eF-site ID 3ze5-ABC
PDB Code 3ze5
Chain A, B, C

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Title Crystal structure of the integral membrane diacylglycerol kinase - delta4
Classification TRANSFERASE
Compound DIACYLGLYCEROL KINASE
Source (KDGL_ECOLI)
Sequence A:  FTRIIKAAGYSWKGLRAAWINEAAFRQEGVAVLLAVVIAC
WLDVDACTRVLLISSVMLVMIVELLNSAIEAVVDRIGSEY
HELSGRAKDLGSAAVLIAIIDAVITWCILLWSHFG
B:  GFTRIIKAAGYSWKGLRAAWINEAAFRQEGVAVLLAVVIA
CWLDVDACTRVLLISSVMLVMIVELLNSAIEAVVDRIGSE
YHELSGRAKDLGSAAVLIAIIDAVITWCILLWSHFG
C:  YSWKGLRAAWINEAAFRQEGVAVLLAVVIACWLDVDACTR
VLLISSVMLVMIVELLNSAIEAVVDRIGSEYHELSGRAKD
LGSAAVLIAIIDAVITWCILLWSH
Description


Functional site
1) 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
2) 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
3) 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
4) 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
5) 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
6) 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
7) 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
8) 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
9) 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
10) chain A
residue 69-94
type TOPO_DOM
sequence ELLNSAIEAVVDRIGSEYHELSGRAK
description Cytoplasmic => ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI4
11) chain B
residue 69-94
type TOPO_DOM
sequence ELLNSAIEAVVDRIGSEYHELSGRAK
description Cytoplasmic => ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI4
12) chain C
residue 69-94
type TOPO_DOM
sequence ELLNSAIEAVVDRIGSEYHELSGRAK
description Cytoplasmic => ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI4
13) chain A
residue 95-118
type TRANSMEM
sequence DLGSAAVLIAIIDAVITWCILLWS
description Helical => ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI5
14) chain B
residue 95-118
type TRANSMEM
sequence DLGSAAVLIAIIDAVITWCILLWS
description Helical => ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI5
15) chain C
residue 95-118
type TRANSMEM
sequence DLGSAAVLIAIIDAVITWCILLWS
description Helical => ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI5
16) 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
17) 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
18) chain A
residue 69
type ACT_SITE
sequence E
description Proton acceptor => ECO:0000305|PubMed:26673816
source Swiss-Prot : SWS_FT_FI7
19) chain B
residue 69
type ACT_SITE
sequence E
description Proton acceptor => ECO:0000305|PubMed:26673816
source Swiss-Prot : SWS_FT_FI7
20) chain C
residue 69
type ACT_SITE
sequence E
description Proton acceptor => ECO:0000305|PubMed:26673816
source Swiss-Prot : SWS_FT_FI7
21) 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
22) 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
23) chain A
residue 16
type BINDING
sequence Y
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10
24) chain B
residue 94
type BINDING
sequence K
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10
25) chain C
residue 16
type BINDING
sequence Y
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10
26) chain C
residue 28
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10
27) chain C
residue 76
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10
28) chain C
residue 85
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10
29) chain C
residue 94
type BINDING
sequence K
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10
30) chain A
residue 28
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10
31) chain A
residue 76
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10
32) chain A
residue 85
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10
33) chain A
residue 94
type BINDING
sequence K
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10
34) chain B
residue 16
type BINDING
sequence Y
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10
35) chain B
residue 28
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10
36) chain B
residue 76
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10
37) chain B
residue 85
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10
38) 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
39) 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
40) 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
41) chain A
residue 69-80
type prosite
sequence ELLNSAIEAVVD
description DAGK_PROKAR Prokaryotic diacylglycerol kinase signature. ElLNSAIEavVD
source prosite : PS01069
42) 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
43) 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
44) 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
45) 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
46) 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
47) 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
48) 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
49) 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
50) 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
51) 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
52) 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
53) 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
54) 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
55) 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
56) 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
57) 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
58) 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
59) 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
60) 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
61) 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

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