eF-site/Summary 4ck0-ABC

eF-site ID	4ck0-ABC
PDB Code	4ck0
Chain	A, B, C

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Title	Crystal structure of the integral membrane diacylglycerol kinase - form 2
Classification	TRANSFERASE
Compound	DIACYLGLYCEROL KINASE
Source	(KDGL_ECOLI)

Sequence	A:	FTRIIKAAGYSWKGLRAAWINEAAFRQEGVAVLLAVVIAC WLDVDACTRVLLISSVMLVMIVELLNSAIEAVVDRIGSEY HELSGRAKDLGSAAVLIAIIDAVITWCILLWSHF
	B:	FTRIIKAAGYSWKGLRAAWINEAAFRQEGVAVLLAVVIAC WLDVDACTRVLLISSVMLVMIVELLNSAIEAVVDRIGSEY HELSGRAKDLGSAAVLIAIIDAVITWCILLWSHF
	C:	YSWKGLRAAWINEAAFRQEGVAVLLAVVIACWLDVDACTR VLLISSVMLVMIVELLNSAIEAVVDRIGSEYHELSGRAKD LGSAAVLIAIIDAVITWCILLWSH

Description

Functional site


1)	chain	C
	residue	28
	type
	sequence	E
	description	BINDING SITE FOR RESIDUE ZN C 1120
	source	: AC1

2)	chain	C
	residue	76
	type
	sequence	E
	description	BINDING SITE FOR RESIDUE ZN C 1120
	source	: AC1

3)	chain	C
	residue	76
	type
	sequence	E
	description	BINDING SITE FOR RESIDUE ZN C 1121
	source	: AC2

4)	chain	B
	residue	9
	type
	sequence	R
	description	BINDING SITE FOR RESIDUE ACP C 1122
	source	: AC3

5)	chain	B
	residue	12
	type
	sequence	K
	description	BINDING SITE FOR RESIDUE ACP C 1122
	source	: AC3

6)	chain	B
	residue	16
	type
	sequence	Y
	description	BINDING SITE FOR RESIDUE ACP C 1122
	source	: AC3

7)	chain	C
	residue	28
	type
	sequence	E
	description	BINDING SITE FOR RESIDUE ACP C 1122
	source	: AC3

8)	chain	C
	residue	76
	type
	sequence	E
	description	BINDING SITE FOR RESIDUE ACP C 1122
	source	: AC3

9)	chain	C
	residue	85
	type
	sequence	E
	description	BINDING SITE FOR RESIDUE ACP C 1122
	source	: AC3

10)	chain	C
	residue	86
	type
	sequence	Y
	description	BINDING SITE FOR RESIDUE ACP C 1122
	source	: AC3

11)	chain	C
	residue	87
	type
	sequence	H
	description	BINDING SITE FOR RESIDUE ACP C 1122
	source	: AC3

12)	chain	C
	residue	90
	type
	sequence	S
	description	BINDING SITE FOR RESIDUE ACP C 1122
	source	: AC3

13)	chain	C
	residue	91
	type
	sequence	G
	description	BINDING SITE FOR RESIDUE ACP C 1122
	source	: AC3

14)	chain	C
	residue	94
	type
	sequence	K
	description	BINDING SITE FOR RESIDUE ACP C 1122
	source	: AC3

15)	chain	C
	residue	95
	type
	sequence	D
	description	BINDING SITE FOR RESIDUE ACP C 1122
	source	: AC3

16)	chain	A
	residue	13
	type
	sequence	A
	description	BINDING SITE FOR RESIDUE OLC B 1121
	source	: AC4

17)	chain	A
	residue	14
	type
	sequence	A
	description	BINDING SITE FOR RESIDUE OLC B 1121
	source	: AC4

18)	chain	A
	residue	17
	type
	sequence	S
	description	BINDING SITE FOR RESIDUE OLC B 1121
	source	: AC4

19)	chain	B
	residue	44
	type
	sequence	I
	description	BINDING SITE FOR RESIDUE OLC B 1121
	source	: AC4

20)	chain	B
	residue	69
	type
	sequence	E
	description	BINDING SITE FOR RESIDUE OLC B 1121
	source	: AC4

21)	chain	B
	residue	72
	type
	sequence	N
	description	BINDING SITE FOR RESIDUE OLC B 1121
	source	: AC4

22)	chain	B
	residue	102
	type
	sequence	L
	description	BINDING SITE FOR RESIDUE OLC B 1121
	source	: AC4

23)	chain	B
	residue	105
	type
	sequence	I
	description	BINDING SITE FOR RESIDUE OLC B 1121
	source	: AC4

24)	chain	A
	residue	10
	type
	sequence	I
	description	BINDING SITE FOR RESIDUE OLC B 1122
	source	: AC5

25)	chain	A
	residue	117
	type
	sequence	W
	description	BINDING SITE FOR RESIDUE OLC B 1122
	source	: AC5

26)	chain	B
	residue	33
	type
	sequence	Q
	description	BINDING SITE FOR RESIDUE OLC B 1122
	source	: AC5

27)	chain	B
	residue	34
	type
	sequence	E
	description	BINDING SITE FOR RESIDUE OLC B 1122
	source	: AC5

28)	chain	B
	residue	37
	type
	sequence	A
	description	BINDING SITE FOR RESIDUE OLC B 1122
	source	: AC5

29)	chain	B
	residue	62
	type
	sequence	V
	description	BINDING SITE FOR RESIDUE OLC B 1122
	source	: AC5

30)	chain	B
	residue	105
	type
	sequence	I
	description	BINDING SITE FOR RESIDUE OLC B 1122
	source	: AC5

31)	chain	B
	residue	113
	type
	sequence	C
	description	BINDING SITE FOR RESIDUE OLC B 1122
	source	: AC5

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	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

42)	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

43)	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

44)	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

45)	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

46)	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

47)	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

48)	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

49)	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

50)	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

51)	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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

67)	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

68)	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

69)	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

70)	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

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

72)	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

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

74)	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

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

76)	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

77)	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

78)	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

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

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

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

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

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

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

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

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

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

88)	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

89)	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

90)	chain	A
	residue	69-80
	type	prosite
	sequence	ELLNSAIEAVVD
	description	DAGK_PROKAR Prokaryotic diacylglycerol kinase signature. ElLNSAIEavVD
	source	prosite : PS01069