eF-site ID 1qg6-A
PDB Code 1qg6
Chain A

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Title CRYSTAL STRUCTURE OF E. COLI ENOYL ACYL CARRIER PROTEIN REDUCTASE IN COMPLEX WITH NAD AND TRICLOSAN
Classification OXIDOREDUCTASE
Compound PROTEIN (ENOYL-[ACYL-CARRIER PROTEIN] REDUCTASE)
Source Escherichia coli (strain K12) (FABI_ECOLI)
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 14
type
sequence V
description BINDING SITE FOR RESIDUE NAD A 501
source : AC1
3) chain A
residue 15
type
sequence A
description BINDING SITE FOR RESIDUE NAD A 501
source : AC1
4) chain A
residue 19
type
sequence S
description BINDING SITE FOR RESIDUE NAD A 501
source : AC1
5) chain A
residue 20
type
sequence I
description BINDING SITE FOR RESIDUE NAD A 501
source : AC1
6) chain A
residue 40
type
sequence Q
description BINDING SITE FOR RESIDUE NAD A 501
source : AC1
7) chain A
residue 44
type
sequence L
description BINDING SITE FOR RESIDUE NAD A 501
source : AC1
8) chain A
residue 63
type
sequence C
description BINDING SITE FOR RESIDUE NAD A 501
source : AC1
9) chain A
residue 64
type
sequence D
description BINDING SITE FOR RESIDUE NAD A 501
source : AC1
10) chain A
residue 65
type
sequence V
description BINDING SITE FOR RESIDUE NAD A 501
source : AC1
11) chain A
residue 91
type
sequence S
description BINDING SITE FOR RESIDUE NAD A 501
source : AC1
12) chain A
residue 92
type
sequence I
description BINDING SITE FOR RESIDUE NAD A 501
source : AC1
13) chain A
residue 93
type
sequence G
description BINDING SITE FOR RESIDUE NAD A 501
source : AC1
14) chain A
residue 144
type
sequence L
description BINDING SITE FOR RESIDUE NAD A 501
source : AC1
15) chain A
residue 145
type
sequence S
description BINDING SITE FOR RESIDUE NAD A 501
source : AC1
16) chain A
residue 163
type
sequence K
description BINDING SITE FOR RESIDUE NAD A 501
source : AC1
17) chain A
residue 189
type
sequence A
description BINDING SITE FOR RESIDUE NAD A 501
source : AC1
18) chain A
residue 190
type
sequence G
description BINDING SITE FOR RESIDUE NAD A 501
source : AC1
19) chain A
residue 191
type
sequence P
description BINDING SITE FOR RESIDUE NAD A 501
source : AC1
20) chain A
residue 192
type
sequence I
description BINDING SITE FOR RESIDUE NAD A 501
source : AC1
21) chain A
residue 194
type
sequence T
description BINDING SITE FOR RESIDUE NAD A 501
source : AC1
22) chain A
residue 196
type
sequence A
description BINDING SITE FOR RESIDUE NAD A 501
source : AC1
23) chain A
residue 93
type
sequence G
description BINDING SITE FOR RESIDUE TCL A 601
source : AC2
24) chain A
residue 95
type
sequence A
description BINDING SITE FOR RESIDUE TCL A 601
source : AC2
25) chain A
residue 100
type
sequence L
description BINDING SITE FOR RESIDUE TCL A 601
source : AC2
26) chain A
residue 146
type
sequence Y
description BINDING SITE FOR RESIDUE TCL A 601
source : AC2
27) chain A
residue 156
type
sequence Y
description BINDING SITE FOR RESIDUE TCL A 601
source : AC2
28) chain A
residue 196
type
sequence A
description BINDING SITE FOR RESIDUE TCL A 601
source : AC2
29) chain A
residue 200
type
sequence I
description BINDING SITE FOR RESIDUE TCL A 601
source : AC2
30) chain A
residue 157
type catalytic
sequence N
description 606
source MCSA : MCSA1
31) chain A
residue 164
type catalytic
sequence A
description 606
source MCSA : MCSA1
32) chain A
residue 147
type ACT_SITE
sequence L
description Proton acceptor => ECO:0000250
source Swiss-Prot : SWS_FT_FI1
33) chain A
residue 157
type ACT_SITE
sequence N
description Proton acceptor => ECO:0000250
source Swiss-Prot : SWS_FT_FI1
34) chain A
residue 14
type BINDING
sequence V
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 20
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
36) chain A
residue 41
type BINDING
sequence N
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
37) chain A
residue 65
type BINDING
sequence V
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
38) chain A
residue 93
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
39) chain A
residue 164
type BINDING
sequence A
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
40) chain A
residue 193
type BINDING
sequence R
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
41) chain A
residue 96
type BINDING
sequence P
description
source Swiss-Prot : SWS_FT_FI3
42) chain A
residue 202
type SITE
sequence D
description Involved in acyl-ACP binding
source Swiss-Prot : SWS_FT_FI4
43) chain A
residue 205
type SITE
sequence K
description Involved in acyl-ACP binding
source Swiss-Prot : SWS_FT_FI4
44) chain A
residue 206
type SITE
sequence M
description Involved in acyl-ACP binding
source Swiss-Prot : SWS_FT_FI4

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