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

click to enlarge
Title Structure of delta7-DgkA-syn in 7.9 MAG to 2.18 angstrom resolution
Classification TRANSFERASE
Compound DIACYLGLYCEROL KINASE-DELTA 7
Source (KDGL_ECOLI)
Sequence B:  AWINEAAFRQEGVAVLLCVVIAAWLDVDAVTRVLLISSVM
LVMIVELLNSAIEAVVDRIGSEYHELSGRAKDLGSAAVLI
AIIDAVITWAILLWSHF
Description


Functional site
1) chain B
residue 50
type
sequence V
description BINDING SITE FOR RESIDUE 79M B 1121
source : AC3
2) chain B
residue 52
type
sequence A
description BINDING SITE FOR RESIDUE 79M B 1121
source : AC3
3) chain B
residue 55
type
sequence R
description BINDING SITE FOR RESIDUE 79M B 1121
source : AC3
4) chain B
residue 26
type
sequence I
description BINDING SITE FOR RESIDUE 79N D 1123
source : AC4
5) chain B
residue 35
type
sequence G
description BINDING SITE FOR RESIDUE 79N D 1123
source : AC4
6) chain B
residue 38
type
sequence V
description BINDING SITE FOR RESIDUE 79N D 1123
source : AC4
7) chain B
residue 34
type
sequence E
description BINDING SITE FOR RESIDUE 79M B 1122
source : AC5
8) chain B
residue 41
type
sequence C
description BINDING SITE FOR RESIDUE 79M B 1122
source : AC5
9) chain B
residue 62
type
sequence V
description BINDING SITE FOR RESIDUE 79M B 1122
source : AC5
10) chain B
residue 65
type
sequence V
description BINDING SITE FOR RESIDUE 79M B 1122
source : AC5
11) chain B
residue 69
type
sequence E
description BINDING SITE FOR RESIDUE 79M B 1122
source : AC5
12) chain B
residue 108
type
sequence A
description BINDING SITE FOR RESIDUE 79M B 1122
source : AC5
13) chain B
residue 112
type
sequence W
description BINDING SITE FOR RESIDUE 79M B 1122
source : AC5
14) chain B
residue 116
type
sequence L
description BINDING SITE FOR RESIDUE 79M B 1122
source : AC5
15) chain B
residue 110
type
sequence I
description BINDING SITE FOR RESIDUE 79N A 1122
source : AC7
16) chain B
residue 49
type
sequence D
description BINDING SITE FOR RESIDUE 79M B 1123
source : AC8
17) chain B
residue 113
type
sequence A
description BINDING SITE FOR RESIDUE 79M A 1126
source : BC5
18) chain B
residue 114
type
sequence I
description BINDING SITE FOR RESIDUE 79M A 1126
source : BC5
19) chain B
residue 117
type
sequence W
description BINDING SITE FOR RESIDUE 79M A 1126
source : BC5
20) chain B
residue 118
type
sequence S
description BINDING SITE FOR RESIDUE 79M A 1126
source : BC5
21) chain B
residue 95-118
type TRANSMEM
sequence DLGSAAVLIAIIDAVITWAILLWS
description Helical => ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI5
22) chain B
residue 94
type BINDING
sequence K
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10
23) chain B
residue 28
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10
24) chain B
residue 76
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10
25) chain B
residue 85
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10
26) chain B
residue 31-47
type TRANSMEM
sequence FRQEGVAVLLCVVIAAW
description Helical => ECO:0000305|PubMed:12379131, ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI2
27) chain B
residue 51-68
type TRANSMEM
sequence DAVTRVLLISSVMLVMIV
description Helical => ECO:0000305|PubMed:12379131, ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI2
28) 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
29) chain B
residue 69-94
type TOPO_DOM
sequence ELLNSAIEAVVDRIGSEYHELSGRAK
description Cytoplasmic => ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI4
30) 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
31) 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
32) 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
33) 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
34) 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
35) 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
36) chain B
residue 69
type ACT_SITE
sequence E
description Proton acceptor => ECO:0000305|PubMed:26673816
source Swiss-Prot : SWS_FT_FI7

Display surface

Download
Links