eF-site ID 3v80-A
PDB Code 3v80
Chain A

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Title Crystal structure of NAD kinase 1 from Listeria monocytogenes in complex with 5'-O-Propargylamino-5'-deoxyadenosine
Classification TRANSFERASE
Compound Probable inorganic polyphosphate/ATP-NAD kinase 1
Source null (PPNK1_LISMO)
Sequence A:  MKYMITSKGDEKSDLLRLNMIAGFGEYDMEYDDVEPEIVI
SIGGDGTFLSAFHQYEERLDEIAFIGIHTGHLGFYADWRP
AEADKLVKLLAYQKVSYPLLKTTVKYGKEATYLALNESTV
KSSGGPFVVDVVINDIHFERFRGDGLCMSTPSGTTAYNKS
LGGALMHPSIEAMQLTEMASINNRVYRTIGSPLVFPKHHV
VSLQPVNDKDFQISVDHLSILHRDVQEIRYEVSAKKIHFA
RFRSFPFWRRVHDSFIED
Description


Functional site

1) chain A
residue 49
type
sequence L
description BINDING SITE FOR RESIDUE AOC A 301
source : AC1

2) chain A
residue 122
type
sequence N
description BINDING SITE FOR RESIDUE AOC A 301
source : AC1

3) chain A
residue 123
type
sequence E
description BINDING SITE FOR RESIDUE AOC A 301
source : AC1

4) chain A
residue 149
type
sequence G
description BINDING SITE FOR RESIDUE AOC A 301
source : AC1

5) chain A
residue 150
type
sequence D
description BINDING SITE FOR RESIDUE AOC A 301
source : AC1

6) chain A
residue 162
type
sequence A
description BINDING SITE FOR RESIDUE AOC A 301
source : AC1

7) chain A
residue 163
type
sequence Y
description BINDING SITE FOR RESIDUE AOC A 301
source : AC1

8) chain A
residue 166
type
sequence S
description BINDING SITE FOR RESIDUE AOC A 301
source : AC1

9) chain A
residue 185
type
sequence A
description BINDING SITE FOR RESIDUE AOC A 301
source : AC1

10) chain A
residue 187
type
sequence I
description BINDING SITE FOR RESIDUE AOC A 301
source : AC1

11) chain A
residue 223
type
sequence H
description BINDING SITE FOR RESIDUE AOC A 301
source : AC1

12) chain A
residue 45
type
sequence D
description BINDING SITE FOR RESIDUE AOC A 302
source : AC2

13) chain A
residue 72
type
sequence L
description BINDING SITE FOR RESIDUE AOC A 302
source : AC2

14) chain A
residue 74
type
sequence F
description BINDING SITE FOR RESIDUE AOC A 302
source : AC2

15) chain A
residue 75
type
sequence Y
description BINDING SITE FOR RESIDUE AOC A 302
source : AC2

16) chain A
residue 122
type
sequence N
description BINDING SITE FOR RESIDUE AOC A 302
source : AC2

17) chain A
residue 158
type
sequence S
description BINDING SITE FOR RESIDUE AOC A 302
source : AC2

18) chain A
residue 161
type
sequence T
description BINDING SITE FOR RESIDUE AOC A 302
source : AC2

19) chain A
residue 162
type
sequence A
description BINDING SITE FOR RESIDUE AOC A 302
source : AC2

20) chain A
residue 187
type
sequence I
description BINDING SITE FOR RESIDUE AOC A 302
source : AC2

21) chain A
residue 192
type
sequence Y
description BINDING SITE FOR RESIDUE AOC A 302
source : AC2

22) chain A
residue 98
type
sequence V
description BINDING SITE FOR RESIDUE CIT A 303
source : AC3

23) chain A
residue 100
type
sequence Y
description BINDING SITE FOR RESIDUE CIT A 303
source : AC3

24) chain A
residue 173
type
sequence H
description BINDING SITE FOR RESIDUE CIT A 303
source : AC3

25) chain A
residue 247
type
sequence R
description BINDING SITE FOR RESIDUE CIT A 303
source : AC3

26) chain A
residue 251
type
sequence F
description BINDING SITE FOR RESIDUE CIT A 303
source : AC3

27) chain A
residue 252
type
sequence P
description BINDING SITE FOR RESIDUE CIT A 303
source : AC3

28) chain A
residue 253
type
sequence F
description BINDING SITE FOR RESIDUE CIT A 303
source : AC3

29) chain A
residue 256
type
sequence R
description BINDING SITE FOR RESIDUE CIT A 303
source : AC3

30) chain A
residue 8
type
sequence K
description BINDING SITE FOR RESIDUE GOL A 304
source : AC4

31) chain A
residue 44
type
sequence G
description BINDING SITE FOR RESIDUE GOL A 304
source : AC4

32) chain A
residue 46
type
sequence G
description BINDING SITE FOR RESIDUE GOL A 304
source : AC4

33) chain A
residue 47
type
sequence T
description BINDING SITE FOR RESIDUE GOL A 304
source : AC4

34) chain A
residue 71
type
sequence H
description BINDING SITE FOR RESIDUE GOL A 304
source : AC4

35) chain A
residue 45
type ACT_SITE
sequence D
description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780
source Swiss-Prot : SWS_FT_FI1

36) chain A
residue 46
type BINDING
sequence G
description BINDING => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780
source Swiss-Prot : SWS_FT_FI2

37) chain A
residue 122
type BINDING
sequence N
description BINDING => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780
source Swiss-Prot : SWS_FT_FI2

38) chain A
residue 158
type BINDING
sequence S
description BINDING => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780
source Swiss-Prot : SWS_FT_FI2

39) chain A
residue 161
type BINDING
sequence T
description BINDING => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780
source Swiss-Prot : SWS_FT_FI2

40) chain A
residue 223
type BINDING
sequence H
description BINDING => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780
source Swiss-Prot : SWS_FT_FI2

41) chain A
residue 45
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:17686780
source Swiss-Prot : SWS_FT_FI2

42) chain A
residue 148
type BINDING
sequence R
description BINDING => ECO:0000255|HAMAP-Rule:MF_00361
source Swiss-Prot : SWS_FT_FI3

43) chain A
residue 150
type BINDING
sequence D
description BINDING => ECO:0000305|PubMed:17686780
source Swiss-Prot : SWS_FT_FI4


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