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

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Title Structure of delta4-DgkA with AMPPCP in 9.9 MAG
Classification TRANSFERASE
Compound DIACYLGLYCEROL KINASE
Source (KDGL_ECOLI)
Sequence A:  FTRIIKAAGYSWKGLRAAWINEAAFRQEGVAVLLAVVIAC
WLDVDACTRVLLISSVMLVMIVELLNSAIEAVVDRIGSEY
HELSGRAKDLGSAAVLIAIIDAVITWCILLWSHFG
Description


Functional site
1) chain A
residue 27
type
sequence N
description BINDING SITE FOR RESIDUE CL A 1121
source : AC3
2) chain A
residue 29
type
sequence A
description BINDING SITE FOR RESIDUE CL A 1121
source : AC3
3) chain A
residue 32
type
sequence R
description BINDING SITE FOR RESIDUE CL A 1121
source : AC3
4) chain A
residue 81
type
sequence R
description BINDING SITE FOR RESIDUE MPD B 1122
source : AC5
5) chain A
residue 28
type
sequence E
description BINDING SITE FOR RESIDUE NA A 1122
source : AC6
6) chain A
residue 76
type
sequence E
description BINDING SITE FOR RESIDUE NA A 1122
source : AC6
7) chain A
residue 28
type
sequence E
description BINDING SITE FOR RESIDUE ACT A 1123
source : AC7
8) chain A
residue 76
type
sequence E
description BINDING SITE FOR RESIDUE ACT A 1123
source : AC7
9) chain A
residue 17
type
sequence S
description BINDING SITE FOR RESIDUE OLC B 1123
source : AC9
10) chain A
residue 113
type
sequence C
description BINDING SITE FOR RESIDUE OLC B 1123
source : AC9
11) chain A
residue 117
type
sequence W
description BINDING SITE FOR RESIDUE OLC B 1123
source : AC9
12) chain A
residue 10
type
sequence I
description BINDING SITE FOR RESIDUE OLC B 1124
source : BC1
13) chain A
residue 117
type
sequence W
description BINDING SITE FOR RESIDUE OLC B 1124
source : BC1
14) chain A
residue 18
type
sequence W
description BINDING SITE FOR RESIDUE OLC A 1124
source : BC2
15) chain A
residue 25
type
sequence W
description BINDING SITE FOR RESIDUE OLC A 1124
source : BC2
16) chain A
residue 26
type
sequence I
description BINDING SITE FOR RESIDUE OLC A 1124
source : BC2
17) chain A
residue 33
type
sequence Q
description BINDING SITE FOR RESIDUE OLC A 1125
source : BC3
18) chain A
residue 34
type
sequence E
description BINDING SITE FOR RESIDUE OLC A 1125
source : BC3
19) chain A
residue 37
type
sequence A
description BINDING SITE FOR RESIDUE OLC A 1125
source : BC3
20) chain A
residue 44
type
sequence I
description BINDING SITE FOR RESIDUE OLC A 1125
source : BC3
21) chain A
residue 62
type
sequence V
description BINDING SITE FOR RESIDUE OLC A 1125
source : BC3
22) chain A
residue 108
type
sequence A
description BINDING SITE FOR RESIDUE OLC A 1125
source : BC3
23) chain A
residue 109
type
sequence V
description BINDING SITE FOR RESIDUE OLC A 1125
source : BC3
24) chain A
residue 112
type
sequence W
description BINDING SITE FOR RESIDUE OLC A 1125
source : BC3
25) chain A
residue 116
type
sequence L
description BINDING SITE FOR RESIDUE OLC A 1125
source : BC3
26) chain A
residue 119
type
sequence H
description BINDING SITE FOR RESIDUE ACT A 1126
source : BC8
27) 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
28) 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
29) 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
30) chain A
residue 16
type BINDING
sequence Y
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10
31) chain A
residue 28
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 A
residue 76
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10
35) 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
36) 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
37) 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
38) 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
39) 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
40) 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
41) 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
42) 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
43) chain A
residue 69-94
type TOPO_DOM
sequence ELLNSAIEAVVDRIGSEYHELSGRAK
description Cytoplasmic => ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI4
44) chain A
residue 95-118
type TRANSMEM
sequence DLGSAAVLIAIIDAVITWCILLWS
description Helical => ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI5
45) 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
46) chain A
residue 69
type ACT_SITE
sequence E
description Proton acceptor => ECO:0000305|PubMed:26673816
source Swiss-Prot : SWS_FT_FI7
47) 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
48) chain A
residue 69-80
type prosite
sequence ELLNSAIEAVVD
description DAGK_PROKAR Prokaryotic diacylglycerol kinase signature. ElLNSAIEavVD
source prosite : PS01069

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