eF-site/Summary 4ck0-C

eF-site ID	4ck0-C
PDB Code	4ck0
Chain	C

click to enlarge

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

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

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

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

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

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

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

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

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

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

13)	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

14)	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

15)	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

16)	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

17)	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

18)	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

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

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

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

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

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

24)	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

25)	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

26)	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

27)	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

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

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

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