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

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


Functional site
1) chain B
residue 13
type
sequence G
description BINDING SITE FOR RESIDUE NAD B 503
source : AC2
2) chain B
residue 15
type
sequence A
description BINDING SITE FOR RESIDUE NAD B 503
source : AC2
3) chain B
residue 19
type
sequence S
description BINDING SITE FOR RESIDUE NAD B 503
source : AC2
4) chain B
residue 20
type
sequence I
description BINDING SITE FOR RESIDUE NAD B 503
source : AC2
5) chain B
residue 40
type
sequence Q
description BINDING SITE FOR RESIDUE NAD B 503
source : AC2
6) chain B
residue 44
type
sequence L
description BINDING SITE FOR RESIDUE NAD B 503
source : AC2
7) chain B
residue 63
type
sequence C
description BINDING SITE FOR RESIDUE NAD B 503
source : AC2
8) chain B
residue 64
type
sequence D
description BINDING SITE FOR RESIDUE NAD B 503
source : AC2
9) chain B
residue 65
type
sequence V
description BINDING SITE FOR RESIDUE NAD B 503
source : AC2
10) chain B
residue 91
type
sequence S
description BINDING SITE FOR RESIDUE NAD B 503
source : AC2
11) chain B
residue 92
type
sequence I
description BINDING SITE FOR RESIDUE NAD B 503
source : AC2
12) chain B
residue 144
type
sequence L
description BINDING SITE FOR RESIDUE NAD B 503
source : AC2
13) chain B
residue 145
type
sequence S
description BINDING SITE FOR RESIDUE NAD B 503
source : AC2
14) chain B
residue 163
type
sequence K
description BINDING SITE FOR RESIDUE NAD B 503
source : AC2
15) chain B
residue 189
type
sequence A
description BINDING SITE FOR RESIDUE NAD B 503
source : AC2
16) chain B
residue 190
type
sequence G
description BINDING SITE FOR RESIDUE NAD B 503
source : AC2
17) chain B
residue 191
type
sequence P
description BINDING SITE FOR RESIDUE NAD B 503
source : AC2
18) chain B
residue 192
type
sequence I
description BINDING SITE FOR RESIDUE NAD B 503
source : AC2
19) chain B
residue 194
type
sequence T
description BINDING SITE FOR RESIDUE NAD B 503
source : AC2
20) chain B
residue 196
type
sequence A
description BINDING SITE FOR RESIDUE NAD B 503
source : AC2
21) chain B
residue 93
type
sequence G
description BINDING SITE FOR RESIDUE TCL B 504
source : AC4
22) chain B
residue 95
type
sequence A
description BINDING SITE FOR RESIDUE TCL B 504
source : AC4
23) chain B
residue 156
type
sequence Y
description BINDING SITE FOR RESIDUE TCL B 504
source : AC4
24) chain B
residue 191
type
sequence P
description BINDING SITE FOR RESIDUE TCL B 504
source : AC4
25) chain B
residue 196
type
sequence A
description BINDING SITE FOR RESIDUE TCL B 504
source : AC4
26) chain B
residue 203
type
sequence F
description BINDING SITE FOR RESIDUE TCL B 504
source : AC4
27) 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
28) 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
29) 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
30) 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
31) 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
32) 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
33) 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
34) chain B
residue 95
type BINDING
sequence A
description
source Swiss-Prot : SWS_FT_FI3
35) chain B
residue 201
type SITE
sequence K
description Involved in acyl-ACP binding
source Swiss-Prot : SWS_FT_FI4
36) chain B
residue 204
type SITE
sequence R
description Involved in acyl-ACP binding
source Swiss-Prot : SWS_FT_FI4
37) chain B
residue 205
type SITE
sequence K
description Involved in acyl-ACP binding
source Swiss-Prot : SWS_FT_FI4
38) chain B
residue 146
type ACT_SITE
sequence Y
description Proton acceptor => ECO:0000250
source Swiss-Prot : SWS_FT_FI1
39) chain B
residue 156
type ACT_SITE
sequence Y
description Proton acceptor => ECO:0000250
source Swiss-Prot : SWS_FT_FI1
40) chain B
residue 156
type catalytic
sequence Y
description 606
source MCSA : MCSA2
41) chain B
residue 163
type catalytic
sequence K
description 606
source MCSA : MCSA2

Display surface

Download
Links