eF-site ID 2hve-ABC
PDB Code 2hve
Chain A, B, C

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Title S120G mutant of human nucleoside diphosphate kinase A complexed with ADP
Classification SIGNALING PROTEIN,TRANSFERASE
Compound Nucleoside diphosphate kinase A
Source Homo sapiens (Human) (NDKA_HUMAN)
Sequence A:  ANCERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVGLKFM
QASEDLLKEHYVDLKDRPFFAGLVKYMHSGPVVAMVWEGL
NVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGGD
SVESAEKEIGLWFHPEELVDYTSCAQNWIYE
B:  ANCERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVGLKFM
QASEDLLKEHYVDLKDRPFFAGLVKYMHSGPVVAMVWEGL
NVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGGD
SVESAEKEIGLWFHPEELVDYTSCAQNWIYE
C:  ANCERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVGLKFM
QASEDLLKEHYVDLKDRPFFAGLVKYMHSGPVVAMVWEGL
NVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGGD
SVESAEKEIGLWFHPEELVDYTSCAQNWIYE
Description


Functional site

1) chain A
residue 12
type
sequence K
description BINDING SITE FOR RESIDUE ADP A 160
source : AC1

2) chain A
residue 52
type
sequence Y
description BINDING SITE FOR RESIDUE ADP A 160
source : AC1

3) chain A
residue 55
type
sequence L
description BINDING SITE FOR RESIDUE ADP A 160
source : AC1

4) chain A
residue 60
type
sequence F
description BINDING SITE FOR RESIDUE ADP A 160
source : AC1

5) chain A
residue 64
type
sequence L
description BINDING SITE FOR RESIDUE ADP A 160
source : AC1

6) chain A
residue 88
type
sequence R
description BINDING SITE FOR RESIDUE ADP A 160
source : AC1

7) chain A
residue 94
type
sequence T
description BINDING SITE FOR RESIDUE ADP A 160
source : AC1

8) chain A
residue 112
type
sequence V
description BINDING SITE FOR RESIDUE ADP A 160
source : AC1

9) chain A
residue 115
type
sequence N
description BINDING SITE FOR RESIDUE ADP A 160
source : AC1

10) chain B
residue 12
type
sequence K
description BINDING SITE FOR RESIDUE ADP B 160
source : AC2

11) chain B
residue 55
type
sequence L
description BINDING SITE FOR RESIDUE ADP B 160
source : AC2

12) chain B
residue 60
type
sequence F
description BINDING SITE FOR RESIDUE ADP B 160
source : AC2

13) chain B
residue 64
type
sequence L
description BINDING SITE FOR RESIDUE ADP B 160
source : AC2

14) chain B
residue 88
type
sequence R
description BINDING SITE FOR RESIDUE ADP B 160
source : AC2

15) chain B
residue 94
type
sequence T
description BINDING SITE FOR RESIDUE ADP B 160
source : AC2

16) chain B
residue 112
type
sequence V
description BINDING SITE FOR RESIDUE ADP B 160
source : AC2

17) chain B
residue 115
type
sequence N
description BINDING SITE FOR RESIDUE ADP B 160
source : AC2

18) chain C
residue 12
type
sequence K
description BINDING SITE FOR RESIDUE ADP C 160
source : AC3

19) chain C
residue 55
type
sequence L
description BINDING SITE FOR RESIDUE ADP C 160
source : AC3

20) chain C
residue 60
type
sequence F
description BINDING SITE FOR RESIDUE ADP C 160
source : AC3

21) chain C
residue 88
type
sequence R
description BINDING SITE FOR RESIDUE ADP C 160
source : AC3

22) chain C
residue 94
type
sequence T
description BINDING SITE FOR RESIDUE ADP C 160
source : AC3

23) chain C
residue 112
type
sequence V
description BINDING SITE FOR RESIDUE ADP C 160
source : AC3

24) chain C
residue 115
type
sequence N
description BINDING SITE FOR RESIDUE ADP C 160
source : AC3

25) chain A
residue 118
type ACT_SITE
sequence H
description Pros-phosphohistidine intermediate => ECO:0000269|PubMed:1851158
source Swiss-Prot : SWS_FT_FI1

26) chain B
residue 118
type ACT_SITE
sequence H
description Pros-phosphohistidine intermediate => ECO:0000269|PubMed:1851158
source Swiss-Prot : SWS_FT_FI1

27) chain C
residue 118
type ACT_SITE
sequence H
description Pros-phosphohistidine intermediate => ECO:0000269|PubMed:1851158
source Swiss-Prot : SWS_FT_FI1

28) chain A
residue 12
type BINDING
sequence K
description
source Swiss-Prot : SWS_FT_FI2

29) chain B
residue 94
type BINDING
sequence T
description
source Swiss-Prot : SWS_FT_FI2

30) chain B
residue 105
type BINDING
sequence R
description
source Swiss-Prot : SWS_FT_FI2

31) chain B
residue 115
type BINDING
sequence N
description
source Swiss-Prot : SWS_FT_FI2

32) chain C
residue 12
type BINDING
sequence K
description
source Swiss-Prot : SWS_FT_FI2

33) chain C
residue 60
type BINDING
sequence F
description
source Swiss-Prot : SWS_FT_FI2

34) chain C
residue 88
type BINDING
sequence R
description
source Swiss-Prot : SWS_FT_FI2

35) chain C
residue 94
type BINDING
sequence T
description
source Swiss-Prot : SWS_FT_FI2

36) chain C
residue 105
type BINDING
sequence R
description
source Swiss-Prot : SWS_FT_FI2

37) chain C
residue 115
type BINDING
sequence N
description
source Swiss-Prot : SWS_FT_FI2

38) chain A
residue 60
type BINDING
sequence F
description
source Swiss-Prot : SWS_FT_FI2

39) chain A
residue 88
type BINDING
sequence R
description
source Swiss-Prot : SWS_FT_FI2

40) chain A
residue 94
type BINDING
sequence T
description
source Swiss-Prot : SWS_FT_FI2

41) chain A
residue 105
type BINDING
sequence R
description
source Swiss-Prot : SWS_FT_FI2

42) chain A
residue 115
type BINDING
sequence N
description
source Swiss-Prot : SWS_FT_FI2

43) chain B
residue 12
type BINDING
sequence K
description
source Swiss-Prot : SWS_FT_FI2

44) chain B
residue 60
type BINDING
sequence F
description
source Swiss-Prot : SWS_FT_FI2

45) chain B
residue 88
type BINDING
sequence R
description
source Swiss-Prot : SWS_FT_FI2

46) chain A
residue 120
type MOD_RES
sequence G
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI3

47) chain A
residue 122
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI3

48) chain A
residue 125
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI3

49) chain B
residue 120
type MOD_RES
sequence G
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI3

50) chain B
residue 122
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI3

51) chain B
residue 125
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI3

52) chain C
residue 120
type MOD_RES
sequence G
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI3

53) chain C
residue 122
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI3

54) chain C
residue 125
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI3

55) chain A
residue 100
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
source Swiss-Prot : SWS_FT_FI4

56) chain B
residue 100
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
source Swiss-Prot : SWS_FT_FI4

57) chain C
residue 100
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
source Swiss-Prot : SWS_FT_FI4


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