eF-site ID 1d8a-A
PDB Code 1d8a
Chain A

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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
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 A
residue 93
type
sequence G
description BINDING SITE FOR RESIDUE TCL A 502
source : AC3
22) chain A
residue 94
type
sequence F
description BINDING SITE FOR RESIDUE TCL A 502
source : AC3
23) chain A
residue 95
type
sequence A
description BINDING SITE FOR RESIDUE TCL A 502
source : AC3
24) chain A
residue 100
type
sequence L
description BINDING SITE FOR RESIDUE TCL A 502
source : AC3
25) chain A
residue 146
type
sequence Y
description BINDING SITE FOR RESIDUE TCL A 502
source : AC3
26) chain A
residue 156
type
sequence Y
description BINDING SITE FOR RESIDUE TCL A 502
source : AC3
27) chain A
residue 196
type
sequence A
description BINDING SITE FOR RESIDUE TCL A 502
source : AC3
28) 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
29) 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
30) 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
31) 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
32) 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
33) 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
34) 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
35) chain A
residue 95
type BINDING
sequence A
description
source Swiss-Prot : SWS_FT_FI3
36) chain A
residue 201
type SITE
sequence K
description Involved in acyl-ACP binding
source Swiss-Prot : SWS_FT_FI4
37) chain A
residue 204
type SITE
sequence R
description Involved in acyl-ACP binding
source Swiss-Prot : SWS_FT_FI4
38) chain A
residue 205
type SITE
sequence K
description Involved in acyl-ACP binding
source Swiss-Prot : SWS_FT_FI4
39) chain A
residue 146
type ACT_SITE
sequence Y
description Proton acceptor => ECO:0000250
source Swiss-Prot : SWS_FT_FI1
40) chain A
residue 156
type ACT_SITE
sequence Y
description Proton acceptor => ECO:0000250
source Swiss-Prot : SWS_FT_FI1
41) chain A
residue 156
type catalytic
sequence Y
description 606
source MCSA : MCSA1
42) chain A
residue 163
type catalytic
sequence K
description 606
source MCSA : MCSA1

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