eF-site ID 5qjl-C
PDB Code 5qjl
Chain C

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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 C:  QYIISEELISEGKWVKLEKTTYMDPTGKTRTWESVKRTTR
KQTADGVAVIPVLQRTLHYECIVLVKQFRPPMGGYCIEFP
AGLIDDGETPEAAALRELEEETGYKGDIAECSPAVCMDPG
LSNCTIHIVTVTINGDDAENARPKPKPGDGEFVEVISLPK
NDLLQRLDALVAEEHLTVDARVYSYALALKHA
Description


Functional site

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

23) 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

24) 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

25) 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

26) 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

27) 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

28) 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

29) 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

30) 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

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

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

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

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

35) 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


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