Target Binding Site Detail

Content Navigation (  All   None )                                      
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 oxa(dethia)-CoA Ligand Info
Canonical SMILES CC(C)(COP(=O)(O)OP(=O)(O)OCC1C(C(C(O1)N2C=NC3=C(N=CN=C32)N)O)OP(=O)(O)O)C(C(=O)NCCC(=O)NCCO)O
InChI 1S/C21H36N7O17P3/c1-21(2,16(32)19(33)24-4-3-12(30)23-5-6-29)8-42-48(39,40)45-47(37,38)41-7-11-15(44-46(34,35)36)14(31)20(43-11)28-10-27-13-17(22)25-9-26-18(13)28/h9-11,14-16,20,29,31-32H,3-8H2,1-2H3,(H,23,30)(H,24,33)(H,37,38)(H,39,40)(H2,22,25,26)(H2,34,35,36)/t11-,14-,15-,16+,20-/m1/s1
InChIKey JHUGPYYCEXFQAL-IBOSZNHHSA-N
PubChem Compound ID 102402838
Drug Binding Sites of Target  Top
PDB ID: 8D1U      E. coli beta-ketoacyl-[acyl carrier protein] synthase III (FabH) with an acetylated cysteine and in complex with oxa(dethia)-Coenzyme A
Method X-ray diffraction Resolution 1.30 Å Mutation No [1]
PDB Sequence
GMYTKIIGTG
9
SYLPEQVRTN
19
ADLEKMVDTS
29
DEWIVTRTGI
39
RERHIAAPNE
49

TVSTMGFEAA
59
TRAIEMAGIE
69
KDQIGLIVVA
79
TTSATHAFPS
89
AACQIQSMLG
99

IKGCPAFDVA
109
AAAGFTYALS
120
VADQYVKSGA
130
VKYALVVGSD
140
VLARTCDPTD
150

RGTIIIFGDG
160
AGAAVLAASE
170
EPGIISTHLH
180
ADGSYGELLT
190
LPNADRVNPE
200

NSIHLTMAGN
210
EVFKVAVTEL
220
AHIVDETLAA
230
NNLDRSQLDW
240
LVPHQANLRI
250

ISATAKKLGM
260
SMDNVVVTLD
270
RHGNTSAASV
280
PCALDEAVRD
290
GRIKPGQLVL
300

LEAFGGGFTW
310
GSALVRF
Residue
Distance (Å)
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
Residue
Distance (Å)
GLY209
2.919
ASN210
3.374
VAL212
3.470
PHE213
3.804
ALA216
4.345
HIS244
3.365
ALA246
3.739
ASN247
2.807
ARG249
2.978
ILE250
3.427
ASN274
2.674
PHE304
3.352
GLY305
4.447
PDB ID: 6X7R      E. coli beta-ketoacyl-[acyl carrier protein] synthase III (FabH) in complex with oxa(dethia)-coenzyme A
Method X-ray diffraction Resolution 1.35 Å Mutation No [2]
PDB Sequence
GMYTKIIGTG
9
SYLPEQVRTN
19
ADLEKMVDTS
29
DEWIVTRTGI
39
RERHIAAPNE
49

TVSTMGFEAA
59
TRAIEMAGIE
69
KDQIGLIVVA
79
TTSATHAFPS
89
AACQIQSMLG
99

IKGCPAFDVA
109
AACAGFTYAL
119
SVADQYVKSG
129
AVKYALVVGS
139
DVLARTCDPT
149

DRGTIIIFGD
159
GAGAAVLAAS
169
EEPGIISTHL
179
HADGSYGELL
189
TLPNADRVNP
199

ENSIHLTMAG
209
NEVFKVAVTE
219
LAHIVDETLA
229
ANNLDRSQLD
239
WLVPHQANLR
249

IISATAKKLG
259
MSMDNVVVTL
269
DRHGNTSAAS
279
VPCALDEAVR
289
DGRIKPGQLV
299

LLEAFGGGFT
309
WGSALVRF
Residue
Distance (Å)
ASP27
3.855
THR28
2.735
SER29
4.657
TRP32
3.219
ILE33
4.928
ARG36
2.880
THR37
3.624
CYS112
3.014
ARG151
2.995
GLY152
3.913
ILE155
3.574
ILE156
3.758
PHE157
4.255
LEU189
3.607
Residue
Distance (Å)
MET207
3.620
GLY209
2.934
ASN210
3.265
VAL212
3.521
PHE213
3.733
ALA216
4.340
HIS244
3.346
ALA246
3.762
ASN247
2.853
ARG249
2.937
ILE250
3.617
ASN274
2.650
PHE304
3.316
GLY305
4.372
References  Top
REF 1 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.
REF 2 Structures of chloramphenicol acetyltransferase III and Escherichia coli beta-keto-acylsynthase III co-crystallized with partially hydrolysed acetyl-oxa(de-thia)CoA. doi:10.1107/S2053230X23001206.

If You Find Any Error in Data or Bug in Web Service, Please Kindly Report It to Dr. Zhou and Dr. Zhang.