eF-site/Summary 4uyo-A

eF-site ID	4uyo-A
PDB Code	4uyo
Chain	A

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Title	Structure of delta7-DgkA in 7.9 MAG by serial femtosecond crystatallography to 2.18 angstrom resolution
Classification	TRANSFERASE
Compound	DIACYLGLYCEROL KINASE-DELTA 7
Source	(KDGL_ECOLI)

Sequence	A:	GFTRIIKAAGYSWKGLRAAWINEAAFRQEGVAVLLCVVIA AWLDVDAVTRVLLISSVMLVMIVELLNSAIEAVVDRIGSE YHELSGRAKDLGSAAVLIAIIDAVITWAILLWSHFG

Description

Functional site


1)	chain	A
	residue	21
	type
	sequence	L
	description	BINDING SITE FOR RESIDUE 79N A 1122
	source	: AC1

2)	chain	A
	residue	22
	type
	sequence	R
	description	BINDING SITE FOR RESIDUE 79N A 1122
	source	: AC1

3)	chain	A
	residue	25
	type
	sequence	W
	description	BINDING SITE FOR RESIDUE 79N A 1122
	source	: AC1

4)	chain	A
	residue	39
	type
	sequence	L
	description	BINDING SITE FOR RESIDUE 79N C 1122
	source	: AC5

5)	chain	A
	residue	40
	type
	sequence	L
	description	BINDING SITE FOR RESIDUE 79N C 1122
	source	: AC5

6)	chain	A
	residue	33
	type
	sequence	Q
	description	BINDING SITE FOR RESIDUE 79N D 1123
	source	: AC6

7)	chain	A
	residue	34
	type
	sequence	E
	description	BINDING SITE FOR RESIDUE 79M D 1125
	source	: AC8

8)	chain	A
	residue	69
	type
	sequence	E
	description	BINDING SITE FOR RESIDUE 79M D 1125
	source	: AC8

9)	chain	A
	residue	101
	type
	sequence	V
	description	BINDING SITE FOR RESIDUE 79M D 1125
	source	: AC8

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

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

12)	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

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

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

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

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

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

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

19)	chain	A
	residue	94
	type	BINDING
	sequence	K
	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	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

22)	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

23)	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

24)	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

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

26)	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

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

28)	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

29)	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

30)	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

31)	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