Binding Site Information of Target
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T72444 | Target Info | |||
| Target Name | Bacterial Beta-ketoacyl-ACP synthase III (Bact fabH) | ||||
| Synonyms | KAS III; FabH; EcFabH; Condensing enzyme FabH; Beta-ketoacyl-acyl carrier protein synthase III; Acetoacetyl-acyl carrier protein synthase; Acetoacetyl-ACP synthase; 3-oxoacyl-[acyl-carrier-protein] synthase III | ||||
| Target Type | Literature-reported Target | ||||
| Gene Name | Bact fabH | ||||
| Biochemical Class | Acyltransferase | ||||
| UniProt ID | |||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| Ligand Name: Malonyl-CoA | Ligand Info | |||||
| Structure Description | CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III + MALONYL-COA | PDB:1HNJ | ||||
| Method | X-ray diffraction | Resolution | 1.46 Å | Mutation | No | [1] |
| PDB Sequence |
MYTKIIGTGS
10 YLPEQVRTNA20 DLEKMVDTSD30 EWIVTRTGIR40 ERHIAAPNET50 VSTMGFEAAT 60 RAIEMAGIEK70 DQIGLIVVAT80 TSATHAFPSA90 ACQIQSMLGI100 KGCPAFDVAA 110 ACAGFTYALS120 VADQYVKSGA130 VKYALVVGSD140 VLARTCDPTD150 RGTIIIFGDG 160 AGAAVLAASE170 EPGIISTHLH180 ADGSYGELLT190 LPNADRVNPE200 NSIHLTMAGN 210 EVFKVAVTEL220 AHIVDETLAA230 NNLDRSQLDW240 LVPHQANLRI250 ISATAKKLGM 260 SMDNVVVTLD270 RHGNTSAASV280 PCALDEAVRD290 GRIKPGQLVL300 LEAFGGGFTW 310 GSALVRF
|
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|
|
ASP27
3.819
THR28
2.625
SER29
4.628
TRP32
3.256
ILE33
4.915
ARG36
2.990
THR37
3.448
CYS112
4.505
ARG151
2.931
GLY152
3.794
ILE155
3.559
ILE156
3.764
LEU189
3.786
MET207
3.541
|
|||||
| Ligand Name: Coenzyme A | Ligand Info | |||||
| Structure Description | CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III-COA COMPLEX | PDB:1HND | ||||
| Method | X-ray diffraction | Resolution | 1.60 Å | Mutation | No | [1] |
| PDB Sequence |
MYTKIIGTGS
10 YLPEQVRTNA20 DLEKMVDTSD30 EWIVTRTGIR40 ERHIAAPNET50 VSTMGFEAAT 60 RAIEMAGIEK70 DQIGLIVVAT80 TSATHAFPSA90 ACQIQSMLGI100 KGCPAFDVAA 110 ACAGFTYALS120 VADQYVKSGA130 VKYALVVGSD140 VLARTCDPTD150 RGTIIIFGDG 160 AGAAVLAASE170 EPGIISTHLH180 ADGSYGELLT190 LPNADRVNPE200 NSIHLTMAGN 210 EVFKVAVTEL220 AHIVDETLAA230 NNLDRSQLDW240 LVPHQANLRI250 ISATAKKLGM 260 SMDNVVVTLD270 RHGNTSAASV280 PCALDEAVRD290 GRIKPGQLVL300 LEAFGGGFTW 310 GSALVRF
|
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|
|
ASP27
3.811
THR28
2.593
SER29
4.600
TRP32
3.232
ILE33
4.752
ARG36
3.294
THR37
3.569
CYS112
2.838
ARG151
2.930
GLY152
3.821
ILE155
3.410
ILE156
3.389
LEU189
3.419
MET207
3.559
|
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| Click to View More Binding Site Information of This Target and Ligand Pair | ||||||
| Ligand Name: Cysteinesulfonic Acid | Ligand Info | |||||
| Structure Description | CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III WITH BOUND dichlorobenzyloxy-indole-carboxylic acid inhibitor | PDB:1MZS | ||||
| Method | X-ray diffraction | Resolution | 2.10 Å | Mutation | Yes | [2] |
| PDB Sequence |
MYTKIIGTGS
10 YLPEQVRTNA20 DLEKMVDTSD30 EWIVTRTGIR40 ERHIAAPNET50 VSTMGFEAAT 60 RAIEMAGIEK70 DQIGLIVVAT80 TSATHAFPSA90 ACQIQSMLGI100 KGCPAFDVAA 110 AAGFTYALSV121 ADQYVKSGAV131 KYALVVGSDV141 LARTCDPTDR151 GTIIIFGDGA 161 GAAVLAASEE171 PGIISTHLHA181 DGSYGELLTL191 PNADRVNPEN201 SIHLTMAGNE 211 VFKVAVTELA221 HIVDETLAAN231 NLDRSQLDWL241 VPHQANLRII251 SATAKKLGMS 261 MDNVVVTLDR271 HGNTSAASVP281 CALDEAVRDG291 RIKPGQLVLL301 EAFGGGFTWG 311 SALVRF
|
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .OCS or .OCS2 or .OCS3 or :3OCS;style chemicals stick;color identity;select .A:110 or .A:111 or .A:113 or .A:114 or .A:115 or .A:142 or .A:157 or .A:189 or .A:244 or .A:274 or .A:276 or .A:277 or .A:303 or .A:304 or .A:305 or .A:306; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| Ligand Name: N-{[3'-(Hydroxymethyl)biphenyl-4-Yl]methyl}benzenesulfonamide | Ligand Info | |||||
| Structure Description | E. coli FabH with Small Molecule Inhibitor 1 | PDB:5BNM | ||||
| Method | X-ray diffraction | Resolution | 1.70 Å | Mutation | No | [3] |
| PDB Sequence |
MYTKIIGTGS
10 YLPEQVRTNA20 DLEKMVDTSD30 EWIVTRTGIR40 ERHIAAPNET50 VSTMGFEAAT 60 RAIEMAGIEK70 DQIGLIVVAT80 TSATHAFPSA90 ACQIQSMLGI100 KGCPAFDVAA 110 ACAGFTYALS120 VADQYVKSGA130 VKYALVVGSD140 VLARTCDPTD150 RGTIIIFGDG 160 AGAAVLAASE170 EPGIISTHLH180 ADGSYGELLT190 LPNADRVNPE200 NSIHLTMAGN 210 EVFKVAVTEL220 AHIVDETLAA230 NNLDRSQLDW240 LVPHQANLRI250 ISATAKKLGM 260 SMDNVVVTLD270 RHGNTSAASV280 PCALDEAVRD290 GRIKPGQLVL300 LEAFGGGFTW 310 GSALVRF
|
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|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .4VK or .4VK2 or .4VK3 or :34VK;style chemicals stick;color identity;select .A:32 or .A:36 or .A:37 or .A:112 or .A:155 or .A:156 or .A:157 or .A:189 or .A:207 or .A:209 or .A:210 or .A:212 or .A:213 or .A:216 or .A:244 or .A:246 or .A:247 or .A:249 or .A:250 or .A:274 or .A:304 or .A:305; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
TRP32
3.588
ARG36
3.197
THR37
3.353
CYS112
2.972
ILE155
4.699
ILE156
3.651
PHE157
3.973
LEU189
3.915
MET207
3.882
GLY209
3.211
ASN210
4.901
|
|||||
| Ligand Name: Selenomethionine | Ligand Info | |||||
| Structure Description | THE 1.8 A CRYSTAL STRUCTURE AND ACTIVE SITE ARCHITECTURE OF BETA-KETOACYL-[ACYL CARRIER PROTEIN] SYNTHASE III (FABH) FROM ESCHERICHIA COLI | PDB:1EBL | ||||
| Method | X-ray diffraction | Resolution | 1.80 Å | Mutation | Yes | [4] |
| PDB Sequence |
YTKIIGTGSY
11 LPEQVRTNAD21 LEKVDTSDEW32 IVTRTGIRER42 HIAAPNETVS52 TGFEAATRAI 63 EAGIEKDQIG74 LIVVATTSAT84 HAFPSAACQI94 QSLGIKGCPA105 FDVAAACAGF 115 TYALSVADQY125 VKSGAVKYAL135 VVGSDVLART145 CDPTDRGTII155 IFGDGAGAAV 165 LAASEEPGII175 STHLHADGSY185 GELLTLPNAD195 RVNPENSIHL205 TAGNEVFKVA 216 VTELAHIVDE226 TLAANNNDRS236 QLDWLVPHQA246 NLRIISATAK256 KLGSDNVVVT 268 LDRHGNTSAA278 SVPCALDEAV288 RDGRIKPGQL298 VLLEAFGGGF308 TWGSALVRF |
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .MSE or .MSE2 or .MSE3 or :3MSE;style chemicals stick;color identity;select .A:2 or .A:3 or .A:6 or .A:7 or .A:8 or .A:11 or .A:13 or .A:17 or .A:21 or .A:22 or .A:23 or .A:24 or .A:26 or .A:27 or .A:45 or .A:49 or .A:50 or .A:51 or .A:52 or .A:53 or .A:55 or .A:56 or .A:57 or .A:58 or .A:59 or .A:61 or .A:62 or .A:63 or .A:64 or .A:66 or .A:67 or .A:90 or .A:93 or .A:94 or .A:95 or .A:96 or .A:98 or .A:99 or .A:126 or .A:127 or .A:128 or .A:129 or .A:139 or .A:140 or .A:141 or .A:148 or .A:149 or .A:152 or .A:153 or .A:154 or .A:156 or .A:159 or .A:160 or .A:161 or .A:168 or .A:169 or .A:188 or .A:189 or .A:205 or .A:206 or .A:208 or .A:209 or .A:212 or .A:224 or .A:235 or .A:238 or .A:241 or .A:248 or .A:251 or .A:252 or .A:255 or .A:256 or .A:258 or .A:259 or .A:261 or .A:263 or .A:264 or .A:265 or .A:267 or .A:285 or .A:288 or .A:289; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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TYR2
1.333
THR3
4.651
ILE6
3.821
GLY7
3.890
THR8
3.418
TYR11
3.814
PRO13
3.911
ARG17
3.772
ASP21
3.175
LEU22
2.877
GLU23
3.356
LYS24
1.337
VAL26
1.316
ASP27
4.667
ALA45
4.229
GLU49
4.056
THR50
3.065
VAL51
3.750
SER52
3.124
THR53
1.334
GLY55
1.331
PHE56
3.201
GLU57
3.112
ALA58
3.069
ALA59
4.924
ARG61
3.004
ALA62
3.267
ILE63
3.309
GLU64
1.330
ALA66
1.319
GLY67
3.217
ALA90
4.835
GLN93
2.979
ILE94
3.130
GLN95
3.247
SER96
1.335
LEU98
1.329
GLY99
3.195
VAL126
3.981
LYS127
3.670
SER128
4.587
GLY129
3.507
SER139
3.801
ASP140
3.453
VAL141
3.391
PRO148
3.905
THR149
4.856
GLY152
4.385
THR153
4.316
ILE154
4.052
ILE156
3.655
ASP159
4.328
GLY160
3.457
ALA161
3.380
ALA168
3.832
SER169
3.755
LEU188
3.396
LEU189
3.339
LEU205
4.153
THR206
1.335
ALA208
1.311
GLY209
3.504
VAL212
4.847
VAL224
4.267
ARG235
4.241
LEU238
4.391
LEU241
3.894
LEU248
4.127
ILE251
3.894
SER252
4.021
ALA255
2.897
LYS256
4.615
LEU258
3.205
GLY259
1.327
SER261
1.324
ASP263
1.336
ASN264
3.155
VAL265
3.213
VAL267
3.770
ASP285
4.095
VAL288
4.081
ARG289
3.322
|
|||||
| Click to View More Binding Site Information of This Target and Ligand Pair | ||||||
| Ligand Name: 1-{5-[2-Fluoro-5-(Hydroxymethyl)phenyl]pyridin-2-Yl}piperidine-4-Carboxylic Acid | Ligand Info | |||||
| Structure Description | E. coli Fabh with small molecule inhibitor 2 | PDB:5BNR | ||||
| Method | X-ray diffraction | Resolution | 1.89 Å | Mutation | No | [3] |
| PDB Sequence |
MYTKIIGTGS
10 YLPEQVRTNA20 DLEKMVDTSD30 EWIVTRTGIR40 ERHIAAPNET50 VSTMGFEAAT 60 RAIEMAGIEK70 DQIGLIVVAT80 TSATHAFPSA90 ACQIQSMLGI100 KGCPAFDVAA 110 ACAGFTYALS120 VADQYVKSGA130 VKYALVVGSD140 VLARTCDPTD150 RGTIIIFGDG 160 AGAAVLAASE170 EPGIISTHLH180 ADGSYGELLT190 LPNAIHLTMA208 GNEVFKVAVT 218 ELAHIVDETL228 AANNLDRSQL238 DWLVPHQANL248 RIISATAKKL258 GMSMDNVVVT 268 LDRHGNTSAA278 SVPCALDEAV288 RDGRIKPGQL298 VLLEAFGGGF308 TWGSALVRF |
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|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .4VL or .4VL2 or .4VL3 or :34VL;style chemicals stick;color identity;select .A:32 or .A:36 or .A:37 or .A:112 or .A:151 or .A:152 or .A:156 or .A:157 or .A:189 or .A:207 or .A:209 or .A:210 or .A:212 or .A:213 or .A:216 or .A:244 or .A:246 or .A:247 or .A:249 or .A:250 or .A:274 or .A:304 or .A:305; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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TRP32
3.354
ARG36
3.376
THR37
4.325
CYS112
2.975
ARG151
4.657
GLY152
4.042
ILE156
3.337
PHE157
3.849
LEU189
3.894
MET207
3.596
GLY209
3.124
ASN210
3.656
|
|||||
| Ligand Name: Methanethiol | Ligand Info | |||||
| Structure Description | Methanethiol-CYS 112 inhibition complex of E. coli ketoacyl synthase III (FABH) and Coenzyme A (high concentration (1.7mM) soak) | PDB:2EFT | ||||
| Method | X-ray diffraction | Resolution | 2.00 Å | Mutation | No | [5] |
| PDB Sequence |
MYTKIIGTGS
10 YLPEQVRTNA20 DLEKMVDTSD30 EWIVTRTGIR40 ERHIAAPNET50 VSTMGFEAAT 60 RAIEMAGIEK70 DQIGLIVVAT80 TSATHAFPSA90 ACQIQSMLGI100 KGCPAFDVAA 110 ACAGFTYALS120 VADQYVKSGA130 VKYALVVGSD140 VLARTCDPTD150 RGTIIIFGDG 160 AGAAVLAASE170 EPGIISTHLH180 ADGSYGELLT190 LPNADRVNPE200 NSIHLTMAGN 210 EVFKVAVTEL220 AHIVDETLAA230 NNLDRSQLDW240 LVPHQANLRI250 ISATAKKLGM 260 SMDNVVVTLD270 RHGNTSAASV280 PCALDEAVRD290 GRIKPGQLVL300 LEAFGGGFTW 310 GSALVRF
|
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|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .MEE or .MEE2 or .MEE3 or :3MEE;style chemicals stick;color identity;select .A:111 or .A:112 or .A:142 or .A:157 or .A:189 or .A:276 or .A:304 or .A:305 or .A:306; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| Click to View More Binding Site Information of This Target and Ligand Pair | ||||||
| Ligand Name: Trans-4-[({[(2-Chlorobenzyl)oxy]carbonyl}amino)methyl]cyclohexanecarboxylic Acid | Ligand Info | |||||
| Structure Description | Antibacterial FabH Inhibitors with Validated Mode of Action in Haemophilus Influenzae by in vitro resistance mutation mapping | PDB:4Z8D | ||||
| Method | X-ray diffraction | Resolution | 2.00 Å | Mutation | No | [3] |
| PDB Sequence |
MYTKIIGTGS
10 YLPEQVRTNA20 DLEKMVDTSD30 EWIVTRTGIR40 ERHIAAPNET50 VSTMGFEAAT 60 RAIEMAGIEK70 DQIGLIVVAT80 TSATHAFPSA90 ACQIQSMLGI100 KGCPAFDVAA 110 ACAGFTYALS120 VADQYVKSGA130 VKYALVVGSD140 VLARTCDPTD150 RGTIIIFGDG 160 AGAAVLAASE170 EPGIISTHLH180 ADGSYGELLT190 LPNADRVNPE200 NSIHLTMAGN 210 EVFKVAVTEL220 AHIVDETLAA230 NNLDRSQLDW240 LVPHQANLRI250 ISATAKKLGM 260 SMDNVVVTLD270 RHGNTSAASV280 PCALDEAVRD290 GRIKPGQLVL300 LEAFGGGFTW 310 GSALVRF
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|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .4LB or .4LB2 or .4LB3 or :34LB;style chemicals stick;color identity;select .A:32 or .A:36 or .A:37 or .A:112 or .A:156 or .A:157 or .A:189 or .A:207 or .A:209 or .A:210 or .A:212 or .A:213 or .A:216 or .A:244 or .A:246 or .A:247 or .A:249 or .A:250 or .A:274 or .A:304 or .A:305; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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TRP32
4.126
ARG36
3.691
THR37
4.320
CYS112
3.820
ILE156
3.952
PHE157
4.171
LEU189
3.827
MET207
3.729
GLY209
2.913
ASN210
3.868
VAL212
3.526
|
|||||
| Ligand Name: 1-(5-Carboxypentyl)-5-[(2,6-dichlorobenzyl)oxy]-1 H-indole-2-carboxylic acid | Ligand Info | |||||
| Structure Description | CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III WITH BOUND dichlorobenzyloxy-indole-carboxylic acid inhibitor | PDB:1MZS | ||||
| Method | X-ray diffraction | Resolution | 2.10 Å | Mutation | Yes | [2] |
| PDB Sequence |
MYTKIIGTGS
10 YLPEQVRTNA20 DLEKMVDTSD30 EWIVTRTGIR40 ERHIAAPNET50 VSTMGFEAAT 60 RAIEMAGIEK70 DQIGLIVVAT80 TSATHAFPSA90 ACQIQSMLGI100 KGCPAFDVAA 110 AAGFTYALSV121 ADQYVKSGAV131 KYALVVGSDV141 LARTCDPTDR151 GTIIIFGDGA 161 GAAVLAASEE171 PGIISTHLHA181 DGSYGELLTL191 PNADRVNPEN201 SIHLTMAGNE 211 VFKVAVTELA221 HIVDETLAAN231 NLDRSQLDWL241 VPHQANLRII251 SATAKKLGMS 261 MDNVVVTLDR271 HGNTSAASVP281 CALDEAVRDG291 RIKPGQLVLL301 EAFGGGFTWG 311 SALVRF
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .669 or .6692 or .6693 or :3669;style chemicals stick;color identity;select .A:32 or .A:36 or .A:37 or .A:151 or .A:152 or .A:155 or .A:156 or .A:157 or .A:189 or .A:207 or .A:209 or .A:210 or .A:212 or .A:213 or .A:216 or .A:244 or .A:246 or .A:247 or .A:249 or .A:250 or .A:274 or .A:304 or .A:305; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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TRP32
3.239
ARG36
3.410
THR37
3.446
ARG151
2.520
GLY152
3.292
ILE155
4.219
ILE156
3.834
PHE157
4.352
LEU189
3.662
MET207
3.570
GLY209
3.416
ASN210
3.718
|
|||||
| Ligand Name: 1-{5-[2-Fluoro-5-(Hydroxymethyl)phenyl]pyridin-2-Yl}-N-(Quinolin-6-Ylmethyl)piperidine-4-Carboxamide | Ligand Info | |||||
| Structure Description | E. coli Fabh with small molecule inhibitor 2 | PDB:5BNS | ||||
| Method | X-ray diffraction | Resolution | 2.20 Å | Mutation | No | [3] |
| PDB Sequence |
MYTKIIGTGS
10 YLPEQVRTNA20 DLEKMVDTSD30 EWIVTRTGIR40 ERHIAAPNET50 VSTMGFEAAT 60 RAIEMAGIEK70 DQIGLIVVAT80 TSATHAFPSA90 ACQIQSMLGI100 KGCPAFDVAA 110 ACAGFTYALS120 VADQYVKSGA130 VKYALVVGSD140 VLARTCDPTD150 RGTIIIFGDG 160 AGAAVLAASE170 EPGIISTHLH180 ADGSYGELLT190 LPNADRVNPE200 NSIHLTMAGN 210 EVFKVAVTEL220 AHIVDETLAA230 NNLDRSQLDW240 LVPHQANLRI250 ISATAKKLGM 260 SMDNVVVTLD270 RHGNTSAASV280 PCALDEAVRD290 GRIKPGQLVL300 LEAFGGGFTW 310 GSALVRF
|
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|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .4VM or .4VM2 or .4VM3 or :34VM;style chemicals stick;color identity;select .A:27 or .A:28 or .A:29 or .A:32 or .A:36 or .A:37 or .A:112 or .A:151 or .A:152 or .A:155 or .A:156 or .A:157 or .A:189 or .A:207 or .A:209 or .A:210 or .A:212 or .A:213 or .A:216 or .A:244 or .A:246 or .A:247 or .A:250 or .A:274 or .A:304 or .A:305; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ASP27
3.729
THR28
2.776
SER29
4.656
TRP32
3.470
ARG36
4.597
THR37
3.899
CYS112
2.974
ARG151
3.573
GLY152
3.235
ILE155
3.896
ILE156
3.879
PHE157
4.031
LEU189
3.785
|
|||||
| Ligand Name: oxa(dethia)-CoA | Ligand Info | |||||
| Structure Description | E. coli beta-ketoacyl-[acyl carrier protein] synthase III (FabH) with an acetylated cysteine and in complex with oxa(dethia)-Coenzyme A | PDB:8D1U | ||||
| Method | X-ray diffraction | Resolution | 1.30 Å | Mutation | No | [6] |
| PDB Sequence |
GMYTKIIGTG
9 SYLPEQVRTN19 ADLEKMVDTS29 DEWIVTRTGI39 RERHIAAPNE49 TVSTMGFEAA 59 TRAIEMAGIE69 KDQIGLIVVA79 TTSATHAFPS89 AACQIQSMLG99 IKGCPAFDVA 109 AAAGFTYALS120 VADQYVKSGA130 VKYALVVGSD140 VLARTCDPTD150 RGTIIIFGDG 160 AGAAVLAASE170 EPGIISTHLH180 ADGSYGELLT190 LPNADRVNPE200 NSIHLTMAGN 210 EVFKVAVTEL220 AHIVDETLAA230 NNLDRSQLDW240 LVPHQANLRI250 ISATAKKLGM 260 SMDNVVVTLD270 RHGNTSAASV280 PCALDEAVRD290 GRIKPGQLVL300 LEAFGGGFTW 310 GSALVRF
|
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|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .UT7 or .UT72 or .UT73 or :3UT7;style chemicals stick;color identity;select .A:27 or .A:28 or .A:29 or .A:32 or .A:33 or .A:36 or .A:37 or .A:151 or .A:152 or .A:155 or .A:156 or .A:157 or .A:189 or .A:207 or .A:209 or .A:210 or .A:212 or .A:213 or .A:216 or .A:244 or .A:246 or .A:247 or .A:249 or .A:250 or .A:274 or .A:304 or .A:305; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
ASP27
3.877
THR28
2.711
SER29
4.720
TRP32
3.273
ILE33
4.901
ARG36
2.689
THR37
3.705
ARG151
2.996
GLY152
3.801
ILE155
3.367
ILE156
3.429
PHE157
4.421
LEU189
3.633
MET207
3.611
|
|||||
| Click to View More Binding Site Information of This Target and Ligand Pair | ||||||
| Ligand Name: S-Acetyl-Cysteine | Ligand Info | |||||
| Structure Description | E. coli beta-ketoacyl-[acyl carrier protein] synthase III (FabH) with an acetylated cysteine and in complex with oxa(dethia)-Coenzyme A | PDB:8D1U | ||||
| Method | X-ray diffraction | Resolution | 1.30 Å | Mutation | No | [6] |
| PDB Sequence |
GMYTKIIGTG
9 SYLPEQVRTN19 ADLEKMVDTS29 DEWIVTRTGI39 RERHIAAPNE49 TVSTMGFEAA 59 TRAIEMAGIE69 KDQIGLIVVA79 TTSATHAFPS89 AACQIQSMLG99 IKGCPAFDVA 109 AAAGFTYALS120 VADQYVKSGA130 VKYALVVGSD140 VLARTCDPTD150 RGTIIIFGDG 160 AGAAVLAASE170 EPGIISTHLH180 ADGSYGELLT190 LPNADRVNPE200 NSIHLTMAGN 210 EVFKVAVTEL220 AHIVDETLAA230 NNLDRSQLDW240 LVPHQANLRI250 ISATAKKLGM 260 SMDNVVVTLD270 RHGNTSAASV280 PCALDEAVRD290 GRIKPGQLVL300 LEAFGGGFTW 310 GSALVRF
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Refined structures of beta-ketoacyl-acyl carrier protein synthase III. J Mol Biol. 2001 Mar 16;307(1):341-56. | ||||
| REF 2 | First X-ray cocrystal structure of a bacterial FabH condensing enzyme and a small molecule inhibitor achieved using rational design and homology modeling. J Med Chem. 2003 Jan 2;46(1):5-8. | ||||
| REF 3 | Antibacterial FabH Inhibitors with Mode of Action Validated in Haemophilus influenzae by in Vitro Resistance Mutation Mapping. ACS Infect Dis. 2016 Jul 8;2(7):456-64. | ||||
| REF 4 | The 1.8 A crystal structure and active-site architecture of beta-ketoacyl-acyl carrier protein synthase III (FabH) from escherichia coli. Structure. 2000 Feb 15;8(2):185-95. | ||||
| REF 5 | Alkyl-CoA disulfides as inhibitors and mechanistic probes for FabH enzymes. Chem Biol. 2007 May;14(5):513-24. | ||||
| REF 6 | Structures of chloramphenicol acetyltransferase III and Escherichia coli Beta-ketoacylsynthase III co-crystallized with partially hydrolysed acetyl-oxa(dethia)CoA. Acta Crystallogr F Struct Biol Commun. 2023 Mar 1;79(Pt 3):61-69. | ||||
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