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

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Title Crystal structure of the integral membrane diacylglycerol kinase - form 2
Classification TRANSFERASE
Compound DIACYLGLYCEROL KINASE
Source (KDGL_ECOLI)
Sequence B:  FTRIIKAAGYSWKGLRAAWINEAAFRQEGVAVLLAVVIAC
WLDVDACTRVLLISSVMLVMIVELLNSAIEAVVDRIGSEY
HELSGRAKDLGSAAVLIAIIDAVITWCILLWSHF
Description


Functional site
1) chain B
residue 9
type
sequence R
description BINDING SITE FOR RESIDUE ACP C 1122
source : AC3
2) chain B
residue 12
type
sequence K
description BINDING SITE FOR RESIDUE ACP C 1122
source : AC3
3) chain B
residue 16
type
sequence Y
description BINDING SITE FOR RESIDUE ACP C 1122
source : AC3
4) chain B
residue 44
type
sequence I
description BINDING SITE FOR RESIDUE OLC B 1121
source : AC4
5) chain B
residue 69
type
sequence E
description BINDING SITE FOR RESIDUE OLC B 1121
source : AC4
6) chain B
residue 72
type
sequence N
description BINDING SITE FOR RESIDUE OLC B 1121
source : AC4
7) chain B
residue 102
type
sequence L
description BINDING SITE FOR RESIDUE OLC B 1121
source : AC4
8) chain B
residue 105
type
sequence I
description BINDING SITE FOR RESIDUE OLC B 1121
source : AC4
9) chain B
residue 33
type
sequence Q
description BINDING SITE FOR RESIDUE OLC B 1122
source : AC5
10) chain B
residue 34
type
sequence E
description BINDING SITE FOR RESIDUE OLC B 1122
source : AC5
11) chain B
residue 37
type
sequence A
description BINDING SITE FOR RESIDUE OLC B 1122
source : AC5
12) chain B
residue 62
type
sequence V
description BINDING SITE FOR RESIDUE OLC B 1122
source : AC5
13) chain B
residue 105
type
sequence I
description BINDING SITE FOR RESIDUE OLC B 1122
source : AC5
14) chain B
residue 113
type
sequence C
description BINDING SITE FOR RESIDUE OLC B 1122
source : AC5
15) chain B
residue 94
type BINDING
sequence K
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10
16) chain B
residue 16
type BINDING
sequence Y
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10
17) chain B
residue 28
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10
18) chain B
residue 76
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10
19) chain B
residue 85
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10
20) 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
21) 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
22) 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
23) 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
24) 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
25) 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
26) 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
27) 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
28) 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
29) 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
30) chain B
residue 69-94
type TOPO_DOM
sequence ELLNSAIEAVVDRIGSEYHELSGRAK
description Cytoplasmic => ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI4
31) chain B
residue 95-118
type TRANSMEM
sequence DLGSAAVLIAIIDAVITWCILLWS
description Helical => ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI5
32) chain B
residue 69
type ACT_SITE
sequence E
description Proton acceptor => ECO:0000305|PubMed:26673816
source Swiss-Prot : SWS_FT_FI7
33) 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
34) 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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