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

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Title Structure of delta4-DgkA with AMPPCP in 9.9 MAG
Classification TRANSFERASE
Compound DIACYLGLYCEROL KINASE
Source (KDGL_ECOLI)
Sequence C:  YSWKGLRAAWINEAAFRQEGVAVLLAVVIACWLDVDACTR
VLLISSVMLVMIVELLNSAIEAVVDRIGSEYHELSGRAKD
LGSAAVLIAIIDAVITWCILLWSHF
Description


Functional site
1) chain C
residue 28
type
sequence E
description BINDING SITE FOR RESIDUE ZN C 1121
source : AC1
2) chain C
residue 76
type
sequence E
description BINDING SITE FOR RESIDUE ZN C 1121
source : AC1
3) chain C
residue 76
type
sequence E
description BINDING SITE FOR RESIDUE ZN C 1122
source : AC2
4) chain C
residue 28
type
sequence E
description BINDING SITE FOR RESIDUE ACP C 1123
source : AC4
5) chain C
residue 72
type
sequence N
description BINDING SITE FOR RESIDUE ACP C 1123
source : AC4
6) chain C
residue 76
type
sequence E
description BINDING SITE FOR RESIDUE ACP C 1123
source : AC4
7) chain C
residue 85
type
sequence E
description BINDING SITE FOR RESIDUE ACP C 1123
source : AC4
8) chain C
residue 86
type
sequence Y
description BINDING SITE FOR RESIDUE ACP C 1123
source : AC4
9) chain C
residue 87
type
sequence H
description BINDING SITE FOR RESIDUE ACP C 1123
source : AC4
10) chain C
residue 90
type
sequence S
description BINDING SITE FOR RESIDUE ACP C 1123
source : AC4
11) chain C
residue 91
type
sequence G
description BINDING SITE FOR RESIDUE ACP C 1123
source : AC4
12) chain C
residue 94
type
sequence K
description BINDING SITE FOR RESIDUE ACP C 1123
source : AC4
13) chain C
residue 95
type
sequence D
description BINDING SITE FOR RESIDUE ACP C 1123
source : AC4
14) chain C
residue 30
type
sequence A
description BINDING SITE FOR RESIDUE OLC C 1124
source : AC8
15) chain C
residue 33
type
sequence Q
description BINDING SITE FOR RESIDUE OLC C 1124
source : AC8
16) chain C
residue 34
type
sequence E
description BINDING SITE FOR RESIDUE OLC C 1124
source : AC8
17) chain C
residue 113
type
sequence C
description BINDING SITE FOR RESIDUE OLC C 1124
source : AC8
18) chain C
residue 69
type
sequence E
description BINDING SITE FOR RESIDUE OLC C 1125
source : BC4
19) chain C
residue 72
type
sequence N
description BINDING SITE FOR RESIDUE OLC C 1125
source : BC4
20) chain C
residue 98
type
sequence S
description BINDING SITE FOR RESIDUE OLC C 1125
source : BC4
21) chain C
residue 102
type
sequence L
description BINDING SITE FOR RESIDUE OLC C 1125
source : BC4
22) chain C
residue 106
type
sequence I
description BINDING SITE FOR RESIDUE OLC C 1125
source : BC4
23) chain C
residue 109
type
sequence V
description BINDING SITE FOR RESIDUE OLC C 1125
source : BC4
24) chain C
residue 88
type
sequence E
description BINDING SITE FOR RESIDUE NA C 1126
source : BC7
25) chain C
residue 88
type
sequence E
description BINDING SITE FOR RESIDUE NA C 1126
source : BC7
26) 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
27) 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
28) 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
29) chain C
residue 16
type BINDING
sequence Y
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10
30) chain C
residue 28
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10
31) chain C
residue 76
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10
32) chain C
residue 85
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10
33) chain C
residue 94
type BINDING
sequence K
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10
34) 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
35) 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
36) 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
37) 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
38) 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
39) 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
40) 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
41) chain C
residue 69-94
type TOPO_DOM
sequence ELLNSAIEAVVDRIGSEYHELSGRAK
description Cytoplasmic => ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI4
42) chain C
residue 95-118
type TRANSMEM
sequence DLGSAAVLIAIIDAVITWCILLWS
description Helical => ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI5
43) chain C
residue 69
type ACT_SITE
sequence E
description Proton acceptor => ECO:0000305|PubMed:26673816
source Swiss-Prot : SWS_FT_FI7

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