eF-site/Summary 4uyo-B

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

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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	B:	AWINEAAFRQEGVAVLLCVVIAAWLDVDAVTRVLLISSVM LVMIVELLNSAIEAVVDRIGSEYHELSGRAKDLGSAAVLI AIIDAVITWAILLWSHFG

Description

Functional site


1)	chain	B
	residue	46
	type
	sequence	A
	description	BINDING SITE FOR RESIDUE 79M B 1122
	source	: AC2

2)	chain	B
	residue	50
	type
	sequence	V
	description	BINDING SITE FOR RESIDUE 79M B 1122
	source	: AC2

3)	chain	B
	residue	52
	type
	sequence	A
	description	BINDING SITE FOR RESIDUE 79M B 1122
	source	: AC2

4)	chain	B
	residue	55
	type
	sequence	R
	description	BINDING SITE FOR RESIDUE 79M B 1122
	source	: AC2

5)	chain	B
	residue	34
	type
	sequence	E
	description	BINDING SITE FOR RESIDUE 79N B 1123
	source	: AC3

6)	chain	B
	residue	41
	type
	sequence	C
	description	BINDING SITE FOR RESIDUE 79N B 1123
	source	: AC3

7)	chain	B
	residue	62
	type
	sequence	V
	description	BINDING SITE FOR RESIDUE 79N B 1123
	source	: AC3

8)	chain	B
	residue	69
	type
	sequence	E
	description	BINDING SITE FOR RESIDUE 79N B 1123
	source	: AC3

9)	chain	B
	residue	112
	type
	sequence	W
	description	BINDING SITE FOR RESIDUE 79N B 1123
	source	: AC3

10)	chain	B
	residue	49
	type
	sequence	D
	description	BINDING SITE FOR RESIDUE 79M B 1124
	source	: AC4

11)	chain	B
	residue	26
	type
	sequence	I
	description	BINDING SITE FOR RESIDUE 79N D 1124
	source	: AC7

12)	chain	B
	residue	32
	type
	sequence	R
	description	BINDING SITE FOR RESIDUE 79N D 1124
	source	: AC7

13)	chain	B
	residue	35
	type
	sequence	G
	description	BINDING SITE FOR RESIDUE 79N D 1124
	source	: AC7

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

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

16)	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

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

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

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

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

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

22)	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

23)	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

24)	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

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

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

27)	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

28)	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

29)	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

30)	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