eF-site ID 5qj8-ABCD
PDB Code 5qj8
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 Z2856434829
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 B
residue 69
type
sequence Q
description binding site for residue EDO B 302
source : AC3
7) chain B
residue 149
type
sequence N
description binding site for residue EDO B 302
source : AC3
8) chain B
residue 151
type
sequence D
description binding site for residue EDO B 302
source : AC3
9) chain B
residue 96
type
sequence A
description binding site for residue MG B 303
source : AC4
10) chain B
residue 116
type
sequence E
description binding site for residue MG B 303
source : AC4
11) chain B
residue 112
type
sequence E
description binding site for residue MG B 304
source : AC5
12) chain B
residue 115
type
sequence E
description binding site for residue MG B 304
source : AC5
13) chain B
residue 116
type
sequence E
description binding site for residue MG B 304
source : AC5
14) chain B
residue 166
type
sequence E
description binding site for residue MG B 304
source : AC5
15) chain A
residue 28
type
sequence W
description binding site for residue ELQ B 305
source : AC6
16) chain A
residue 51
type
sequence R
description binding site for residue ELQ B 305
source : AC6
17) chain B
residue 45
type
sequence T
description binding site for residue ELQ B 305
source : AC6
18) chain B
residue 46
type
sequence W
description binding site for residue ELQ B 305
source : AC6
19) chain B
residue 47
type
sequence E
description binding site for residue ELQ B 305
source : AC6
20) chain B
residue 135
type
sequence G
description binding site for residue ELQ B 305
source : AC6
21) chain C
residue 122
type
sequence D
description binding site for residue EDO C 301
source : AC7
22) chain C
residue 152
type
sequence D
description binding site for residue EDO C 301
source : AC7
23) chain C
residue 154
type
sequence E
description binding site for residue EDO C 301
source : AC7
24) chain C
residue 155
type
sequence N
description binding site for residue EDO C 301
source : AC7
25) chain C
residue 112
type
sequence E
description binding site for residue MG C 302
source : AC8
26) chain C
residue 116
type
sequence E
description binding site for residue MG C 302
source : AC8
27) chain C
residue 166
type
sequence E
description binding site for residue MG C 302
source : AC8
28) chain C
residue 96
type
sequence A
description binding site for residue MG C 303
source : AC9
29) chain C
residue 116
type
sequence E
description binding site for residue MG C 303
source : AC9
30) chain C
residue 166
type
sequence E
description binding site for residue MG C 303
source : AC9
31) chain D
residue 82
type
sequence Q
description binding site for residue MG D 301
source : AD1
32) chain D
residue 96
type
sequence A
description binding site for residue MG D 301
source : AD1
33) chain D
residue 116
type
sequence E
description binding site for residue MG D 301
source : AD1
34) chain D
residue 96
type
sequence A
description binding site for residue MG D 302
source : AD2
35) chain D
residue 97
type
sequence G
description binding site for residue MG D 302
source : AD2
36) chain D
residue 112
type
sequence E
description binding site for residue MG D 302
source : AD2
37) chain D
residue 116
type
sequence E
description binding site for residue MG D 302
source : AD2
38) chain D
residue 166
type
sequence E
description binding site for residue MG D 302
source : AD2
39) chain A
residue 97-118
type prosite
sequence GLIDDGETPEAAALRELEEETG
description NUDIX_BOX Nudix box signature. GliddgEtpeaAAlRELeEEtG
source prosite : PS00893
40) 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
41) 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
42) 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
43) 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
44) 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
45) 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
46) 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
47) 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
48) 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
49) 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
50) 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
51) 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
52) 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
53) 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
54) 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
55) 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
56) 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
57) 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
58) 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
59) 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
60) 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
61) 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
62) 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
63) 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
64) 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
65) 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
66) 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
67) 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
68) 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
69) 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
70) 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
71) 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
72) chain A
residue 133
type BINDING
sequence D
description in other chain => ECO:0000269|PubMed:17052728
source Swiss-Prot : SWS_FT_FI3
73) chain A
residue 98
type BINDING
sequence L
description in other chain => ECO:0000269|PubMed:17052728
source Swiss-Prot : SWS_FT_FI3
74) chain B
residue 98
type BINDING
sequence L
description in other chain => ECO:0000269|PubMed:17052728
source Swiss-Prot : SWS_FT_FI3
75) chain B
residue 133
type BINDING
sequence D
description in other chain => ECO:0000269|PubMed:17052728
source Swiss-Prot : SWS_FT_FI3
76) chain C
residue 98
type BINDING
sequence L
description in other chain => ECO:0000269|PubMed:17052728
source Swiss-Prot : SWS_FT_FI3
77) chain C
residue 133
type BINDING
sequence D
description in other chain => ECO:0000269|PubMed:17052728
source Swiss-Prot : SWS_FT_FI3
78) chain D
residue 98
type BINDING
sequence L
description in other chain => ECO:0000269|PubMed:17052728
source Swiss-Prot : SWS_FT_FI3
79) chain D
residue 133
type BINDING
sequence D
description in other chain => ECO:0000269|PubMed:17052728
source Swiss-Prot : SWS_FT_FI3
80) chain A
residue 45
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000269|PubMed:27257257
source Swiss-Prot : SWS_FT_FI7
81) chain B
residue 45
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000269|PubMed:27257257
source Swiss-Prot : SWS_FT_FI7
82) chain C
residue 45
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000269|PubMed:27257257
source Swiss-Prot : SWS_FT_FI7
83) chain D
residue 45
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000269|PubMed:27257257
source Swiss-Prot : SWS_FT_FI7
84) chain A
residue 74
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:15592455
source Swiss-Prot : SWS_FT_FI8
85) chain B
residue 74
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:15592455
source Swiss-Prot : SWS_FT_FI8
86) chain C
residue 74
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:15592455
source Swiss-Prot : SWS_FT_FI8
87) chain D
residue 74
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:15592455
source Swiss-Prot : SWS_FT_FI8
88) 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
89) 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
90) 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
91) 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

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