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

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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 C:  GFLSGKRILVTGVASKLSIAYGIAQAMHREGAELAFTYQN
DKLKGRVEEFAAQLGSDIVLQCDVAEDASIDTMFAELGKV
WPKFDGFVHSIGFAPGDQLDGDYVNAVTREGFKIAHDISS
YSFVAMAKACRSMLNPGSALLTLSYLGAERAIPNYNVMGL
AKASLEANVRYMANAMGPEGVRVNAISAGPIRTLAASGIK
DFRKMLAHCEAVTPIRRTVTIEDVGNSAAFLCSDLSAGIS
GEVVHVDGGFSIAAMNE
Description


Functional site
1) chain C
residue 13
type
sequence G
description BINDING SITE FOR RESIDUE NAD C 503
source : AC5
2) chain C
residue 14
type
sequence V
description BINDING SITE FOR RESIDUE NAD C 503
source : AC5
3) chain C
residue 15
type
sequence A
description BINDING SITE FOR RESIDUE NAD C 503
source : AC5
4) chain C
residue 19
type
sequence S
description BINDING SITE FOR RESIDUE NAD C 503
source : AC5
5) chain C
residue 20
type
sequence I
description BINDING SITE FOR RESIDUE NAD C 503
source : AC5
6) chain C
residue 40
type
sequence Q
description BINDING SITE FOR RESIDUE NAD C 503
source : AC5
7) chain C
residue 44
type
sequence L
description BINDING SITE FOR RESIDUE NAD C 503
source : AC5
8) chain C
residue 63
type
sequence C
description BINDING SITE FOR RESIDUE NAD C 503
source : AC5
9) chain C
residue 64
type
sequence D
description BINDING SITE FOR RESIDUE NAD C 503
source : AC5
10) chain C
residue 65
type
sequence V
description BINDING SITE FOR RESIDUE NAD C 503
source : AC5
11) chain C
residue 91
type
sequence S
description BINDING SITE FOR RESIDUE NAD C 503
source : AC5
12) chain C
residue 92
type
sequence I
description BINDING SITE FOR RESIDUE NAD C 503
source : AC5
13) chain C
residue 93
type
sequence G
description BINDING SITE FOR RESIDUE NAD C 503
source : AC5
14) chain C
residue 144
type
sequence L
description BINDING SITE FOR RESIDUE NAD C 503
source : AC5
15) chain C
residue 145
type
sequence S
description BINDING SITE FOR RESIDUE NAD C 503
source : AC5
16) chain C
residue 163
type
sequence K
description BINDING SITE FOR RESIDUE NAD C 503
source : AC5
17) chain C
residue 189
type
sequence A
description BINDING SITE FOR RESIDUE NAD C 503
source : AC5
18) chain C
residue 190
type
sequence G
description BINDING SITE FOR RESIDUE NAD C 503
source : AC5
19) chain C
residue 191
type
sequence P
description BINDING SITE FOR RESIDUE NAD C 503
source : AC5
20) chain C
residue 192
type
sequence I
description BINDING SITE FOR RESIDUE NAD C 503
source : AC5
21) chain C
residue 194
type
sequence T
description BINDING SITE FOR RESIDUE NAD C 503
source : AC5
22) chain C
residue 196
type
sequence A
description BINDING SITE FOR RESIDUE NAD C 503
source : AC5
23) chain C
residue 93
type
sequence G
description BINDING SITE FOR RESIDUE TCL C 603
source : AC6
24) chain C
residue 95
type
sequence A
description BINDING SITE FOR RESIDUE TCL C 603
source : AC6
25) chain C
residue 100
type
sequence L
description BINDING SITE FOR RESIDUE TCL C 603
source : AC6
26) chain C
residue 146
type
sequence Y
description BINDING SITE FOR RESIDUE TCL C 603
source : AC6
27) chain C
residue 156
type
sequence Y
description BINDING SITE FOR RESIDUE TCL C 603
source : AC6
28) chain C
residue 196
type
sequence A
description BINDING SITE FOR RESIDUE TCL C 603
source : AC6
29) chain C
residue 200
type
sequence I
description BINDING SITE FOR RESIDUE TCL C 603
source : AC6
30) chain C
residue 157
type catalytic
sequence N
description 606
source MCSA : MCSA3
31) chain C
residue 164
type catalytic
sequence A
description 606
source MCSA : MCSA3
32) chain C
residue 147
type ACT_SITE
sequence L
description Proton acceptor => ECO:0000250
source Swiss-Prot : SWS_FT_FI1
33) chain C
residue 157
type ACT_SITE
sequence N
description Proton acceptor => ECO:0000250
source Swiss-Prot : SWS_FT_FI1
34) chain C
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 C
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 C
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 C
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 C
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 C
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 C
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 C
residue 96
type BINDING
sequence P
description
source Swiss-Prot : SWS_FT_FI3
42) chain C
residue 202
type SITE
sequence D
description Involved in acyl-ACP binding
source Swiss-Prot : SWS_FT_FI4
43) chain C
residue 205
type SITE
sequence K
description Involved in acyl-ACP binding
source Swiss-Prot : SWS_FT_FI4
44) chain C
residue 206
type SITE
sequence M
description Involved in acyl-ACP binding
source Swiss-Prot : SWS_FT_FI4

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