eF-site ID 5w6x-B
PDB Code 5w6x
Chain B

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Title Crystal structure of the HsNUDT16 in complex with Mg+2 and ADP-ribose
Classification HYDROLASE
Compound U8 snoRNA-decapping enzyme
Source (NUD16_HUMAN)
Sequence B:  ARRLELGEALALGSGWRHVCHALLYAPDPGMLFGRIPLRY
AILMQMRFDGRLGFPGGFVDQDRSLEDGLNRELREELGEA
AAAFRVERTDYRSSHVPRVVAHFYAKRLTLEELLAVEAGA
TRAKDHGLEVLGLVRVPLYTLRDGVGGLPTFLENSFIGSA
REQLLEALQDLGLL
Description


Functional site

1) chain B
residue 36
type
sequence F
description binding site for residue APR A 401
source : AC1

2) chain B
residue 24
type
sequence H
description binding site for residue APR B 401
source : AC5

3) chain B
residue 50
type
sequence R
description binding site for residue APR B 401
source : AC5

4) chain B
residue 51
type
sequence F
description binding site for residue APR B 401
source : AC5

5) chain B
residue 60
type
sequence G
description binding site for residue APR B 401
source : AC5

6) chain B
residue 61
type
sequence F
description binding site for residue APR B 401
source : AC5

7) chain B
residue 76
type
sequence E
description binding site for residue APR B 401
source : AC5

8) chain B
residue 80
type
sequence E
description binding site for residue APR B 401
source : AC5

9) chain B
residue 108
type
sequence A
description binding site for residue APR B 401
source : AC5

10) chain B
residue 136
type
sequence E
description binding site for residue APR B 401
source : AC5

11) chain B
residue 164
type
sequence I
description binding site for residue APR B 401
source : AC5

12) chain B
residue 166
type
sequence S
description binding site for residue APR B 401
source : AC5

13) chain B
residue 170
type
sequence Q
description binding site for residue APR B 401
source : AC5

14) chain B
residue 76
type
sequence E
description binding site for residue MG B 402
source : AC6

15) chain B
residue 80
type
sequence E
description binding site for residue MG B 402
source : AC6

16) chain B
residue 132
type
sequence D
description binding site for residue MG B 402
source : AC6

17) chain B
residue 136
type
sequence E
description binding site for residue MG B 402
source : AC6

18) chain B
residue 59
type
sequence G
description binding site for residue MG B 403
source : AC7

19) chain B
residue 80
type
sequence E
description binding site for residue MG B 403
source : AC7

20) chain B
residue 82
type
sequence G
description binding site for residue ACY B 404
source : AC8

21) chain B
residue 83
type
sequence E
description binding site for residue ACY B 404
source : AC8

22) chain B
residue 84
type
sequence A
description binding site for residue ACY B 404
source : AC8

23) chain B
residue 126
type
sequence G
description binding site for residue ACY B 404
source : AC8

24) chain B
residue 129
type
sequence R
description binding site for residue ACY B 404
source : AC8

25) chain B
residue 30
type
sequence P
description binding site for residue PEG B 405
source : AC9

26) chain B
residue 114
type
sequence R
description binding site for residue PEG B 405
source : AC9

27) chain B
residue 115
type
sequence L
description binding site for residue PEG B 405
source : AC9

28) chain B
residue 116
type
sequence T
description binding site for residue PEG B 405
source : AC9

29) chain B
residue 117
type
sequence L
description binding site for residue PEG B 405
source : AC9

30) chain B
residue 59
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:32432673, ECO:0000305|PubMed:26121039, ECO:0007744|PDB:6X7U
source Swiss-Prot : SWS_FT_FI2

31) chain B
residue 24
type BINDING
sequence H
description BINDING => ECO:0000305|PubMed:26121039
source Swiss-Prot : SWS_FT_FI1

32) chain B
residue 50
type BINDING
sequence R
description BINDING => ECO:0000305|PubMed:26121039
source Swiss-Prot : SWS_FT_FI1

33) chain B
residue 57
type BINDING
sequence F
description BINDING => ECO:0000305|PubMed:26121039
source Swiss-Prot : SWS_FT_FI1

34) chain B
residue 170
type BINDING
sequence Q
description BINDING => ECO:0000305|PubMed:26121039
source Swiss-Prot : SWS_FT_FI1

35) chain B
residue 76
type BINDING
sequence E
description BINDING => ECO:0000250|UniProtKB:Q6TEC1
source Swiss-Prot : SWS_FT_FI3

36) chain B
residue 80
type BINDING
sequence E
description BINDING => ECO:0000250|UniProtKB:Q6TEC1
source Swiss-Prot : SWS_FT_FI3

37) chain B
residue 99
type BINDING
sequence H
description BINDING => ECO:0000269|PubMed:32432673, ECO:0007744|PDB:6X7U, ECO:0007744|PDB:6X7V
source Swiss-Prot : SWS_FT_FI4

38) chain B
residue 173
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:32432673, ECO:0007744|PDB:6X7U, ECO:0007744|PDB:6X7V
source Swiss-Prot : SWS_FT_FI4


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