Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5UGS

Crystal structure of M. tuberculosis InhA inhibited by PT501

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
A	0005504	molecular_function	fatty acid binding
A	0005886	cellular_component	plasma membrane
A	0006633	biological_process	fatty acid biosynthetic process
A	0009274	cellular_component	peptidoglycan-based cell wall
A	0016491	molecular_function	oxidoreductase activity
A	0030497	biological_process	fatty acid elongation
A	0046677	biological_process	response to antibiotic
A	0050343	molecular_function	trans-2-enoyl-CoA reductase (NADH) activity
A	0070403	molecular_function	NAD+ binding
A	0071768	biological_process	mycolic acid biosynthetic process
B	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
B	0005504	molecular_function	fatty acid binding
B	0005886	cellular_component	plasma membrane
B	0006633	biological_process	fatty acid biosynthetic process
B	0009274	cellular_component	peptidoglycan-based cell wall
B	0016491	molecular_function	oxidoreductase activity
B	0030497	biological_process	fatty acid elongation
B	0046677	biological_process	response to antibiotic
B	0050343	molecular_function	trans-2-enoyl-CoA reductase (NADH) activity
B	0070403	molecular_function	NAD+ binding
B	0071768	biological_process	mycolic acid biosynthetic process
C	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
C	0005504	molecular_function	fatty acid binding
C	0005886	cellular_component	plasma membrane
C	0006633	biological_process	fatty acid biosynthetic process
C	0009274	cellular_component	peptidoglycan-based cell wall
C	0016491	molecular_function	oxidoreductase activity
C	0030497	biological_process	fatty acid elongation
C	0046677	biological_process	response to antibiotic
C	0050343	molecular_function	trans-2-enoyl-CoA reductase (NADH) activity
C	0070403	molecular_function	NAD+ binding
C	0071768	biological_process	mycolic acid biosynthetic process
D	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
D	0005504	molecular_function	fatty acid binding
D	0005886	cellular_component	plasma membrane
D	0006633	biological_process	fatty acid biosynthetic process
D	0009274	cellular_component	peptidoglycan-based cell wall
D	0016491	molecular_function	oxidoreductase activity
D	0030497	biological_process	fatty acid elongation
D	0046677	biological_process	response to antibiotic
D	0050343	molecular_function	trans-2-enoyl-CoA reductase (NADH) activity
D	0070403	molecular_function	NAD+ binding
D	0071768	biological_process	mycolic acid biosynthetic process
E	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
E	0005504	molecular_function	fatty acid binding
E	0005886	cellular_component	plasma membrane
E	0006633	biological_process	fatty acid biosynthetic process
E	0009274	cellular_component	peptidoglycan-based cell wall
E	0016491	molecular_function	oxidoreductase activity
E	0030497	biological_process	fatty acid elongation
E	0046677	biological_process	response to antibiotic
E	0050343	molecular_function	trans-2-enoyl-CoA reductase (NADH) activity
E	0070403	molecular_function	NAD+ binding
E	0071768	biological_process	mycolic acid biosynthetic process
G	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
G	0005504	molecular_function	fatty acid binding
G	0005886	cellular_component	plasma membrane
G	0006633	biological_process	fatty acid biosynthetic process
G	0009274	cellular_component	peptidoglycan-based cell wall
G	0016491	molecular_function	oxidoreductase activity
G	0030497	biological_process	fatty acid elongation
G	0046677	biological_process	response to antibiotic
G	0050343	molecular_function	trans-2-enoyl-CoA reductase (NADH) activity
G	0070403	molecular_function	NAD+ binding
G	0071768	biological_process	mycolic acid biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	25
Details	binding site for residue NAD A 301

Chain	Residue
A	GLY14
A	SER94
A	ILE95
A	GLY96
A	ILE122
A	MET147
A	ASP148
A	MET161
A	LYS165
A	GLY192
A	PRO193
A	ILE15
A	ILE194
A	THR196
A	LEU197
A	ALA198
A	XT5302
A	HOH405
A	ILE16
A	SER20
A	ILE21
A	PHE41
A	LEU63
A	ASP64
A	VAL65

site_id	AC2
Number of Residues	10
Details	binding site for residue XT5 A 302

Chain	Residue
A	GLY96
A	PHE97
A	MET103
A	PHE149
A	PRO156
A	TYR158
A	ALA198
A	MET199
A	GLN214
A	NAD301

site_id	AC3
Number of Residues	11
Details	binding site for residue XT5 A 303

Chain	Residue
A	THR17
A	LEU46
A	LEU197
A	SER200
C	ILE16
C	THR17
C	ARG43
C	LEU46
C	LEU197
C	SER200
C	ALA206

site_id	AC4
Number of Residues	2
Details	binding site for residue CL A 304

Chain	Residue
A	ILE105
A	GLY204

site_id	AC5
Number of Residues	3
Details	binding site for residue CL A 305

Chain	Residue
A	ARG195
A	MET232
A	LYS233

site_id	AC6
Number of Residues	5
Details	binding site for residue CL A 306

Chain	Residue
A	ARG43
A	LEU44
A	ARG45
A	LEU46
C	LYS233

site_id	AC7
Number of Residues	25
Details	binding site for residue NAD B 301

Chain	Residue
B	GLY14
B	ILE15
B	ILE16
B	SER20
B	ILE21
B	PHE41
B	LEU63
B	ASP64
B	VAL65
B	SER94
B	ILE95
B	GLY96
B	ILE122
B	MET147
B	ASP148
B	LYS165
B	ALA191
B	GLY192
B	PRO193
B	ILE194
B	THR196
B	ALA198
B	XT5302
B	HOH408
B	HOH418

site_id	AC8
Number of Residues	12
Details	binding site for residue XT5 B 302

Chain	Residue
B	GLY96
B	PHE97
B	MET98
B	MET103
B	PHE149
B	ALA157
B	TYR158
B	ALA198
B	MET199
B	VAL203
B	LEU218
B	NAD301

site_id	AC9
Number of Residues	3
Details	binding site for residue CL B 303

Chain	Residue
B	LEU61
B	GLU62
B	ARG77

site_id	AD1
Number of Residues	4
Details	binding site for residue NA B 304

Chain	Residue
B	HOH434
B	ASP223
B	GLN224
B	ALA226

site_id	AD2
Number of Residues	26
Details	binding site for residue NAD E 301

Chain	Residue
E	GLY14
E	ILE15
E	ILE16
E	SER20
E	ILE21
E	PHE41
E	LEU63
E	ASP64
E	VAL65
E	SER94
E	ILE95
E	GLY96
E	ILE122
E	MET147
E	ASP148
E	PHE149
E	LYS165
E	ALA191
E	GLY192
E	PRO193
E	ILE194
E	THR196
E	ALA198
E	XT5302
E	HOH414
E	HOH418

site_id	AD3
Number of Residues	11
Details	binding site for residue XT5 E 302

Chain	Residue
E	GLY96
E	MET103
E	PHE149
E	PRO156
E	TYR158
E	ALA198
E	ILE202
E	VAL203
E	GLN214
E	LEU218
E	NAD301

site_id	AD4
Number of Residues	26
Details	binding site for residue NAD G 301

Chain	Residue
G	GLY14
G	ILE15
G	ILE16
G	SER20
G	ILE21
G	PHE41
G	LEU63
G	ASP64
G	VAL65
G	SER94
G	ILE95
G	GLY96
G	ILE122
G	MET147
G	ASP148
G	LYS165
G	GLY192
G	PRO193
G	ILE194
G	THR196
G	ALA198
G	XT5302
G	HOH402
G	HOH403
G	HOH418
G	HOH427

site_id	AD5
Number of Residues	10
Details	binding site for residue XT5 G 302

Chain	Residue
G	GLY96
G	MET103
G	PHE149
G	ALA157
G	TYR158
G	ALA198
G	GLN214
G	LEU217
G	LEU218
G	NAD301

site_id	AD6
Number of Residues	1
Details	binding site for residue CL G 303

Chain	Residue
G	LYS240

site_id	AD7
Number of Residues	2
Details	binding site for residue CL G 304

Chain	Residue
A	ARG177
G	ARG225

site_id	AD8
Number of Residues	26
Details	binding site for residue NAD C 301

Chain	Residue
C	GLY14
C	ILE15
C	ILE16
C	SER20
C	ILE21
C	PHE41
C	LEU63
C	ASP64
C	VAL65
C	SER94
C	ILE95
C	GLY96
C	ILE122
C	MET147
C	ASP148
C	LYS165
C	GLY192
C	PRO193
C	ILE194
C	THR196
C	LEU197
C	ALA198
C	XT5302
C	HOH402
C	HOH413
C	HOH418

site_id	AD9
Number of Residues	12
Details	binding site for residue XT5 C 302

Chain	Residue
C	GLY96
C	PHE97
C	MET103
C	PHE149
C	PRO156
C	ALA157
C	TYR158
C	ALA198
C	MET199
C	ILE202
C	GLN214
C	NAD301

site_id	AE1
Number of Residues	4
Details	binding site for residue CL C 303

Chain	Residue
A	ARG43
C	ARG195
C	MET199
C	SER200

site_id	AE2
Number of Residues	3
Details	binding site for residue CL C 304

Chain	Residue
C	LEU61
C	GLU62
C	ARG77

site_id	AE3
Number of Residues	1
Details	binding site for residue CL C 305

Chain	Residue
D	PRO237

site_id	AE4
Number of Residues	25
Details	binding site for residue NAD D 301

Chain	Residue
D	GLY14
D	ILE15
D	ILE16
D	SER20
D	ILE21
D	PHE41
D	LEU63
D	ASP64
D	VAL65
D	SER94
D	ILE95
D	GLY96
D	ILE122
D	MET147
D	ASP148
D	MET161
D	LYS165
D	ALA191
D	GLY192
D	PRO193
D	ILE194
D	THR196
D	ALA198
D	XT5302
D	HOH407

site_id	AE5
Number of Residues	8
Details	binding site for residue XT5 D 302

Chain	Residue
D	GLY96
D	PHE97
D	MET103
D	PHE149
D	TYR158
D	ALA198
D	GLN214
D	NAD301

site_id	AE6
Number of Residues	3
Details	binding site for residue CL D 303

Chain	Residue
D	ASP150
D	ALA191
D	HOH408

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	30
Details	BINDING: BINDING => ECO:0000269\|PubMed:10336454, ECO:0000269\|PubMed:16647717, ECO:0000269\|PubMed:7886450, ECO:0007744\|PDB:1BVR, ECO:0007744\|PDB:1ENY, ECO:0007744\|PDB:2AQ8

Chain	Residue	Details
A	SER20
B	ILE194
E	SER20
E	ASP64
E	ILE95
E	LYS165
E	ILE194
G	SER20
G	ASP64
G	ILE95
G	LYS165
A	ASP64
G	ILE194
C	SER20
C	ASP64
C	ILE95
C	LYS165
C	ILE194
D	SER20
D	ASP64
D	ILE95
D	LYS165
A	ILE95
D	ILE194
A	LYS165
A	ILE194
B	SER20
B	ASP64
B	ILE95
B	LYS165

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269\|PubMed:10336454

Chain	Residue	Details
A	TYR158
B	TYR158
E	TYR158
G	TYR158
C	TYR158
D	TYR158

site_id	SWS_FT_FI3
Number of Residues	6
Details	SITE: May act as an intermediate that passes the hydride ion from NADH to the substrate => ECO:0000305\|PubMed:10336454

Chain	Residue	Details
A	PHE149
B	PHE149
E	PHE149
G	PHE149
C	PHE149
D	PHE149

site_id	SWS_FT_FI4
Number of Residues	6
Details	SITE: Transition state stabilizer => ECO:0000305\|PubMed:10521269

Chain	Residue	Details
A	TYR158
B	TYR158
E	TYR158
G	TYR158
C	TYR158
D	TYR158

site_id	SWS_FT_FI5
Number of Residues	6
Details	MOD_RES: Phosphothreonine => ECO:0000269\|PubMed:20864541, ECO:0000269\|PubMed:21143326

Chain	Residue	Details
A	THR266
B	THR266
E	THR266
G	THR266
C	THR266
D	THR266

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)