Target Binding Site Detail

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Target General Information
Ligand General Information
Drug Binding Sites of Target
References
Target General Information  Top
Target ID T53588 Target Info
Target Name Bacterial NADH-dependent enoyl-ACP reductase (Bact fabI)
Synonyms Enoyl[acylcarrierprotein] reductase [NADH] FabI; ENR of Mycobacterium tuberculosis
Target Type Literature-reported Target
Gene Name Bact fabI
Biochemical Class Short-chain dehydrogenases reductase
UniProt ID
FABI_ECOLI
Ligand General Information  Top
Ligand Name Nicotinamide-Adenine-Dinucleotide Ligand Info
Canonical SMILES C1=CC(=C[N+](=C1)C2C(C(C(O2)COP(=O)([O-])OP(=O)(O)OCC3C(C(C(O3)N4C=NC5=C(N=CN=C54)N)O)O)O)O)C(=O)N
InChI 1S/C21H27N7O14P2/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(32)14(30)11(41-21)6-39-44(36,37)42-43(34,35)38-5-10-13(29)15(31)20(40-10)27-3-1-2-9(4-27)18(23)33/h1-4,7-8,10-11,13-16,20-21,29-32H,5-6H2,(H5-,22,23,24,25,33,34,35,36,37)/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1
InChIKey BAWFJGJZGIEFAR-NNYOXOHSSA-N
PubChem Compound ID 5892
Drug Binding Sites of Target  Top
PDB ID: 1C14      CRYSTAL STRUCTURE OF E COLI ENOYL REDUCTASE-NAD+-TRICLOSAN COMPLEX
Method X-ray diffraction Resolution 2.00 Å Mutation No [1]
PDB Sequence
GFLSGKRILV
11
TGVASKLSIA
21
YGIAQAMHRE
31
GAELAFTYQN
41
DKLKGRVEEF
51

AAQLGSDIVL
61
QCDVAEDASI
71
DTMFAELGKV
81
WPKFDGFVHS
91
IGFAPGDQLD
101

GDYVNAVTRE
111
GFKIAHDISS
121
YSFVAMAKAC
131
RSMLNPGSAL
141
LTLSYLGAER
151

AIPNYNVMGL
161
AKASLEANVR
171
YMANAMGPEG
181
VRVNAISAGP
191
IRTLAASGIK
201

DFRKMLAHCE
211
AVTPIRRTVT
221
IEDVGNSAAF
231
LCSDLSAGIS
241
GEVVHVDGGF
251

SIAAMN
Residue
Distance (Å)
GLY13
2.961
VAL14
3.669
ALA15
3.627
SER16
4.801
LEU18
4.892
SER19
2.551
ILE20
3.085
ALA21
4.719
GLN40
2.678
LEU44
3.503
CYS63
3.558
ASP64
2.942
VAL65
3.087
ALA66
4.368
SER91
3.178
ILE92
3.408
GLY93
3.418
Residue
Distance (Å)
PHE94
3.905
ILE119
3.647
LEU144
3.535
SER145
2.951
TYR146
3.882
TYR156
4.456
MET159
4.759
LYS163
2.991
ALA189
3.274
GLY190
3.592
PRO191
3.448
ILE192
2.820
THR194
2.549
LEU195
3.660
ALA196
3.202
ALA197
4.573
PHE203
4.108
PDB ID: 1MFP      E. coli Enoyl Reductase in complex with NAD and SB611113
Method X-ray diffraction Resolution 2.33 Å Mutation No [2]
PDB Sequence
GFLSGKRILV
11
TGVASKLSIA
21
YGIAQAMHRE
31
GAELAFTYQN
41
DKLKGRVEEF
51

AAQLGSDIVL
61
QCDVAEDASI
71
DTMFAELGKV
81
WPKFDGFVHS
91
IGFAPGDQLD
101

GDYVNAVTRE
111
GFKIAHDISS
121
YSFVAMAKAC
131
RSMLNPGSAL
141
LTLSYLGAER
151

AIPNYNVMGL
161
AKASLEANVR
171
YMANAMGPEG
181
VRVNAISAGP
191
IRTLAASGIK
201

DFRKMLAHCE
211
AVTPIRRTVT
221
IEDVGNSAAF
231
LCSDLSAGIS
241
GEVVHVDGGF
251

SIAAMNEL
Residue
Distance (Å)
GLY13
2.698
VAL14
3.873
ALA15
2.980
SER19
2.754
ILE20
3.099
ALA21
4.351
GLN40
3.218
LEU44
3.934
CYS63
3.381
ASP64
2.974
VAL65
3.063
ALA66
4.340
SER91
3.282
ILE92
3.139
GLY93
3.179
PHE94
4.356
Residue
Distance (Å)
ILE119
3.875
LEU144
3.320
SER145
3.078
TYR146
3.838
TYR156
4.335
MET159
4.555
LYS163
2.565
ALA189
3.416
GLY190
3.595
PRO191
3.729
ILE192
2.874
THR194
2.634
LEU195
3.802
ALA196
3.109
ALA197
4.671
PHE203
4.706
PDB ID: 1I30      E. Coli Enoyl Reductase +NAD+SB385826
Method X-ray diffraction Resolution 2.40 Å Mutation No [3]
PDB Sequence
GFLSGKRILV
11
TGVASKLSIA
21
YGIAQAMHRE
31
GAELAFTYQN
41
DKLKGRVEEF
51

AAQLGSDIVL
61
QCDVAEDASI
71
DTMFAELGKV
81
WPKFDGFVHS
91
IGFAPGDQLD
101

GDYVNAVTRE
111
GFKIAHDISS
121
YSFVAMAKAC
131
RSMLNPGSAL
141
LTLSYLGAER
151

AIPNYNVMGL
161
AKASLEANVR
171
YMANAMGPEG
181
VRVNAISAGP
191
IRTFRKMLAH
209

CEAVTPIRRT
219
VTIEDVGNSA
229
AFLCSDLSAG
239
ISGEVVHVDG
249
GFSIAAMN
Residue
Distance (Å)
GLY13
2.687
VAL14
4.058
ALA15
3.052
SER19
2.493
ILE20
3.162
ALA21
4.430
GLN40
3.182
LEU44
4.244
CYS63
3.330
ASP64
2.615
VAL65
2.849
ALA66
4.138
SER91
3.169
ILE92
2.962
GLY93
3.707
Residue
Distance (Å)
PHE94
4.531
ILE119
3.966
LEU144
3.387
SER145
3.124
TYR146
4.020
TYR156
4.373
MET159
4.635
LYS163
2.898
ALA189
3.389
GLY190
3.445
PRO191
3.496
ILE192
2.841
ARG193
4.967
THR194
2.520
PHE203
4.285
PDB ID: 1LX6      Crystal Structure of E. Coli Enoyl Reductase-NAD+ with a Bound Benzamide Inhibitor
Method X-ray diffraction Resolution 2.40 Å Mutation No [4]
PDB Sequence
GFLSGKRILV
11
TGVASKLSIA
21
YGIAQAMHRE
31
GAELAFTYQN
41
DKLKGRVEEF
51

AAQLGSDIVL
61
QCDVAEDASI
71
DTMFAELGKV
81
WPKFDGFVHS
91
IGFAPGDQLD
101

GDYVNAVTRE
111
GFKIAHDISS
121
YSFVAMAKAC
131
RSMLNPGSAL
141
LTLSYLGAER
151

AIPNYNVMGL
161
AKASLEANVR
171
YMANAMGPEG
181
VRVNAISAGP
191
IMLAHCEAVT
214

PIRRTVTIED
224
VGNSAAFLCS
234
DLSAGISGEV
244
VHVDGGFSIA
254
AMN
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAD or .NAD2 or .NAD3 or :3NAD;style chemicals stick;color identity;select .A:13 or .A:14 or .A:15 or .A:19 or .A:20 or .A:21 or .A:40 or .A:44 or .A:63 or .A:64 or .A:65 or .A:66 or .A:91 or .A:92 or .A:93 or .A:94 or .A:119 or .A:144 or .A:145 or .A:146 or .A:156 or .A:163 or .A:189 or .A:190 or .A:191 or .A:192; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY13
2.823
VAL14
4.051
ALA15
3.746
SER19
2.864
ILE20
3.116
ALA21
4.438
GLN40
3.109
LEU44
4.411
CYS63
3.522
ASP64
2.876
VAL65
3.146
ALA66
4.357
SER91
3.054
Residue
Distance (Å)
ILE92
3.084
GLY93
3.222
PHE94
4.322
ILE119
3.663
LEU144
3.449
SER145
2.903
TYR146
3.924
TYR156
4.387
LYS163
3.413
ALA189
3.506
GLY190
3.508
PRO191
3.399
ILE192
2.696
PDB ID: 1LXC      Crystal Structure of E. Coli Enoyl Reductase-NAD+ with a Bound Acrylamide Inhibitor
Method X-ray diffraction Resolution 2.40 Å Mutation No [4]
PDB Sequence
GFLSGKRILV
11
TGVASKLSIA
21
YGIAQAMHRE
31
GAELAFTYQN
41
DKLKGRVEEF
51

AAQLGSDIVL
61
QCDVAEDASI
71
DTMFAELGKV
81
WPKFDGFVHS
91
IGFAPGDQLD
101

GDYVNAVTRE
111
GFKIAHDISS
121
YSFVAMAKAC
131
RSMLNPGSAL
141
LTLSYLGAER
151

AIPNYNVMGL
161
AKASLEANVR
171
YMANAMGPEG
181
VRVNAISAGP
191
IRTLFRKMLA
208

HCEAVTPIRR
218
TVTIEDVGNS
228
AAFLCSDLSA
238
GISGEVVHVD
248
GGFSIAAMNE
258

L
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAD or .NAD2 or .NAD3 or :3NAD;style chemicals stick;color identity;select .A:13 or .A:14 or .A:15 or .A:16 or .A:18 or .A:19 or .A:20 or .A:21 or .A:40 or .A:44 or .A:63 or .A:64 or .A:65 or .A:66 or .A:91 or .A:92 or .A:93 or .A:94 or .A:119 or .A:144 or .A:145 or .A:146 or .A:156 or .A:159 or .A:163 or .A:189 or .A:190 or .A:191 or .A:192 or .A:194 or .A:195 or .A:203; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY13
2.729
VAL14
3.727
ALA15
3.055
SER16
4.825
LEU18
4.951
SER19
2.602
ILE20
3.004
ALA21
4.402
GLN40
3.502
LEU44
4.535
CYS63
3.513
ASP64
3.321
VAL65
3.263
ALA66
4.448
SER91
3.008
ILE92
3.188
Residue
Distance (Å)
GLY93
3.286
PHE94
4.344
ILE119
4.026
LEU144
3.320
SER145
3.133
TYR146
4.134
TYR156
4.503
MET159
4.896
LYS163
2.928
ALA189
3.462
GLY190
3.582
PRO191
3.767
ILE192
3.063
THR194
2.696
LEU195
4.026
PHE203
4.092
PDB ID: 1I2Z      E. COLI ENOYL REDUCTASE IN COMPLEX WITH NAD AND BRL-12654
Method X-ray diffraction Resolution 2.80 Å Mutation No [5]
PDB Sequence
GFLSGKRILV
11
TGVASKLSIA
21
YGIAQAMHRE
31
GAELAFTYQN
41
DKLKGRVEEF
51

AAQLGSDIVL
61
QCDVAEDASI
71
DTMFAELGKV
81
WPKFDGFVHS
91
IGFAPGDQLD
101

GDYVNAVTRE
111
GFKIAHDISS
121
YSFVAMAKAC
131
RSMLNPGSAL
141
LTLSYLGAER
151

AIPNYNVMGL
161
AKASLEANVR
171
YMANAMGPEG
181
VRVNAISAGP
191
IRTLAASGIK
201

DFRKMLAHCE
211
AVTPIRRTVT
221
IEDVGNSAAF
231
LCSDLSAGIS
241
GEVVHVDGGF
251

SIAAMNE
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAD or .NAD2 or .NAD3 or :3NAD;style chemicals stick;color identity;select .A:13 or .A:14 or .A:15 or .A:19 or .A:20 or .A:21 or .A:40 or .A:44 or .A:63 or .A:64 or .A:65 or .A:66 or .A:91 or .A:92 or .A:93 or .A:94 or .A:119 or .A:144 or .A:145 or .A:146 or .A:156 or .A:163 or .A:189 or .A:190 or .A:191 or .A:192 or .A:194 or .A:195 or .A:196; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY13
2.747
VAL14
4.215
ALA15
3.403
SER19
2.556
ILE20
3.039
ALA21
4.175
GLN40
3.124
LEU44
4.086
CYS63
3.440
ASP64
2.736
VAL65
3.039
ALA66
4.290
SER91
2.949
ILE92
2.993
GLY93
3.459
Residue
Distance (Å)
PHE94
4.269
ILE119
3.817
LEU144
3.318
SER145
2.923
TYR146
3.534
TYR156
4.219
LYS163
3.003
ALA189
3.365
GLY190
3.471
PRO191
3.209
ILE192
2.672
THR194
2.857
LEU195
3.216
ALA196
4.132
PDB ID: 1QG6      CRYSTAL STRUCTURE OF E. COLI ENOYL ACYL CARRIER PROTEIN REDUCTASE IN COMPLEX WITH NAD AND TRICLOSAN
Method X-ray diffraction Resolution 1.90 Å Mutation No [6]
PDB Sequence
GFLSGKRILV
11
TGVASKLSIA
21
YGIAQAMHRE
31
GAELAFTYQN
41
DKLKGRVEEF
51

AAQLGSDIVL
61
QCDVAEDASI
71
DTMFAELGKV
81
WPKFDGFVHS
91
IGFAPGDQLD
101

GDYVNAVTRE
111
GFKIAHDISS
121
YSFVAMAKAC
131
RSMLNPGSAL
141
LTLSYLGAER
151

AIPNYNVMGL
161
AKASLEANVR
171
YMANAMGPEG
181
VRVNAISAGP
191
IRTLAASGIK
201

DFRKMLAHCE
211
AVTPIRRTVT
221
IEDVGNSAAF
231
LCSDLSAGIS
241
GEVVHVDGGF
251

SIAAMNE
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAD or .NAD2 or .NAD3 or :3NAD;style chemicals stick;color identity;select .A:13 or .A:14 or .A:15 or .A:18 or .A:19 or .A:20 or .A:21 or .A:40 or .A:44 or .A:63 or .A:64 or .A:65 or .A:66 or .A:91 or .A:92 or .A:93 or .A:94 or .A:119 or .A:144 or .A:145 or .A:146 or .A:156 or .A:159 or .A:163 or .A:189 or .A:190 or .A:191 or .A:192 or .A:194 or .A:195 or .A:196 or .A:197 or .A:203; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY13
2.675
VAL14
3.681
ALA15
3.354
LEU18
4.971
SER19
2.517
ILE20
2.979
ALA21
4.438
GLN40
2.868
LEU44
3.529
CYS63
3.480
ASP64
3.059
VAL65
3.108
ALA66
4.074
SER91
3.074
ILE92
3.401
GLY93
3.474
PHE94
4.002
Residue
Distance (Å)
ILE119
3.897
LEU144
3.506
SER145
3.076
TYR146
3.718
TYR156
4.379
MET159
4.213
LYS163
2.810
ALA189
3.503
GLY190
3.602
PRO191
3.254
ILE192
2.614
THR194
2.670
LEU195
3.775
ALA196
3.053
ALA197
4.314
PHE203
4.227
PDB ID: 1DFI      X-RAY STRUCTURE OF ESCHERICHIA COLI ENOYL REDUCTASE WITH BOUND NAD
Method X-ray diffraction Resolution 2.09 Å Mutation No [7]
PDB Sequence
GFLSGKRILV
11
TGVASKLSIA
21
YGIAQAMHRE
31
GAELAFTYQN
41
DKLKGRVEEF
51

AAQLGSDIVL
61
QCDVAEDASI
71
DTMFAELGKV
81
WPKFDGFVHS
91
IGFAPGDQLD
101

GDYVNAVTRE
111
GFKIAHDISS
121
YSFVAMAKAC
131
RSMLNPGSAL
141
LTLSYLGAER
151

AIPNYNVMGL
161
AKASLEANVR
171
YMANAMGPEG
181
VRVNAISAGP
191
IRTLMLAHCE
211

AVTPIRRTVT
221
IEDVGNSAAF
231
LCSDLSAGIS
241
GEVVHVDGGF
251
SIAAMNE
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAD or .NAD2 or .NAD3 or :3NAD;style chemicals stick;color identity;select .A:13 or .A:14 or .A:15 or .A:19 or .A:20 or .A:21 or .A:40 or .A:44 or .A:63 or .A:64 or .A:65 or .A:66 or .A:90 or .A:91 or .A:92 or .A:93 or .A:94 or .A:119 or .A:144 or .A:145 or .A:146 or .A:156 or .A:163 or .A:189 or .A:190 or .A:191 or .A:192 or .A:195; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY13
2.544
VAL14
3.692
ALA15
3.548
SER19
3.481
ILE20
2.955
ALA21
4.877
GLN40
3.169
LEU44
4.466
CYS63
3.133
ASP64
2.904
VAL65
3.059
ALA66
3.969
HIS90
4.944
SER91
3.394
Residue
Distance (Å)
ILE92
3.392
GLY93
3.853
PHE94
4.283
ILE119
3.964
LEU144
3.486
SER145
2.816
TYR146
3.781
TYR156
4.382
LYS163
2.434
ALA189
3.308
GLY190
3.828
PRO191
3.872
ILE192
3.515
LEU195
2.757
PDB ID: 1D8A      E. COLI ENOYL REDUCTASE/NAD+/TRICLOSAN COMPLEX
Method X-ray diffraction Resolution 2.20 Å Mutation No [8]
PDB Sequence
GFLSGKRILV
11
TGVASKLSIA
21
YGIAQAMHRE
31
GAELAFTYQN
41
DKLKGRVEEF
51

AAQLGSDIVL
61
QCDVAEDASI
71
DTMFAELGKV
81
WPKFDGFVHS
91
IGFAPGDQLD
101

GDYVNAVTRE
111
GFKIAHDISS
121
YSFVAMAKAC
131
RSMLNPGSAL
141
LTLSYLGAER
151

AIPNYNVMGL
161
AKASLEANVR
171
YMANAMGPEG
181
VRVNAISAGP
191
IRTLAASGIK
201

DFRKMLAHCE
211
AVTPIRRTVT
221
IEDVGNSAAF
231
LCSDLSAGIS
241
GEVVHVDGGF
251

SIAAMNE
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAD or .NAD2 or .NAD3 or :3NAD;style chemicals stick;color identity;select .A:13 or .A:14 or .A:15 or .A:19 or .A:20 or .A:21 or .A:40 or .A:44 or .A:63 or .A:64 or .A:65 or .A:66 or .A:91 or .A:92 or .A:93 or .A:94 or .A:119 or .A:144 or .A:145 or .A:146 or .A:156 or .A:159 or .A:163 or .A:189 or .A:190 or .A:191 or .A:192 or .A:194 or .A:195 or .A:196 or .A:197 or .A:203; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY13
2.742
VAL14
3.865
ALA15
3.174
SER19
2.780
ILE20
3.120
ALA21
4.539
GLN40
2.850
LEU44
4.189
CYS63
3.827
ASP64
3.482
VAL65
3.304
ALA66
3.920
SER91
2.878
ILE92
3.537
GLY93
4.050
PHE94
4.087
Residue
Distance (Å)
ILE119
3.699
LEU144
3.286
SER145
2.874
TYR146
3.696
TYR156
4.257
MET159
4.453
LYS163
3.003
ALA189
3.142
GLY190
3.092
PRO191
3.128
ILE192
2.541
THR194
3.059
LEU195
4.220
ALA196
3.386
ALA197
4.509
PHE203
4.426
PDB ID: 1DFH      X-RAY STRUCTURE OF ESCHERICHIA COLI ENOYL REDUCTASE WITH BOUND NAD AND THIENO-DIAZABORINE
Method X-ray diffraction Resolution 2.20 Å Mutation No [7]
PDB Sequence
GFLSGKRILV
11
TGVASKLSIA
21
YGIAQAMHRE
31
GAELAFTYQN
41
DKLKGRVEEF
51

AAQLGSDIVL
61
QCDVAEDASI
71
DTMFAELGKV
81
WPKFDGFVHS
91
IGFAPGDQLD
101

GDYVNAVTRE
111
GFKIAHDISS
121
YSFVAMAKAC
131
RSMLNPGSAL
141
LTLSYLGAER
151

AIPNYNVMGL
161
AKASLEANVR
171
YMANAMGPEG
181
VRVNAISAGP
191
IRTLAASGIK
201

DFRKMLAHCE
211
AVTPIRRTVT
221
IEDVGNSAAF
231
LCSDLSAGIS
241
GEVVHVDGGF
251

SIAAMNE
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAD or .NAD2 or .NAD3 or :3NAD;style chemicals stick;color identity;select .A:13 or .A:14 or .A:15 or .A:18 or .A:19 or .A:20 or .A:21 or .A:40 or .A:44 or .A:63 or .A:64 or .A:65 or .A:66 or .A:91 or .A:92 or .A:93 or .A:94 or .A:119 or .A:144 or .A:145 or .A:146 or .A:156 or .A:163 or .A:189 or .A:190 or .A:191 or .A:192 or .A:203; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY13
2.873
VAL14
3.778
ALA15
3.326
LEU18
4.981
SER19
2.730
ILE20
2.804
ALA21
4.424
GLN40
2.805
LEU44
3.706
CYS63
3.403
ASP64
2.997
VAL65
3.117
ALA66
4.163
SER91
3.066
Residue
Distance (Å)
ILE92
3.585
GLY93
3.392
PHE94
4.266
ILE119
3.990
LEU144
3.422
SER145
2.916
TYR146
3.802
TYR156
4.317
LYS163
2.905
ALA189
3.119
GLY190
3.294
PRO191
3.260
ILE192
2.694
PHE203
3.914
PDB ID: 1DFG      X-RAY STRUCTURE OF ESCHERICHIA COLI ENOYL REDUCTASE WITH BOUND NAD AND BENZO-DIAZABORINE
Method X-ray diffraction Resolution 2.50 Å Mutation No [7]
PDB Sequence
GFLSGKRILV
11
TGVASKLSIA
21
YGIAQAMHRE
31
GAELAFTYQN
41
DKLKGRVEEF
51

AAQLGSDIVL
61
QCDVAEDASI
71
DTMFAELGKV
81
WPKFDGFVHS
91
IGFAPGDQLD
101

GDYVNAVTRE
111
GFKIAHDISS
121
YSFVAMAKAC
131
RSMLNPGSAL
141
LTLSYLGAER
151

AIPNYNVMGL
161
AKASLEANVR
171
YMANAMGPEG
181
VRVNAISAGP
191
IRTLAASGIK
201

DFRKMLAHCE
211
AVTPIRRTVT
221
IEDVGNSAAF
231
LCSDLSAGIS
241
GEVVHVDGGF
251

SIAAMNE
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAD or .NAD2 or .NAD3 or :3NAD;style chemicals stick;color identity;select .A:13 or .A:14 or .A:15 or .A:19 or .A:20 or .A:21 or .A:40 or .A:44 or .A:63 or .A:64 or .A:65 or .A:66 or .A:91 or .A:92 or .A:93 or .A:94 or .A:119 or .A:144 or .A:145 or .A:146 or .A:156 or .A:163 or .A:189 or .A:190 or .A:191 or .A:192 or .A:203; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY13
2.833
VAL14
3.873
ALA15
3.452
SER19
2.321
ILE20
2.979
ALA21
4.421
GLN40
2.787
LEU44
3.944
CYS63
3.220
ASP64
2.667
VAL65
3.031
ALA66
3.941
SER91
3.122
ILE92
3.647
Residue
Distance (Å)
GLY93
3.775
PHE94
4.046
ILE119
3.913
LEU144
3.813
SER145
2.921
TYR146
3.845
TYR156
4.298
LYS163
2.955
ALA189
3.306
GLY190
3.110
PRO191
3.168
ILE192
2.700
PHE203
4.298
PDB ID: 1QSG      CRYSTAL STRUCTURE OF ENOYL REDUCTASE INHIBITION BY TRICLOSAN
Method X-ray diffraction Resolution 1.75 Å Mutation No [9]
PDB Sequence
GFLSGKRILV
11
TGVASKLSIA
21
YGIAQAMHRE
31
GAELAFTYQN
41
DKLKGRVEEF
51

AAQLGSDIVL
61
QCDVAEDASI
71
DTMFAELGKV
81
WPKFDGFVHS
91
IGFAPGDQLD
101

GDYVNAVTRE
111
GFKIAHDISS
121
YSFVAMAKAC
131
RSMLNPGSAL
141
LTLSYLGAER
151

AIPNYNVMGL
161
AKASLEANVR
171
YMANAMGPEG
181
VRVNAISAGP
191
IRTLAASGIK
201

DFRKMLAHCE
211
AVTPIRRTVT
221
IEDVGNSAAF
231
LCSDLSAGIS
241
GEVVHVDGGF
251

SIAAMNEL
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAD or .NAD2 or .NAD3 or :3NAD;style chemicals stick;color identity;select .A:13 or .A:14 or .A:15 or .A:16 or .A:19 or .A:20 or .A:21 or .A:40 or .A:44 or .A:63 or .A:64 or .A:65 or .A:66 or .A:91 or .A:92 or .A:93 or .A:94 or .A:119 or .A:144 or .A:145 or .A:146 or .A:156 or .A:159 or .A:163 or .A:189 or .A:190 or .A:191 or .A:192 or .A:194 or .A:195 or .A:196 or .A:197 or .A:203; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY13
2.861
VAL14
3.875
ALA15
3.400
SER16
4.976
SER19
2.608
ILE20
2.975
ALA21
4.593
GLN40
2.785
LEU44
3.863
CYS63
3.589
ASP64
2.994
VAL65
3.152
ALA66
4.066
SER91
3.240
ILE92
3.388
GLY93
3.626
PHE94
4.175
Residue
Distance (Å)
ILE119
3.884
LEU144
3.568
SER145
3.168
TYR146
3.761
TYR156
4.526
MET159
4.558
LYS163
3.014
ALA189
3.495
GLY190
3.659
PRO191
3.362
ILE192
2.819
THR194
2.762
LEU195
3.760
ALA196
3.031
ALA197
4.193
PHE203
4.412
PDB ID: 3PJF      Structure of ENR G93V mutant-NAD+-triclosan complex
Method X-ray diffraction Resolution 1.90 Å Mutation Yes [10]
PDB Sequence
GFLSGKRILV
11
TGVASKLSIA
21
YGIAQAMHRE
31
GAELAFTYQN
41
DKLKGRVEEF
51

AAQLGSDIVL
61
QCDVAEDASI
71
DTMFAELGKV
81
WPKFDGFVHS
91
IVFAPGDQLD
101

GDYVNAVTRE
111
GFKIAHDISS
121
YSFVAMAKAC
131
RSMLNPGSAL
141
LTLSYLGAER
151

AIPNYNVMGL
161
AKASLEANVR
171
YMANAMGPEG
181
VRVNAISAGP
191
IRTKMLAHCE
211

AVTPIRRTVT
221
IEDVGNSAAF
231
LCSDLSAGIS
241
GEVVHVDGGF
251
SIAAMNE
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAD or .NAD2 or .NAD3 or :3NAD;style chemicals stick;color identity;select .A:13 or .A:14 or .A:15 or .A:16 or .A:18 or .A:19 or .A:20 or .A:21 or .A:40 or .A:44 or .A:63 or .A:64 or .A:65 or .A:66 or .A:91 or .A:92 or .A:93 or .A:94 or .A:119 or .A:144 or .A:145 or .A:146 or .A:156 or .A:163 or .A:189 or .A:190 or .A:191 or .A:192 or .A:205; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY13
2.877
VAL14
3.839
ALA15
3.414
SER16
4.692
LEU18
4.583
SER19
2.615
ILE20
2.785
ALA21
4.381
GLN40
2.616
LEU44
3.653
CYS63
3.240
ASP64
2.803
VAL65
3.047
ALA66
4.079
SER91
3.115
Residue
Distance (Å)
ILE92
3.537
VAL93
3.374
PHE94
4.062
ILE119
3.756
LEU144
3.202
SER145
3.168
TYR146
3.725
TYR156
4.538
LYS163
2.929
ALA189
3.296
GLY190
3.609
PRO191
3.360
ILE192
2.803
LYS205
4.949
PDB ID: 3PJD      Structure of ENR G93A mutant-NAD+-Triclosan complex
Method X-ray diffraction Resolution 2.50 Å Mutation Yes [10]
PDB Sequence
GFLSGKRILV
11
TGVASKLSIA
21
YGIAQAMHRE
31
GAELAFTYQN
41
DKLKGRVEEF
51

AAQLGSDIVL
61
QCDVAEDASI
71
DTMFAELGKV
81
WPKFDGFVHS
91
IAFAPGDQLD
101

GDYVNAVTRE
111
GFKIAHDISS
121
YSFVAMAKAC
131
RSMLNPGSAL
141
LTLSYLGAER
151

AIPNYNVMGL
161
AKASLEANVR
171
YMANAMGPEG
181
VRVNAISAGP
191
IRTLAASGIK
201

DFRKMLAHCE
211
AVTPIRRTVT
221
IEDVGNSAAF
231
LCSDLSAGIS
241
GEVVHVDGGF
251

SIAAMNE
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAD or .NAD2 or .NAD3 or :3NAD;style chemicals stick;color identity;select .A:13 or .A:14 or .A:15 or .A:18 or .A:19 or .A:20 or .A:21 or .A:40 or .A:44 or .A:63 or .A:64 or .A:65 or .A:66 or .A:91 or .A:92 or .A:93 or .A:94 or .A:119 or .A:144 or .A:145 or .A:146 or .A:156 or .A:159 or .A:163 or .A:189 or .A:190 or .A:191 or .A:192 or .A:194 or .A:195 or .A:196 or .A:197 or .A:203; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY13
2.734
VAL14
3.800
ALA15
3.800
LEU18
4.776
SER19
2.530
ILE20
2.941
ALA21
4.417
GLN40
3.243
LEU44
4.172
CYS63
3.323
ASP64
2.795
VAL65
3.288
ALA66
4.320
SER91
3.320
ILE92
3.566
ALA93
3.584
PHE94
4.181
Residue
Distance (Å)
ILE119
3.933
LEU144
3.586
SER145
2.984
TYR146
3.880
TYR156
4.625
MET159
4.363
LYS163
2.891
ALA189
3.301
GLY190
3.458
PRO191
3.396
ILE192
2.735
THR194
2.773
LEU195
3.752
ALA196
3.181
ALA197
4.299
PHE203
4.378
PDB ID: 3PJE      Structure of ENR G93S mutant-NAD+-triclosan complex
Method X-ray diffraction Resolution 2.50 Å Mutation Yes [10]
PDB Sequence
GFLSGKRILV
11
TGVASKLSIA
21
YGIAQAMHRE
31
GAELAFTYQN
41
DKLKGRVEEF
51

AAQLGSDIVL
61
QCDVAEDASI
71
DTMFAELGKV
81
WPKFDGFVHS
91
ISFAPGDQLD
101

GDYVNAVTRE
111
GFKIAHDISS
121
YSFVAMAKAC
131
RSMLNPGSAL
141
LTLSYLGAER
151

AIPNYNVMGL
161
AKASLEANVR
171
YMANAMGPEG
181
VRVNAISAGP
191
IRTLAASGIK
201

DFRKMLAHCE
211
AVTPIRRTVT
221
IEDVGNSAAF
231
LCSDLSAGIS
241
GEVVHVDGGF
251

SIAAMNE
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAD or .NAD2 or .NAD3 or :3NAD;style chemicals stick;color identity;select .A:13 or .A:14 or .A:15 or .A:16 or .A:18 or .A:19 or .A:20 or .A:21 or .A:40 or .A:44 or .A:63 or .A:64 or .A:65 or .A:66 or .A:91 or .A:92 or .A:93 or .A:94 or .A:119 or .A:144 or .A:145 or .A:146 or .A:156 or .A:159 or .A:163 or .A:189 or .A:190 or .A:191 or .A:192 or .A:194 or .A:195 or .A:196 or .A:197 or .A:203; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY13
2.684
VAL14
4.042
ALA15
3.453
SER16
4.960
LEU18
4.736
SER19
2.638
ILE20
3.015
ALA21
4.365
GLN40
2.788
LEU44
4.127
CYS63
3.479
ASP64
3.020
VAL65
3.318
ALA66
4.209
SER91
3.213
ILE92
3.484
SER93
3.037
Residue
Distance (Å)
PHE94
4.169
ILE119
3.896
LEU144
3.492
SER145
2.969
TYR146
3.757
TYR156
4.719
MET159
4.473
LYS163
3.028
ALA189
3.488
GLY190
3.395
PRO191
3.368
ILE192
2.794
THR194
2.692
LEU195
3.638
ALA196
3.188
ALA197
4.257
PHE203
4.308
PDB ID: 4JQC      Crystal Structure of E.coli Enoyl Reductase in Complex with NAD and AFN-1252
Method X-ray diffraction Resolution 2.80 Å Mutation No [11]
PDB Sequence
MGFLSGKRIL
10
VTGVASKLSI
20
AYGIAQAMHR
30
EGAELAFTYQ
40
NDKLKGRVEE
50

FAAQLGSDIV
60
LQCDVAEDAS
70
IDTMFAELGK
80
VWPKFDGFVH
90
SIGFAPGDQL
100

DGDYVNAVTR
110
EGFKIAHDIS
120
SYSFVAMAKA
130
CRSMLNPGSA
140
LLTLSYLGAE
150

RAIPNYNVMG
160
LAKASLEANV
170
RYMANAMGPE
180
GVRVNAISAG
190
PIRTLAASGI
200

KDFRKMLAHC
210
EAVTPIRRTV
220
TIEDVGNSAA
230
FLCSDLSAGI
240
SGEVVHVDGG
250

FSIAAMNE
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAD or .NAD2 or .NAD3 or :3NAD;style chemicals stick;color identity;select .A:13 or .A:14 or .A:15 or .A:19 or .A:20 or .A:40 or .A:44 or .A:63 or .A:64 or .A:65 or .A:66 or .A:90 or .A:91 or .A:92 or .A:93 or .A:94 or .A:119 or .A:144 or .A:145 or .A:146 or .A:156 or .A:163 or .A:189 or .A:190 or .A:191 or .A:192 or .A:194 or .A:195 or .A:196 or .A:203; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY13
2.600
VAL14
3.713
ALA15
3.241
SER19
3.948
ILE20
2.986
GLN40
3.046
LEU44
3.629
CYS63
3.515
ASP64
3.405
VAL65
3.138
ALA66
4.212
HIS90
4.921
SER91
3.125
ILE92
3.193
GLY93
3.610
Residue
Distance (Å)
PHE94
4.234
ILE119
3.358
LEU144
3.427
SER145
3.169
TYR146
4.128
TYR156
4.800
LYS163
2.682
ALA189
3.362
GLY190
3.516
PRO191
3.883
ILE192
3.181
THR194
2.345
LEU195
3.226
ALA196
3.051
PHE203
4.828
PDB ID: 4JX8      Crystal Structure of E.coli Enoyl Reductase in Complex with NAD and AEA16
Method X-ray diffraction Resolution 3.20 Å Mutation No [12]
PDB Sequence
MGFLSGKRIL
10
VTGVASKLSI
20
AYGIAQAMHR
30
EGAELAFTYQ
40
NDKLKGRVEE
50

FAAQLGSDIV
60
LQCDVAEDAS
70
IDTMFAELGK
80
VWPKFDGFVH
90
SIGFAPGDQL
100

DGDYVNAVTR
110
EGFKIAHDIS
120
SYSFVAMAKA
130
CRSMLNPGSA
140
LLTLSYLGAE
150

RAIPNYNVMG
160
LAKASLEANV
170
RYMANAMGPE
180
GVRVNAISAG
190
PIRTLAASGI
200

KDFRKMLAHC
210
EAVTPIRRTV
220
TIEDVGNSAA
230
FLCSDLSAGI
240
SGEVVHVDGG
250

FSIAAMNE
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAD or .NAD2 or .NAD3 or :3NAD;style chemicals stick;color identity;select .A:13 or .A:14 or .A:15 or .A:19 or .A:20 or .A:40 or .A:44 or .A:63 or .A:64 or .A:65 or .A:66 or .A:90 or .A:91 or .A:92 or .A:93 or .A:94 or .A:119 or .A:144 or .A:145 or .A:146 or .A:156 or .A:159 or .A:163 or .A:189 or .A:190 or .A:191 or .A:192 or .A:193 or .A:194 or .A:195 or .A:196; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY13
3.076
VAL14
3.617
ALA15
3.426
SER19
3.640
ILE20
2.960
GLN40
3.385
LEU44
4.886
CYS63
3.419
ASP64
2.688
VAL65
3.167
ALA66
4.091
HIS90
4.797
SER91
2.961
ILE92
2.983
GLY93
3.566
PHE94
4.094
Residue
Distance (Å)
ILE119
3.847
LEU144
3.361
SER145
3.203
TYR146
3.651
TYR156
4.404
MET159
3.936
LYS163
2.984
ALA189
3.607
GLY190
3.726
PRO191
3.649
ILE192
3.292
ARG193
4.704
THR194
2.433
LEU195
3.463
ALA196
2.537
PDB ID: 5CG1      Crystal structure of E. coli FabI bound to the carbamoylated benzodiazaborine inhibitor 14b.
Method X-ray diffraction Resolution 2.07 Å Mutation No [13]
PDB Sequence
GFLSGKRILV
11
TGVASKLSIA
21
YGIAQAMHRE
31
GAELAFTYQN
41
DKLKGRVEEF
51

AAQLGSDIVL
61
QCDVAEDASI
71
DTMFAELGKV
81
WPKFDGFVHS
91
IGFAPGDQLD
101

GDYVNAVTRE
111
GFKIAHDISS
121
YSFVAMAKAC
131
RSMLNPGSAL
141
LTLSYLGAER
151

AIPNYNVMGL
161
AKASLEANVR
171
YMANAMGPEG
181
VRVNAISAGP
191
IRTRKMLAHC
210

EAVTPIRRTV
220
TIEDVGNSAA
230
FLCSDLSAGI
240
SGEVVHVDGG
250
FSIAAMN
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAD or .NAD2 or .NAD3 or :3NAD;style chemicals stick;color identity;select .A:13 or .A:14 or .A:15 or .A:18 or .A:19 or .A:20 or .A:21 or .A:40 or .A:44 or .A:63 or .A:64 or .A:65 or .A:66 or .A:91 or .A:92 or .A:93 or .A:94 or .A:119 or .A:144 or .A:145 or .A:146 or .A:156 or .A:163 or .A:189 or .A:190 or .A:191 or .A:192; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLY13
2.802
VAL14
3.919
ALA15
3.624
LEU18
4.872
SER19
2.695
ILE20
2.903
ALA21
4.292
GLN40
2.921
LEU44
3.539
CYS63
3.467
ASP64
2.868
VAL65
3.059
ALA66
4.013
SER91
3.179
Residue
Distance (Å)
ILE92
3.496
GLY93
3.684
PHE94
4.187
ILE119
3.756
LEU144
3.363
SER145
3.080
TYR146
3.726
TYR156
4.122
LYS163
2.864
ALA189
3.290
GLY190
3.633
PRO191
3.212
ILE192
2.827
PDB ID: 5CG2      Crystal structure of E. coli FabI bound to the thiocarbamoylated benzodiazaborine inhibitor 35b.
Method X-ray diffraction Resolution 2.11 Å Mutation No [13]
PDB Sequence
GFLSGKRILV
11
TGVASKLSIA
21
YGIAQAMHRE
31
GAELAFTYQN
41
DKLKGRVEEF
51

AAQLGSDIVL
61
QCDVAEDASI
71
DTMFAELGKV
81
WPKFDGFVHS
91
IGFAPGDQLD
101

GDYVNAVTRE
111
GFKIAHDISS
121
YSFVAMAKAC
131
RSMLNPGSAL
141
LTLSYLGAER
151

AIPNYNVMGL
161
AKASLEANVR
171
YMANAMGPEG
181
VRVNAISAGP
191
IREAVTPIRR
218

TVTIEDVGNS
228
AAFLCSDLSA
238
GISGEVVHVD
248
GGFSIAAMN
Click to Show 3D Structure of This Binding Site
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Residue
Distance (Å)
GLY13
2.885
VAL14
3.852
ALA15
3.461
LEU18
4.887
SER19
2.635
ILE20
2.872
ALA21
4.235
GLN40
2.621
LEU44
3.423
CYS63
3.407
ASP64
2.663
VAL65
2.905
ALA66
3.996
SER91
3.055
Residue
Distance (Å)
ILE92
3.478
GLY93
3.753
PHE94
4.168
ILE119
3.682
LEU144
3.364
SER145
3.112
TYR146
3.740
TYR156
4.199
LYS163
2.944
ALA189
3.260
GLY190
3.413
PRO191
3.401
ILE192
2.776
References  Top
REF 1 Molecular basis for triclosan activity involves a flipping loop in the active site. Protein Sci. 1999 Nov;8(11):2529-32.
REF 2 Indole naphthyridinones as inhibitors of bacterial enoyl-ACP reductases FabI and FabK. J Med Chem. 2003 Apr 24;46(9):1627-35.
REF 3 Inhibitors of bacterial enoyl acyl carrier protein reductase (FabI): 2,9-disubstituted 1,2,3,4-tetrahydropyrido[3,4-b]indoles as potential antibacterial agents. Bioorg Med Chem Lett. 2001 Sep 3;11(17):2241-4.
REF 4 Discovery of aminopyridine-based inhibitors of bacterial enoyl-ACP reductase (FabI). J Med Chem. 2002 Jul 18;45(15):3246-56.
REF 5 1,4-Disubstituted imidazoles are potential antibacterial agents functioning as inhibitors of enoyl acyl carrier protein reductase (FabI). Bioorg Med Chem Lett. 2001 Aug 20;11(16):2061-5.
REF 6 Kinetic and structural characteristics of the inhibition of enoyl (acyl carrier protein) reductase by triclosan. Biochemistry. 1999 Sep 21;38(38):12514-25.
REF 7 A mechanism of drug action revealed by structural studies of enoyl reductase. Science. 1996 Dec 20;274(5295):2107-10.
REF 8 Molecular basis of triclosan activity. Nature. 1999 Apr 1;398(6726):383-4.
REF 9 Structural basis and mechanism of enoyl reductase inhibition by triclosan. J Mol Biol. 1999 Jul 23;290(4):859-65.
REF 10 Structural basis of triclosan resistance. J Struct Biol. 2011 Apr;174(1):173-9.
REF 11 Crystal Structure of E.coli Enoyl Reductase in Complex with NAD and AFN-1252
REF 12 Crystal Structure of E.coli Enoyl Reductase in Complex with NAD and AEA16
REF 13 Crystallographic insights into the structure-activity relationships of diazaborine enoyl-ACP reductase inhibitors. Acta Crystallogr F Struct Biol Commun. 2015 Dec;71(Pt 12):1521-30.

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