eF-site ID 4uxx-ABC
PDB Code 4uxx
Chain A, B, 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 A:  FTRIIKAAGYSWKGLRAAWINEAAFRQEGVAVLLAVVIAC
WLDVDACTRVLLISSVMLVMIVELLNSAIEAVVDRIGSEY
HELSGRAKDLGSAAVLIAIIDAVITWCILLWSHFG
B:  GFTRIIKAAGYSWKGLRAAWINEAAFRQEGVAVLLAVVIA
CWLDVDACTRVLLISSVMLVMIVELLNSAIEAVVDRIGSE
YHELSGRAKDLGSAAVLIAIIDAVITWCILLWSHFG
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 A
residue 27
type
sequence N
description BINDING SITE FOR RESIDUE CL A 1121
source : AC3
5) chain A
residue 29
type
sequence A
description BINDING SITE FOR RESIDUE CL A 1121
source : AC3
6) chain A
residue 32
type
sequence R
description BINDING SITE FOR RESIDUE CL A 1121
source : AC3
7) chain B
residue 9
type
sequence R
description BINDING SITE FOR RESIDUE ACP C 1123
source : AC4
8) chain B
residue 16
type
sequence Y
description BINDING SITE FOR RESIDUE ACP C 1123
source : AC4
9) chain C
residue 28
type
sequence E
description BINDING SITE FOR RESIDUE ACP C 1123
source : AC4
10) chain C
residue 72
type
sequence N
description BINDING SITE FOR RESIDUE ACP C 1123
source : AC4
11) chain C
residue 76
type
sequence E
description BINDING SITE FOR RESIDUE ACP C 1123
source : AC4
12) chain C
residue 85
type
sequence E
description BINDING SITE FOR RESIDUE ACP C 1123
source : AC4
13) chain C
residue 86
type
sequence Y
description BINDING SITE FOR RESIDUE ACP C 1123
source : AC4
14) chain C
residue 87
type
sequence H
description BINDING SITE FOR RESIDUE ACP C 1123
source : AC4
15) chain C
residue 90
type
sequence S
description BINDING SITE FOR RESIDUE ACP C 1123
source : AC4
16) chain C
residue 91
type
sequence G
description BINDING SITE FOR RESIDUE ACP C 1123
source : AC4
17) chain C
residue 94
type
sequence K
description BINDING SITE FOR RESIDUE ACP C 1123
source : AC4
18) chain C
residue 95
type
sequence D
description BINDING SITE FOR RESIDUE ACP C 1123
source : AC4
19) chain A
residue 81
type
sequence R
description BINDING SITE FOR RESIDUE MPD B 1122
source : AC5
20) chain B
residue 88
type
sequence E
description BINDING SITE FOR RESIDUE MPD B 1122
source : AC5
21) chain B
residue 89
type
sequence L
description BINDING SITE FOR RESIDUE MPD B 1122
source : AC5
22) chain B
residue 90
type
sequence S
description BINDING SITE FOR RESIDUE MPD B 1122
source : AC5
23) chain B
residue 92
type
sequence R
description BINDING SITE FOR RESIDUE MPD B 1122
source : AC5
24) chain A
residue 28
type
sequence E
description BINDING SITE FOR RESIDUE NA A 1122
source : AC6
25) chain A
residue 76
type
sequence E
description BINDING SITE FOR RESIDUE NA A 1122
source : AC6
26) chain A
residue 28
type
sequence E
description BINDING SITE FOR RESIDUE ACT A 1123
source : AC7
27) chain A
residue 76
type
sequence E
description BINDING SITE FOR RESIDUE ACT A 1123
source : AC7
28) chain B
residue 9
type
sequence R
description BINDING SITE FOR RESIDUE OLC C 1124
source : AC8
29) chain B
residue 10
type
sequence I
description BINDING SITE FOR RESIDUE OLC C 1124
source : AC8
30) chain C
residue 30
type
sequence A
description BINDING SITE FOR RESIDUE OLC C 1124
source : AC8
31) chain C
residue 33
type
sequence Q
description BINDING SITE FOR RESIDUE OLC C 1124
source : AC8
32) chain C
residue 34
type
sequence E
description BINDING SITE FOR RESIDUE OLC C 1124
source : AC8
33) chain C
residue 113
type
sequence C
description BINDING SITE FOR RESIDUE OLC C 1124
source : AC8
34) chain A
residue 17
type
sequence S
description BINDING SITE FOR RESIDUE OLC B 1123
source : AC9
35) chain A
residue 113
type
sequence C
description BINDING SITE FOR RESIDUE OLC B 1123
source : AC9
36) chain A
residue 117
type
sequence W
description BINDING SITE FOR RESIDUE OLC B 1123
source : AC9
37) chain B
residue 34
type
sequence E
description BINDING SITE FOR RESIDUE OLC B 1123
source : AC9
38) chain B
residue 37
type
sequence A
description BINDING SITE FOR RESIDUE OLC B 1123
source : AC9
39) chain B
residue 44
type
sequence I
description BINDING SITE FOR RESIDUE OLC B 1123
source : AC9
40) chain B
residue 69
type
sequence E
description BINDING SITE FOR RESIDUE OLC B 1123
source : AC9
41) chain B
residue 72
type
sequence N
description BINDING SITE FOR RESIDUE OLC B 1123
source : AC9
42) chain B
residue 102
type
sequence L
description BINDING SITE FOR RESIDUE OLC B 1123
source : AC9
43) chain A
residue 10
type
sequence I
description BINDING SITE FOR RESIDUE OLC B 1124
source : BC1
44) chain A
residue 117
type
sequence W
description BINDING SITE FOR RESIDUE OLC B 1124
source : BC1
45) chain B
residue 33
type
sequence Q
description BINDING SITE FOR RESIDUE OLC B 1124
source : BC1
46) chain B
residue 34
type
sequence E
description BINDING SITE FOR RESIDUE OLC B 1124
source : BC1
47) chain B
residue 112
type
sequence W
description BINDING SITE FOR RESIDUE OLC B 1124
source : BC1
48) chain B
residue 117
type
sequence W
description BINDING SITE FOR RESIDUE OLC B 1124
source : BC1
49) chain A
residue 18
type
sequence W
description BINDING SITE FOR RESIDUE OLC A 1124
source : BC2
50) chain A
residue 25
type
sequence W
description BINDING SITE FOR RESIDUE OLC A 1124
source : BC2
51) chain A
residue 26
type
sequence I
description BINDING SITE FOR RESIDUE OLC A 1124
source : BC2
52) chain A
residue 33
type
sequence Q
description BINDING SITE FOR RESIDUE OLC A 1125
source : BC3
53) chain A
residue 34
type
sequence E
description BINDING SITE FOR RESIDUE OLC A 1125
source : BC3
54) chain A
residue 37
type
sequence A
description BINDING SITE FOR RESIDUE OLC A 1125
source : BC3
55) chain A
residue 44
type
sequence I
description BINDING SITE FOR RESIDUE OLC A 1125
source : BC3
56) chain A
residue 62
type
sequence V
description BINDING SITE FOR RESIDUE OLC A 1125
source : BC3
57) chain A
residue 108
type
sequence A
description BINDING SITE FOR RESIDUE OLC A 1125
source : BC3
58) chain A
residue 109
type
sequence V
description BINDING SITE FOR RESIDUE OLC A 1125
source : BC3
59) chain A
residue 112
type
sequence W
description BINDING SITE FOR RESIDUE OLC A 1125
source : BC3
60) chain A
residue 116
type
sequence L
description BINDING SITE FOR RESIDUE OLC A 1125
source : BC3
61) chain B
residue 39
type
sequence L
description BINDING SITE FOR RESIDUE OLC A 1125
source : BC3
62) chain B
residue 40
type
sequence L
description BINDING SITE FOR RESIDUE OLC A 1125
source : BC3
63) chain B
residue 47
type
sequence W
description BINDING SITE FOR RESIDUE OLC A 1125
source : BC3
64) chain B
residue 13
type
sequence A
description BINDING SITE FOR RESIDUE OLC C 1125
source : BC4
65) chain B
residue 17
type
sequence S
description BINDING SITE FOR RESIDUE OLC C 1125
source : BC4
66) chain C
residue 69
type
sequence E
description BINDING SITE FOR RESIDUE OLC C 1125
source : BC4
67) chain C
residue 72
type
sequence N
description BINDING SITE FOR RESIDUE OLC C 1125
source : BC4
68) chain C
residue 98
type
sequence S
description BINDING SITE FOR RESIDUE OLC C 1125
source : BC4
69) chain C
residue 102
type
sequence L
description BINDING SITE FOR RESIDUE OLC C 1125
source : BC4
70) chain C
residue 106
type
sequence I
description BINDING SITE FOR RESIDUE OLC C 1125
source : BC4
71) chain C
residue 109
type
sequence V
description BINDING SITE FOR RESIDUE OLC C 1125
source : BC4
72) chain B
residue 76
type
sequence E
description BINDING SITE FOR RESIDUE ACT B 1125
source : BC5
73) chain B
residue 83
type
sequence G
description BINDING SITE FOR RESIDUE ACT B 1125
source : BC5
74) chain B
residue 84
type
sequence S
description BINDING SITE FOR RESIDUE ACT B 1125
source : BC5
75) chain B
residue 85
type
sequence E
description BINDING SITE FOR RESIDUE ACT B 1125
source : BC5
76) chain B
residue 86
type
sequence Y
description BINDING SITE FOR RESIDUE ACT B 1125
source : BC5
77) chain B
residue 87
type
sequence H
description BINDING SITE FOR RESIDUE ACT B 1125
source : BC5
78) chain B
residue 94
type
sequence K
description BINDING SITE FOR RESIDUE ACT B 1125
source : BC5
79) chain B
residue 28
type
sequence E
description BINDING SITE FOR RESIDUE NA B 1126
source : BC6
80) chain B
residue 76
type
sequence E
description BINDING SITE FOR RESIDUE NA B 1126
source : BC6
81) chain C
residue 88
type
sequence E
description BINDING SITE FOR RESIDUE NA C 1126
source : BC7
82) chain C
residue 88
type
sequence E
description BINDING SITE FOR RESIDUE NA C 1126
source : BC7
83) chain A
residue 119
type
sequence H
description BINDING SITE FOR RESIDUE ACT A 1126
source : BC8
84) 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
85) 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
86) 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
87) 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
88) 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
89) 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
90) 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
91) 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
92) 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
93) 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
94) 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
95) chain A
residue 69-94
type TOPO_DOM
sequence ELLNSAIEAVVDRIGSEYHELSGRAK
description Cytoplasmic => ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI4
96) chain B
residue 69-94
type TOPO_DOM
sequence ELLNSAIEAVVDRIGSEYHELSGRAK
description Cytoplasmic => ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI4
97) chain C
residue 69-94
type TOPO_DOM
sequence ELLNSAIEAVVDRIGSEYHELSGRAK
description Cytoplasmic => ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI4
98) chain A
residue 95-118
type TRANSMEM
sequence DLGSAAVLIAIIDAVITWCILLWS
description Helical => ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI5
99) chain B
residue 95-118
type TRANSMEM
sequence DLGSAAVLIAIIDAVITWCILLWS
description Helical => ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI5
100) chain C
residue 95-118
type TRANSMEM
sequence DLGSAAVLIAIIDAVITWCILLWS
description Helical => ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI5
101) 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
102) 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
103) 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
104) 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
105) 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
106) 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
107) 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
108) 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
109) 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
110) 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
111) 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
112) chain A
residue 69-80
type prosite
sequence ELLNSAIEAVVD
description DAGK_PROKAR Prokaryotic diacylglycerol kinase signature. ElLNSAIEavVD
source prosite : PS01069
113) chain A
residue 16
type BINDING
sequence Y
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10
114) chain B
residue 94
type BINDING
sequence K
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10
115) chain C
residue 16
type BINDING
sequence Y
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10
116) chain C
residue 28
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10
117) chain C
residue 76
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10
118) chain C
residue 85
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10
119) chain C
residue 94
type BINDING
sequence K
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10
120) chain A
residue 28
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10
121) chain A
residue 76
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10
122) chain A
residue 85
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10
123) chain A
residue 94
type BINDING
sequence K
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10
124) chain B
residue 16
type BINDING
sequence Y
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10
125) chain B
residue 28
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10
126) chain B
residue 76
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10
127) chain B
residue 85
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10
128) 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
129) 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
130) 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
131) 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
132) 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
133) 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
134) 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
135) 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
136) 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
137) 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
138) 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
139) 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
140) chain A
residue 69
type ACT_SITE
sequence E
description Proton acceptor => ECO:0000305|PubMed:26673816
source Swiss-Prot : SWS_FT_FI7
141) chain B
residue 69
type ACT_SITE
sequence E
description Proton acceptor => ECO:0000305|PubMed:26673816
source Swiss-Prot : SWS_FT_FI7
142) chain C
residue 69
type ACT_SITE
sequence E
description Proton acceptor => ECO:0000305|PubMed:26673816
source Swiss-Prot : SWS_FT_FI7
143) 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
144) 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

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