eF-site ID 5qji-A
PDB Code 5qji
Chain A

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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 Z1899842917
Classification HYDROLASE
Compound ADP-sugar pyrophosphatase
Source (NUDT5_HUMAN)
Sequence A:  KQYIISEELISEGKWVKLEKTTYMDPTGKTRTWESVKRTT
RKEQTADGVAVIPVLQRTLHYECIVLVKQFRPPMGGYCIE
FPAGLIDDGETPEAAALRELEEETGYKGDIAECSPAVCMD
PGLSNCTIHIVTVTINGDDAENARPKPKPGDGEFVEVISL
PKNDLLQRLDALVAEEHLTVDARVYSYALALKHA
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 28
type
sequence W
description binding site for residue K1A B 304
source : AC6

7) chain A
residue 51
type
sequence R
description binding site for residue K1A B 304
source : AC6

8) chain A
residue 98
type
sequence L
description binding site for residue K1A B 304
source : AC6

9) chain A
residue 51
type
sequence R
description binding site for residue EDO B 305
source : AC7

10) chain A
residue 139
type
sequence C
description binding site for residue EDO B 305
source : AC7

11) 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

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

13) 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

14) 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

15) 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

16) 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

17) 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

18) 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

19) 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

20) 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

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

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

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

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


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