eF-site ID 5qjj-ABCD
PDB Code 5qjj
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 Z24758179
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 96
type
sequence A
description binding site for residue MG A 302
source : AC2

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

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

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

7) chain A
residue 51
type
sequence R
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 B
residue 69
type
sequence Q
description binding site for residue EDO B 301
source : AC4

11) chain B
residue 149
type
sequence N
description binding site for residue EDO B 301
source : AC4

12) chain B
residue 151
type
sequence D
description binding site for residue EDO B 301
source : AC4

13) chain B
residue 96
type
sequence A
description binding site for residue MG B 302
source : AC5

14) chain B
residue 116
type
sequence E
description binding site for residue MG B 302
source : AC5

15) chain B
residue 112
type
sequence E
description binding site for residue MG B 303
source : AC6

16) chain B
residue 115
type
sequence E
description binding site for residue MG B 303
source : AC6

17) chain B
residue 116
type
sequence E
description binding site for residue MG B 303
source : AC6

18) chain B
residue 166
type
sequence E
description binding site for residue MG B 303
source : AC6

19) chain A
residue 133
type
sequence D
description binding site for residue EDO B 304
source : AC7

20) chain B
residue 51
type
sequence R
description binding site for residue EDO B 304
source : AC7

21) chain B
residue 132
type
sequence M
description binding site for residue EDO B 304
source : AC7

22) chain B
residue 139
type
sequence C
description binding site for residue EDO B 304
source : AC7

23) chain C
residue 122
type
sequence D
description binding site for residue EDO C 301
source : AC8

24) chain C
residue 152
type
sequence D
description binding site for residue EDO C 301
source : AC8

25) chain C
residue 154
type
sequence E
description binding site for residue EDO C 301
source : AC8

26) chain C
residue 155
type
sequence N
description binding site for residue EDO C 301
source : AC8

27) chain C
residue 96
type
sequence A
description binding site for residue MG C 302
source : AC9

28) chain C
residue 97
type
sequence G
description binding site for residue MG C 302
source : AC9

29) chain C
residue 112
type
sequence E
description binding site for residue MG C 302
source : AC9

30) chain C
residue 116
type
sequence E
description binding site for residue MG C 302
source : AC9

31) chain C
residue 166
type
sequence E
description binding site for residue MG C 302
source : AC9

32) chain C
residue 96
type
sequence A
description binding site for residue MG C 303
source : AD1

33) chain C
residue 116
type
sequence E
description binding site for residue MG C 303
source : AD1

34) chain C
residue 166
type
sequence E
description binding site for residue MG C 303
source : AD1

35) chain C
residue 46
type
sequence W
description binding site for residue 6SU C 304
source : AD2

36) chain C
residue 47
type
sequence E
description binding site for residue 6SU C 304
source : AD2

37) chain C
residue 135
type
sequence G
description binding site for residue 6SU C 304
source : AD2

38) chain D
residue 28
type
sequence W
description binding site for residue 6SU C 304
source : AD2

39) chain D
residue 164
type
sequence D
description binding site for residue 6SU C 304
source : AD2

40) chain C
residue 51
type
sequence R
description binding site for residue EDO C 305
source : AD3

41) chain C
residue 139
type
sequence C
description binding site for residue EDO C 305
source : AD3

42) chain D
residue 133
type
sequence D
description binding site for residue EDO C 305
source : AD3

43) chain D
residue 96
type
sequence A
description binding site for residue MG D 301
source : AD4

44) chain D
residue 116
type
sequence E
description binding site for residue MG D 301
source : AD4

45) chain D
residue 96
type
sequence A
description binding site for residue MG D 302
source : AD5

46) chain D
residue 97
type
sequence G
description binding site for residue MG D 302
source : AD5

47) chain D
residue 112
type
sequence E
description binding site for residue MG D 302
source : AD5

48) chain D
residue 116
type
sequence E
description binding site for residue MG D 302
source : AD5

49) chain D
residue 166
type
sequence E
description binding site for residue MG D 302
source : AD5

50) chain C
residue 28
type
sequence W
description binding site for residue 6SU D 303
source : AD6

51) chain D
residue 36
type
sequence Y
description binding site for residue 6SU D 303
source : AD6

52) chain D
residue 44
type
sequence R
description binding site for residue 6SU D 303
source : AD6

53) chain D
residue 46
type
sequence W
description binding site for residue 6SU D 303
source : AD6

54) chain D
residue 47
type
sequence E
description binding site for residue 6SU D 303
source : AD6

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

56) 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

57) 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

58) 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

59) 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

60) 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

61) 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

62) 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

63) 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

64) 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

65) 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

66) 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

67) 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

68) 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

69) 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

70) 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

71) 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

72) 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

73) 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

74) 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

75) 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

76) 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

77) 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

78) 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

79) 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

80) 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

81) 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

82) 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

83) 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

84) 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

85) 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

86) 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

87) 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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

104) 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

105) 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

106) 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

107) 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


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