eF-site ID 2kdc_9-ABC
PDB Code 2kdc
Model 9
Chain A, B, C

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Title NMR Solution Structure of E. coli diacylglycerol kinase (DAGK) in DPC micelles
Classification TRANSFERASE
Compound Diacylglycerol kinase
Source Escherichia coli (strain K12) (KDGL_ECOLI)
Sequence A:  ANNTTGFTRIIKAAGYSWKGLRAAWINEAAFRQEGVAVLL
AVVIACWLDVDAITRVLLISSVMLVMIVEILNSAIEAVVD
RIGSEYHELSGRAKDMGSAAVLIAIIVAVITWCILLWSHF
G
B:  ANNTTGFTRIIKAAGYSWKGLRAAWINEAAFRQEGVAVLL
AVVIACWLDVDAITRVLLISSVMLVMIVEILNSAIEAVVD
RIGSEYHELSGRAKDMGSAAVLIAIIVAVITWCILLWSHF
G
C:  ANNTTGFTRIIKAAGYSWKGLRAAWINEAAFRQEGVAVLL
AVVIACWLDVDAITRVLLISSVMLVMIVEILNSAIEAVVD
RIGSEYHELSGRAKDMGSAAVLIAIIVAVITWCILLWSHF
G
Description


Functional site

1) chain A
residue 69-80
type prosite
sequence EILNSAIEAVVD
description DAGK_PROKAR Prokaryotic diacylglycerol kinase signature. EiLNSAIEavVD
source prosite : PS01069

2) chain A
residue 1-30
type TOPO_DOM
sequence ANNTTGFTRIIKAAGYSWKGLRAAWINEAA
description Cytoplasmic => ECO:0000269|PubMed:8071224
source Swiss-Prot : SWS_FT_FI1

3) chain B
residue 1-30
type TOPO_DOM
sequence ANNTTGFTRIIKAAGYSWKGLRAAWINEAA
description Cytoplasmic => ECO:0000269|PubMed:8071224
source Swiss-Prot : SWS_FT_FI1

4) chain C
residue 1-30
type TOPO_DOM
sequence ANNTTGFTRIIKAAGYSWKGLRAAWINEAA
description Cytoplasmic => ECO:0000269|PubMed:8071224
source Swiss-Prot : SWS_FT_FI1

5) chain A
residue 16
type BINDING
sequence Y
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10

6) chain B
residue 94
type BINDING
sequence K
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10

7) chain C
residue 16
type BINDING
sequence Y
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10

8) chain C
residue 28
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10

9) chain C
residue 76
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10

10) chain C
residue 85
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10

11) chain C
residue 94
type BINDING
sequence K
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10

12) chain A
residue 28
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10

13) chain A
residue 76
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10

14) chain A
residue 85
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10

15) chain A
residue 94
type BINDING
sequence K
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10

16) chain B
residue 16
type BINDING
sequence Y
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10

17) chain B
residue 28
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10

18) chain B
residue 76
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10

19) chain B
residue 85
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10

20) chain A
residue 22
type BINDING
sequence R
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26960129
source Swiss-Prot : SWS_FT_FI11

21) chain B
residue 22
type BINDING
sequence R
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26960129
source Swiss-Prot : SWS_FT_FI11

22) chain C
residue 22
type BINDING
sequence R
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26960129
source Swiss-Prot : SWS_FT_FI11

23) chain A
residue 30
type BINDING
sequence A
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129
source Swiss-Prot : SWS_FT_FI12

24) chain B
residue 30
type BINDING
sequence A
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129
source Swiss-Prot : SWS_FT_FI12

25) chain C
residue 30
type BINDING
sequence A
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129
source Swiss-Prot : SWS_FT_FI12

26) chain A
residue 47
type BINDING
sequence W
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.25
source Swiss-Prot : SWS_FT_FI13

27) chain B
residue 47
type BINDING
sequence W
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.25
source Swiss-Prot : SWS_FT_FI13

28) chain C
residue 47
type BINDING
sequence W
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.25
source Swiss-Prot : SWS_FT_FI13

29) chain A
residue 55
type BINDING
sequence R
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.25
source Swiss-Prot : SWS_FT_FI14

30) chain B
residue 55
type BINDING
sequence R
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.25
source Swiss-Prot : SWS_FT_FI14

31) chain C
residue 55
type BINDING
sequence R
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.25
source Swiss-Prot : SWS_FT_FI14

32) chain A
residue 69
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI15

33) chain B
residue 69
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI15

34) chain C
residue 69
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI15

35) chain A
residue 98
type BINDING
sequence S
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129
source Swiss-Prot : SWS_FT_FI16

36) chain B
residue 98
type BINDING
sequence S
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129
source Swiss-Prot : SWS_FT_FI16

37) chain C
residue 98
type BINDING
sequence S
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129
source Swiss-Prot : SWS_FT_FI16

38) chain A
residue 112
type BINDING
sequence W
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI17

39) chain B
residue 112
type BINDING
sequence W
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI17

40) chain C
residue 112
type BINDING
sequence W
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI17

41) chain A
residue 31-47
type TRANSMEM
sequence FRQEGVAVLLAVVIACW
description Helical => ECO:0000305|PubMed:12379131, ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI2

42) chain A
residue 51-68
type TRANSMEM
sequence DAITRVLLISSVMLVMIV
description Helical => ECO:0000305|PubMed:12379131, ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI2

43) chain B
residue 31-47
type TRANSMEM
sequence FRQEGVAVLLAVVIACW
description Helical => ECO:0000305|PubMed:12379131, ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI2

44) chain B
residue 51-68
type TRANSMEM
sequence DAITRVLLISSVMLVMIV
description Helical => ECO:0000305|PubMed:12379131, ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI2

45) chain C
residue 31-47
type TRANSMEM
sequence FRQEGVAVLLAVVIACW
description Helical => ECO:0000305|PubMed:12379131, ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI2

46) chain C
residue 51-68
type TRANSMEM
sequence DAITRVLLISSVMLVMIV
description Helical => ECO:0000305|PubMed:12379131, ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI2

47) chain A
residue 48-50
type TOPO_DOM
sequence LDV
description Periplasmic => ECO:0000305|PubMed:12379131, ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI3

48) chain B
residue 48-50
type TOPO_DOM
sequence LDV
description Periplasmic => ECO:0000305|PubMed:12379131, ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI3

49) chain C
residue 48-50
type TOPO_DOM
sequence LDV
description Periplasmic => ECO:0000305|PubMed:12379131, ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI3

50) chain A
residue 69-94
type TOPO_DOM
sequence EILNSAIEAVVDRIGSEYHELSGRAK
description Cytoplasmic => ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI4

51) chain B
residue 69-94
type TOPO_DOM
sequence EILNSAIEAVVDRIGSEYHELSGRAK
description Cytoplasmic => ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI4

52) chain C
residue 69-94
type TOPO_DOM
sequence EILNSAIEAVVDRIGSEYHELSGRAK
description Cytoplasmic => ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI4

53) chain A
residue 95-118
type TRANSMEM
sequence DMGSAAVLIAIIVAVITWCILLWS
description Helical => ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI5

54) chain B
residue 95-118
type TRANSMEM
sequence DMGSAAVLIAIIVAVITWCILLWS
description Helical => ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI5

55) chain C
residue 95-118
type TRANSMEM
sequence DMGSAAVLIAIIVAVITWCILLWS
description Helical => ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI5

56) chain A
residue 119-121
type TOPO_DOM
sequence HFG
description Periplasmic => ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:8071224
source Swiss-Prot : SWS_FT_FI6

57) chain B
residue 119-121
type TOPO_DOM
sequence HFG
description Periplasmic => ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:8071224
source Swiss-Prot : SWS_FT_FI6

58) chain C
residue 119-121
type TOPO_DOM
sequence HFG
description Periplasmic => ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:8071224
source Swiss-Prot : SWS_FT_FI6

59) chain A
residue 69
type ACT_SITE
sequence E
description Proton acceptor => ECO:0000305|PubMed:26673816
source Swiss-Prot : SWS_FT_FI7

60) chain B
residue 69
type ACT_SITE
sequence E
description Proton acceptor => ECO:0000305|PubMed:26673816
source Swiss-Prot : SWS_FT_FI7

61) chain C
residue 69
type ACT_SITE
sequence E
description Proton acceptor => ECO:0000305|PubMed:26673816
source Swiss-Prot : SWS_FT_FI7

62) chain A
residue 9
type BINDING
sequence R
description BINDING => ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538
source Swiss-Prot : SWS_FT_FI8

63) chain B
residue 9
type BINDING
sequence R
description BINDING => ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538
source Swiss-Prot : SWS_FT_FI8

64) chain C
residue 9
type BINDING
sequence R
description BINDING => ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538
source Swiss-Prot : SWS_FT_FI8

65) chain A
residue 13
type BINDING
sequence A
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129
source Swiss-Prot : SWS_FT_FI9

66) chain B
residue 13
type BINDING
sequence A
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129
source Swiss-Prot : SWS_FT_FI9

67) chain C
residue 13
type BINDING
sequence A
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129
source Swiss-Prot : SWS_FT_FI9


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