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 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
FABH_ECOLI
Ligand General Information  Top
Ligand Name Selenomethionine Ligand Info
Canonical SMILES C[Se]CCC(C(=O)O)N
InChI 1S/C5H11NO2Se/c1-9-3-2-4(6)5(7)8/h4H,2-3,6H2,1H3,(H,7,8)
InChIKey RJFAYQIBOAGBLC-UHFFFAOYSA-N
PubChem Compound ID 15103
Drug Binding Sites of Target  Top
PDB ID: 1EBL      THE 1.8 A CRYSTAL STRUCTURE AND ACTIVE SITE ARCHITECTURE OF BETA-KETOACYL-[ACYL CARRIER PROTEIN] SYNTHASE III (FABH) FROM ESCHERICHIA COLI
Method X-ray diffraction Resolution 1.80 Å Mutation Yes [1]
PDB Sequence
YTKIIGTGSY
11
LPEQVRTNAD
21
LEKVDTSDEW
32
IVTRTGIRER
42
HIAAPNETVS
52

TGFEAATRAI
63
EAGIEKDQIG
74
LIVVATTSAT
84
HAFPSAACQI
94
QSLGIKGCPA
105

FDVAAACAGF
115
TYALSVADQY
125
VKSGAVKYAL
135
VVGSDVLART
145
CDPTDRGTII
155

IFGDGAGAAV
165
LAASEEPGII
175
STHLHADGSY
185
GELLTLPNAD
195
RVNPENSIHL
205

TAGNEVFKVA
216
VTELAHIVDE
226
TLAANNNDRS
236
QLDWLVPHQA
246
NLRIISATAK
256

KLGSDNVVVT
268
LDRHGNTSAA
278
SVPCALDEAV
288
RDGRIKPGQL
298
VLLEAFGGGF
308

TWGSALVRF
Residue
Distance (Å)
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
Residue
Distance (Å)
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
PDB ID: 1HNH      CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III + DEGRADED FORM OF ACETYL-COA
Method X-ray diffraction Resolution 1.90 Å Mutation Yes [2]
PDB Sequence
YTKIIGTGSY
11
LPEQVRTNAD
21
LEKVDTSDEW
32
IVTRTGIRER
42
HIAAPNETVS
52

TGFEAATRAI
63
EAGIEKDQIG
74
LIVVATTSAT
84
HAFPSAACQI
94
QSLGIKGCPA
105

FDVAAAAGFT
116
YALSVADQYV
126
KSGAVKYALV
136
VGSDVLARTC
146
DPTDRGTIII
156

FGDGAGAAVL
166
AASEEPGIIS
176
THLHADGSYG
186
ELLTLPNADR
196
VNPENSIHLT
206

AGNEVFKVAV
217
TELAHIVDET
227
LAANNLDRSQ
237
LDWLVPHQAN
247
LRIISATAKK
257

LGSDNVVVTL
269
DRHGNTSAAS
279
VPCALDEAVR
289
DGRIKPGQLV
299
LLEAFGGGFT
309

WGSALVRF
Residue
Distance (Å)
TYR2
1.327
THR3
4.548
ILE6
3.372
GLY7
3.413
THR8
3.568
TYR11
3.290
PRO13
3.412
ARG17
3.605
ASP21
3.439
LEU22
2.797
GLU23
3.256
LYS24
1.315
VAL26
1.332
ASP27
4.597
ALA45
2.843
GLU49
3.947
THR50
2.832
VAL51
3.697
SER52
3.219
THR53
1.330
GLY55
1.336
PHE56
3.137
GLU57
3.123
ALA58
3.153
ARG61
3.041
ALA62
3.178
ILE63
3.323
GLU64
1.335
ALA66
1.329
GLY67
3.100
GLN93
3.004
ILE94
3.074
GLN95
3.208
SER96
1.331
LEU98
1.334
GLY99
3.045
VAL126
3.738
LYS127
3.339
GLY129
4.825
Residue
Distance (Å)
SER139
3.830
ASP140
4.739
VAL141
4.078
PRO148
4.612
GLY152
4.042
THR153
4.351
ILE154
3.927
ILE156
4.637
PHE157
4.296
ASP159
4.275
GLY160
3.689
ALA161
3.276
ALA168
3.860
SER169
3.593
GLU170
3.923
LEU188
3.467
LEU189
3.681
LEU205
4.130
THR206
1.331
ALA208
1.322
GLY209
2.997
VAL212
4.302
ARG235
4.659
LEU238
4.153
LEU241
3.888
ILE251
4.164
SER252
4.138
THR254
4.752
ALA255
2.934
LYS256
4.517
LEU258
2.861
GLY259
1.333
SER261
1.325
ASP263
1.337
ASN264
3.087
VAL265
3.098
VAL267
3.586
VAL288
4.348
ARG289
3.839
References  Top
REF 1 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 2 Refined structures of beta-ketoacyl-acyl carrier protein synthase III. J Mol Biol. 2001 Mar 16;307(1):341-56.

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