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 T79068 Target Info
Target Name Bacterial Fatty acid synthetase I (Bact inhA)
Synonyms Enoyl-[acyl-carrier-protein] reductase [NADH]; Bacterial InhA
Target Type Successful Target
Gene Name Bact inhA
Biochemical Class CH-CH donor oxidoreductase
UniProt ID
INHA_MYCTU
Ligand General Information  Top
Ligand Name Pyridomycin Ligand Info
Canonical SMILES CCC(=C1C(=O)OC(C(C(=O)NC(C(C(C(=O)O1)C)O)CC2=CN=CC=C2)NC(=O)C3=C(C=CC=N3)O)C)C
InChI 1S/C27H32N4O8/c1-5-14(2)23-27(37)38-16(4)20(31-25(35)21-19(32)9-7-11-29-21)24(34)30-18(12-17-8-6-10-28-13-17)22(33)15(3)26(36)39-23/h6-11,13,15-16,18,20,22,32-33H,5,12H2,1-4H3,(H,30,34)(H,31,35)/b23-14-/t15-,16-,18+,20+,22+/m1/s1
InChIKey WHIKSLGSXKIHCA-IGCCMALHSA-N
PubChem Compound ID 3037036
Drug Binding Sites of Target  Top
PDB ID: 4BII      How nature bridges the gap: Crystallographic elucidation of pyridomycin binding to InhA
Method X-ray diffraction Resolution 1.95 Å Mutation No [1]
PDB Sequence
GLLDGKRILV
12
SGIITDSSIA
22
FHIARVAQEQ
32
GAQLVLTGFD
42
RLRLIQRITD
52

RLPAKAPLLE
62
LDVQNEEHLA
72
SLAGRVTEAI
82
GAGNKLDGVV
92
HSIGFMPQTG
102

MGINPFFDAP
112
YADVSKGIHI
122
SAYSYASMAK
132
ALLPIMNPGG
142
SIVGMDFDPS
152

RAMPAYNWMT
162
VAKSALESVN
172
RFVAREAGKY
182
GVRSNLVAAG
192
PIRTGGALGE
209

EAGAQIQLLE
219
EGWDQRAPIG
229
WNMKDATPVA
239
KTVCALLSDW
249
LPATTGDIIY
259

ADGGAHTQLL
269
Residue
Distance (Å)
ILE21
3.384
SER94
3.261
ILE95
3.392
GLY96
3.724
MET103
3.121
GLY104
4.699
MET147
3.576
ASP148
3.171
PHE149
3.725
ALA157
3.667
Residue
Distance (Å)
TYR158
2.658
MET161
3.664
LYS165
2.826
ALA191
4.206
GLY192
3.595
PRO193
3.232
ILE194
3.202
THR196
4.827
ILE215
4.237
LEU218
4.415
PDB ID: 4BGE      Crystal structure of InhA(S94A) mutant in complex with pyridomycin
Method X-ray diffraction Resolution 2.25 Å Mutation Yes [1]
PDB Sequence
GLLDGKRILV
12
SGIITDSSIA
22
FHIARVAQEQ
32
GAQLVLTGFD
42
RLRLIQRITD
52

RLPAKAPLLE
62
LDVQNEEHLA
72
SLAGRVTEAI
82
GAGNKLDGVV
92
HAIGFMPQTG
102

MGINPFFDAP
112
YADVSKGIHI
122
SAYSYASMAK
132
ALLPIMNPGG
142
SIVGMDFDPS
152

RAMPAYNWMT
162
VAKSALESVN
172
RFVAREAGKY
182
GVRSNLVAAG
192
PIRTLAMSAI
202

VGGALGEEAG
212
AQIQLLEEGW
222
DQRAPIGWNM
232
KDATPVAKTV
242
CALLSDWLPA
252

TTGDIIYADG
262
GAHTQLL
Residue
Distance (Å)
ILE21
3.390
HIS93
4.728
ALA94
3.387
ILE95
3.468
GLY96
3.572
MET103
3.557
MET147
3.556
ASP148
3.268
PHE149
3.505
PRO156
4.896
ALA157
3.730
TYR158
2.599
Residue
Distance (Å)
MET161
3.577
LYS165
2.757
ALA191
4.380
GLY192
3.453
PRO193
3.318
ILE194
3.153
ALA198
4.945
MET199
3.286
ILE202
3.905
ILE215
4.217
LEU218
4.000
References  Top
REF 1 Pyridomycin bridges the NADH- and substrate-binding pockets of the enoyl reductase InhA. Nat Chem Biol. 2014 Feb;10(2):96-8.

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