SWS_FT_FI3

130) chain B
residue 133
type BINDING
sequence D
description in other chain => ECO:0000269|PubMed:17052728
source Swiss-Prot : SWS_FT_FI3

131) chain C
residue 98
type BINDING
sequence L
description in other chain => ECO:0000269|PubMed:17052728
source Swiss-Prot : SWS_FT_FI3

132) chain C
residue 133
type BINDING
sequence D
description in other chain => ECO:0000269|PubMed:17052728
source Swiss-Prot : SWS_FT_FI3

133) chain D
residue 98
type BINDING
sequence L
description in other chain => ECO:0000269|PubMed:17052728
source Swiss-Prot : SWS_FT_FI3

134) chain D
residue 133
type BINDING
sequence D
description in other chain => ECO:0000269|PubMed:17052728
source Swiss-Prot : SWS_FT_FI3


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