eF-site ID 1d8a-AB
PDB Code 1d8a
Chain A, B

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Title E. COLI ENOYL REDUCTASE/NAD+/TRICLOSAN COMPLEX
Classification OXIDOREDUCTASE
Compound ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE
Source ORGANISM_SCIENTIFIC: Escherichia coli;
Sequence A:  GFLSGKRILVTGVASKLSIAYGIAQAMHREGAELAFTYQN
DKLKGRVEEFAAQLGSDIVLQCDVAEDASIDTMFAELGKV
WPKFDGFVHSIGFAPGDQLDGDYVNAVTREGFKIAHDISS
YSFVAMAKACRSMLNPGSALLTLSYLGAERAIPNYNVMGL
AKASLEANVRYMANAMGPEGVRVNAISAGPIRTLAASGIK
DFRKMLAHCEAVTPIRRTVTIEDVGNSAAFLCSDLSAGIS
GEVVHVDGGFSIAAMNE
B:  GFLSGKRILVTGVASKLSIAYGIAQAMHREGAELAFTYQN
DKLKGRVEEFAAQLGSDIVLQCDVAEDASIDTMFAELGKV
WPKFDGFVHSIGFAPGDQLDGDYVNAVTREGFKIAHDISS
YSFVAMAKACRSMLNPGSALLTLSYLGAERAIPNYNVMGL
AKASLEANVRYMANAMGPEGVRVNAISAGPIRTLAASGIK
DFRKMLAHCEAVTPIRRTVTIEDVGNSAAFLCSDLSAGIS
GEVVHVDGGFSIAAMNE
Description


Functional site
1) chain A
residue 13
type
sequence G
description BINDING SITE FOR RESIDUE NAD A 501
source : AC1
2) chain A
residue 15
type
sequence A
description BINDING SITE FOR RESIDUE NAD A 501
source : AC1
3) chain A
residue 19
type
sequence S
description BINDING SITE FOR RESIDUE NAD A 501
source : AC1
4) chain A
residue 20
type
sequence I
description BINDING SITE FOR RESIDUE NAD A 501
source : AC1
5) chain A
residue 40
type
sequence Q
description BINDING SITE FOR RESIDUE NAD A 501
source : AC1
6) chain A
residue 64
type
sequence D
description BINDING SITE FOR RESIDUE NAD A 501
source : AC1
7) chain A
residue 65
type
sequence V
description BINDING SITE FOR RESIDUE NAD A 501
source : AC1
8) chain A
residue 91
type
sequence S
description BINDING SITE FOR RESIDUE NAD A 501
source : AC1
9) chain A
residue 92
type
sequence I
description BINDING SITE FOR RESIDUE NAD A 501
source : AC1
10) chain A
residue 119
type
sequence I
description BINDING SITE FOR RESIDUE NAD A 501
source : AC1
11) chain A
residue 144
type
sequence L
description BINDING SITE FOR RESIDUE NAD A 501
source : AC1
12) chain A
residue 145
type
sequence S
description BINDING SITE FOR RESIDUE NAD A 501
source : AC1
13) chain A
residue 146
type
sequence Y
description BINDING SITE FOR RESIDUE NAD A 501
source : AC1
14) chain A
residue 163
type
sequence K
description BINDING SITE FOR RESIDUE NAD A 501
source : AC1
15) chain A
residue 189
type
sequence A
description BINDING SITE FOR RESIDUE NAD A 501
source : AC1
16) chain A
residue 190
type
sequence G
description BINDING SITE FOR RESIDUE NAD A 501
source : AC1
17) chain A
residue 191
type
sequence P
description BINDING SITE FOR RESIDUE NAD A 501
source : AC1
18) chain A
residue 192
type
sequence I
description BINDING SITE FOR RESIDUE NAD A 501
source : AC1
19) chain A
residue 194
type
sequence T
description BINDING SITE FOR RESIDUE NAD A 501
source : AC1
20) chain A
residue 196
type
sequence A
description BINDING SITE FOR RESIDUE NAD A 501
source : AC1
21) chain B
residue 13
type
sequence G
description BINDING SITE FOR RESIDUE NAD B 503
source : AC2
22) chain B
residue 15
type
sequence A
description BINDING SITE FOR RESIDUE NAD B 503
source : AC2
23) chain B
residue 19
type
sequence S
description BINDING SITE FOR RESIDUE NAD B 503
source : AC2
24) chain B
residue 20
type
sequence I
description BINDING SITE FOR RESIDUE NAD B 503
source : AC2
25) chain B
residue 40
type
sequence Q
description BINDING SITE FOR RESIDUE NAD B 503
source : AC2
26) chain B
residue 44
type
sequence L
description BINDING SITE FOR RESIDUE NAD B 503
source : AC2
27) chain B
residue 63
type
sequence C
description BINDING SITE FOR RESIDUE NAD B 503
source : AC2
28) chain B
residue 64
type
sequence D
description BINDING SITE FOR RESIDUE NAD B 503
source : AC2
29) chain B
residue 65
type
sequence V
description BINDING SITE FOR RESIDUE NAD B 503
source : AC2
30) chain B
residue 91
type
sequence S
description BINDING SITE FOR RESIDUE NAD B 503
source : AC2
31) chain B
residue 92
type
sequence I
description BINDING SITE FOR RESIDUE NAD B 503
source : AC2
32) chain B
residue 144
type
sequence L
description BINDING SITE FOR RESIDUE NAD B 503
source : AC2
33) chain B
residue 145
type
sequence S
description BINDING SITE FOR RESIDUE NAD B 503
source : AC2
34) chain B
residue 163
type
sequence K
description BINDING SITE FOR RESIDUE NAD B 503
source : AC2
35) chain B
residue 189
type
sequence A
description BINDING SITE FOR RESIDUE NAD B 503
source : AC2
36) chain B
residue 190
type
sequence G
description BINDING SITE FOR RESIDUE NAD B 503
source : AC2
37) chain B
residue 191
type
sequence P
description BINDING SITE FOR RESIDUE NAD B 503
source : AC2
38) chain B
residue 192
type
sequence I
description BINDING SITE FOR RESIDUE NAD B 503
source : AC2
39) chain B
residue 194
type
sequence T
description BINDING SITE FOR RESIDUE NAD B 503
source : AC2
40) chain B
residue 196
type
sequence A
description BINDING SITE FOR RESIDUE NAD B 503
source : AC2
41) chain A
residue 93
type
sequence G
description BINDING SITE FOR RESIDUE TCL A 502
source : AC3
42) chain A
residue 94
type
sequence F
description BINDING SITE FOR RESIDUE TCL A 502
source : AC3
43) chain A
residue 95
type
sequence A
description BINDING SITE FOR RESIDUE TCL A 502
source : AC3
44) chain A
residue 100
type
sequence L
description BINDING SITE FOR RESIDUE TCL A 502
source : AC3
45) chain A
residue 146
type
sequence Y
description BINDING SITE FOR RESIDUE TCL A 502
source : AC3
46) chain A
residue 156
type
sequence Y
description BINDING SITE FOR RESIDUE TCL A 502
source : AC3
47) chain A
residue 196
type
sequence A
description BINDING SITE FOR RESIDUE TCL A 502
source : AC3
48) chain B
residue 93
type
sequence G
description BINDING SITE FOR RESIDUE TCL B 504
source : AC4
49) chain B
residue 95
type
sequence A
description BINDING SITE FOR RESIDUE TCL B 504
source : AC4
50) chain B
residue 156
type
sequence Y
description BINDING SITE FOR RESIDUE TCL B 504
source : AC4
51) chain B
residue 191
type
sequence P
description BINDING SITE FOR RESIDUE TCL B 504
source : AC4
52) chain B
residue 196
type
sequence A
description BINDING SITE FOR RESIDUE TCL B 504
source : AC4
53) chain B
residue 203
type
sequence F
description BINDING SITE FOR RESIDUE TCL B 504
source : AC4
54) chain A
residue 13
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:10201369, ECO:0000269|PubMed:10398587, ECO:0000269|PubMed:10493822, ECO:0000269|PubMed:10595560, ECO:0000269|PubMed:11514139, ECO:0000269|PubMed:12109908, ECO:0000269|PubMed:12699381, ECO:0000269|PubMed:8953047
source Swiss-Prot : SWS_FT_FI2
55) chain B
residue 40
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:10201369, ECO:0000269|PubMed:10398587, ECO:0000269|PubMed:10493822, ECO:0000269|PubMed:10595560, ECO:0000269|PubMed:11514139, ECO:0000269|PubMed:12109908, ECO:0000269|PubMed:12699381, ECO:0000269|PubMed:8953047
source Swiss-Prot : SWS_FT_FI2
56) chain B
residue 64
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:10201369, ECO:0000269|PubMed:10398587, ECO:0000269|PubMed:10493822, ECO:0000269|PubMed:10595560, ECO:0000269|PubMed:11514139, ECO:0000269|PubMed:12109908, ECO:0000269|PubMed:12699381, ECO:0000269|PubMed:8953047
source Swiss-Prot : SWS_FT_FI2
57) chain B
residue 92
type BINDING
sequence I
description BINDING => ECO:0000269|PubMed:10201369, ECO:0000269|PubMed:10398587, ECO:0000269|PubMed:10493822, ECO:0000269|PubMed:10595560, ECO:0000269|PubMed:11514139, ECO:0000269|PubMed:12109908, ECO:0000269|PubMed:12699381, ECO:0000269|PubMed:8953047
source Swiss-Prot : SWS_FT_FI2
58) chain B
residue 163
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:10201369, ECO:0000269|PubMed:10398587, ECO:0000269|PubMed:10493822, ECO:0000269|PubMed:10595560, ECO:0000269|PubMed:11514139, ECO:0000269|PubMed:12109908, ECO:0000269|PubMed:12699381, ECO:0000269|PubMed:8953047
source Swiss-Prot : SWS_FT_FI2
59) chain B
residue 192
type BINDING
sequence I
description BINDING => ECO:0000269|PubMed:10201369, ECO:0000269|PubMed:10398587, ECO:0000269|PubMed:10493822, ECO:0000269|PubMed:10595560, ECO:0000269|PubMed:11514139, ECO:0000269|PubMed:12109908, ECO:0000269|PubMed:12699381, ECO:0000269|PubMed:8953047
source Swiss-Prot : SWS_FT_FI2
60) chain A
residue 19
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:10201369, ECO:0000269|PubMed:10398587, ECO:0000269|PubMed:10493822, ECO:0000269|PubMed:10595560, ECO:0000269|PubMed:11514139, ECO:0000269|PubMed:12109908, ECO:0000269|PubMed:12699381, ECO:0000269|PubMed:8953047
source Swiss-Prot : SWS_FT_FI2
61) chain A
residue 40
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:10201369, ECO:0000269|PubMed:10398587, ECO:0000269|PubMed:10493822, ECO:0000269|PubMed:10595560, ECO:0000269|PubMed:11514139, ECO:0000269|PubMed:12109908, ECO:0000269|PubMed:12699381, ECO:0000269|PubMed:8953047
source Swiss-Prot : SWS_FT_FI2
62) chain A
residue 64
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:10201369, ECO:0000269|PubMed:10398587, ECO:0000269|PubMed:10493822, ECO:0000269|PubMed:10595560, ECO:0000269|PubMed:11514139, ECO:0000269|PubMed:12109908, ECO:0000269|PubMed:12699381, ECO:0000269|PubMed:8953047
source Swiss-Prot : SWS_FT_FI2
63) chain A
residue 92
type BINDING
sequence I
description BINDING => ECO:0000269|PubMed:10201369, ECO:0000269|PubMed:10398587, ECO:0000269|PubMed:10493822, ECO:0000269|PubMed:10595560, ECO:0000269|PubMed:11514139, ECO:0000269|PubMed:12109908, ECO:0000269|PubMed:12699381, ECO:0000269|PubMed:8953047
source Swiss-Prot : SWS_FT_FI2
64) chain A
residue 163
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:10201369, ECO:0000269|PubMed:10398587, ECO:0000269|PubMed:10493822, ECO:0000269|PubMed:10595560, ECO:0000269|PubMed:11514139, ECO:0000269|PubMed:12109908, ECO:0000269|PubMed:12699381, ECO:0000269|PubMed:8953047
source Swiss-Prot : SWS_FT_FI2
65) chain A
residue 192
type BINDING
sequence I
description BINDING => ECO:0000269|PubMed:10201369, ECO:0000269|PubMed:10398587, ECO:0000269|PubMed:10493822, ECO:0000269|PubMed:10595560, ECO:0000269|PubMed:11514139, ECO:0000269|PubMed:12109908, ECO:0000269|PubMed:12699381, ECO:0000269|PubMed:8953047
source Swiss-Prot : SWS_FT_FI2
66) chain B
residue 13
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:10201369, ECO:0000269|PubMed:10398587, ECO:0000269|PubMed:10493822, ECO:0000269|PubMed:10595560, ECO:0000269|PubMed:11514139, ECO:0000269|PubMed:12109908, ECO:0000269|PubMed:12699381, ECO:0000269|PubMed:8953047
source Swiss-Prot : SWS_FT_FI2
67) chain B
residue 19
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:10201369, ECO:0000269|PubMed:10398587, ECO:0000269|PubMed:10493822, ECO:0000269|PubMed:10595560, ECO:0000269|PubMed:11514139, ECO:0000269|PubMed:12109908, ECO:0000269|PubMed:12699381, ECO:0000269|PubMed:8953047
source Swiss-Prot : SWS_FT_FI2
68) chain A
residue 95
type BINDING
sequence A
description
source Swiss-Prot : SWS_FT_FI3
69) chain B
residue 95
type BINDING
sequence A
description
source Swiss-Prot : SWS_FT_FI3
70) chain A
residue 201
type SITE
sequence K
description Involved in acyl-ACP binding
source Swiss-Prot : SWS_FT_FI4
71) chain A
residue 204
type SITE
sequence R
description Involved in acyl-ACP binding
source Swiss-Prot : SWS_FT_FI4
72) chain A
residue 205
type SITE
sequence K
description Involved in acyl-ACP binding
source Swiss-Prot : SWS_FT_FI4
73) chain B
residue 201
type SITE
sequence K
description Involved in acyl-ACP binding
source Swiss-Prot : SWS_FT_FI4
74) chain B
residue 204
type SITE
sequence R
description Involved in acyl-ACP binding
source Swiss-Prot : SWS_FT_FI4
75) chain B
residue 205
type SITE
sequence K
description Involved in acyl-ACP binding
source Swiss-Prot : SWS_FT_FI4
76) chain A
residue 146
type ACT_SITE
sequence Y
description Proton acceptor => ECO:0000250
source Swiss-Prot : SWS_FT_FI1
77) chain A
residue 156
type ACT_SITE
sequence Y
description Proton acceptor => ECO:0000250
source Swiss-Prot : SWS_FT_FI1
78) chain B
residue 146
type ACT_SITE
sequence Y
description Proton acceptor => ECO:0000250
source Swiss-Prot : SWS_FT_FI1
79) chain B
residue 156
type ACT_SITE
sequence Y
description Proton acceptor => ECO:0000250
source Swiss-Prot : SWS_FT_FI1
80) chain A
residue 156
type catalytic
sequence Y
description 606
source MCSA : MCSA1
81) chain A
residue 163
type catalytic
sequence K
description 606
source MCSA : MCSA1
82) chain B
residue 156
type catalytic
sequence Y
description 606
source MCSA : MCSA2
83) chain B
residue 163
type catalytic
sequence K
description 606
source MCSA : MCSA2

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