eF-site/Summary 4uxz-C

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

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

Sequence	C:	RQEGVAVLLCVVIAAWLDVDAVTRVLLISSVMLVMIVELL NSAIEAVVDRIGSEYHELSGRAKDLGSAAVLIAIIDAVIT WAILLWSHFG

Description

Functional site


1)	chain	C
	residue	117
	type
	sequence	W
	description	BINDING SITE FOR RESIDUE 79M C 1122
	source	: AC2

2)	chain	C
	residue	114
	type
	sequence	I
	description	BINDING SITE FOR RESIDUE 79M B 1121
	source	: AC3

3)	chain	C
	residue	102
	type
	sequence	L
	description	BINDING SITE FOR RESIDUE 79N A 1123
	source	: BC1

4)	chain	C
	residue	105
	type
	sequence	I
	description	BINDING SITE FOR RESIDUE 79N A 1123
	source	: BC1

5)	chain	C
	residue	34
	type
	sequence	E
	description	BINDING SITE FOR RESIDUE 79N A 1124
	source	: BC2

6)	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

7)	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

8)	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

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	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

13)	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

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

15)	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

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

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

18)	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

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