Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5MTP

Crystal structure of M. tuberculosis InhA inhibited by PT514

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
A	0006633	biological_process	fatty acid biosynthetic process
A	0016491	molecular_function	oxidoreductase activity
A	0046677	biological_process	response to antibiotic
A	0050343	molecular_function	trans-2-enoyl-CoA reductase (NADH) activity
B	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
B	0006633	biological_process	fatty acid biosynthetic process
B	0016491	molecular_function	oxidoreductase activity
B	0046677	biological_process	response to antibiotic
B	0050343	molecular_function	trans-2-enoyl-CoA reductase (NADH) activity
C	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
C	0006633	biological_process	fatty acid biosynthetic process
C	0016491	molecular_function	oxidoreductase activity
C	0046677	biological_process	response to antibiotic
C	0050343	molecular_function	trans-2-enoyl-CoA reductase (NADH) activity
D	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
D	0006633	biological_process	fatty acid biosynthetic process
D	0016491	molecular_function	oxidoreductase activity
D	0046677	biological_process	response to antibiotic
D	0050343	molecular_function	trans-2-enoyl-CoA reductase (NADH) activity
E	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
E	0006633	biological_process	fatty acid biosynthetic process
E	0016491	molecular_function	oxidoreductase activity
E	0046677	biological_process	response to antibiotic
E	0050343	molecular_function	trans-2-enoyl-CoA reductase (NADH) activity
F	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
F	0006633	biological_process	fatty acid biosynthetic process
F	0016491	molecular_function	oxidoreductase activity
F	0046677	biological_process	response to antibiotic
F	0050343	molecular_function	trans-2-enoyl-CoA reductase (NADH) activity
G	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
G	0006633	biological_process	fatty acid biosynthetic process
G	0016491	molecular_function	oxidoreductase activity
G	0046677	biological_process	response to antibiotic
G	0050343	molecular_function	trans-2-enoyl-CoA reductase (NADH) activity
H	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
H	0006633	biological_process	fatty acid biosynthetic process
H	0016491	molecular_function	oxidoreductase activity
H	0046677	biological_process	response to antibiotic
H	0050343	molecular_function	trans-2-enoyl-CoA reductase (NADH) activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	33
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	PHE149
A	LYS165
A	ALA191
A	GLY192
A	ILE15
A	PRO193
A	ILE194
A	THR196
A	ALA198
A	53K302
A	HOH426
A	HOH427
A	HOH429
A	HOH463
A	HOH467
A	ILE16
A	HOH472
A	HOH476
A	HOH477
A	HOH522
A	SER20
A	ILE21
A	PHE41
A	LEU63
A	ASP64
A	VAL65

site_id	AC2
Number of Residues	12
Details	binding site for residue 53K A 302

Chain	Residue
A	GLY96
A	PHE97
A	MET103
A	PHE149
A	MET155
A	PRO156
A	TYR158
A	MET161
A	ALA198
A	GLN214
A	LEU218
A	NAD301

site_id	AC3
Number of Residues	2
Details	binding site for residue CL A 303

Chain	Residue
A	PRO237
A	HOH408

site_id	AC4
Number of Residues	31
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	53K302
B	HOH402
B	HOH412
B	HOH418
B	HOH448
B	HOH458
B	HOH463
B	HOH476
B	HOH507

site_id	AC5
Number of Residues	14
Details	binding site for residue 53K B 302

Chain	Residue
B	GLY96
B	PHE97
B	MET103
B	PHE149
B	MET155
B	PRO156
B	TYR158
B	MET161
B	ALA198
B	MET199
B	ILE202
B	GLN214
B	NAD301
B	HOH470

site_id	AC6
Number of Residues	32
Details	binding site for residue NAD E 301

Chain	Residue
E	ASP64
E	VAL65
E	SER94
E	ILE95
E	GLY96
E	ILE122
E	MET147
E	ASP148
E	LYS165
E	ALA191
E	GLY192
E	PRO193
E	ILE194
E	THR196
E	LEU197
E	ALA198
E	53K302
E	HOH405
E	HOH410
E	HOH452
E	HOH454
E	HOH460
E	HOH478
E	HOH483
E	HOH485
E	GLY14
E	ILE15
E	ILE16
E	SER20
E	ILE21
E	PHE41
E	LEU63

site_id	AC7
Number of Residues	13
Details	binding site for residue 53K E 302

Chain	Residue
E	GLY96
E	PHE97
E	PHE149
E	MET155
E	PRO156
E	TYR158
E	ALA198
E	MET199
E	VAL203
E	GLN214
E	LEU217
E	LEU218
E	NAD301

site_id	AC8
Number of Residues	32
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	PHE149
G	LYS165
G	ALA191
G	GLY192
G	PRO193
G	ILE194
G	THR196
G	LEU197
G	ALA198
G	53K302
G	HOH408
G	HOH418
G	HOH442
G	HOH474
G	HOH484
G	HOH486
G	HOH492

site_id	AC9
Number of Residues	12
Details	binding site for residue 53K G 302

Chain	Residue
G	GLY96
G	PHE97
G	MET103
G	PHE149
G	MET155
G	PRO156
G	TYR158
G	MET161
G	ALA198
G	ILE202
G	GLN214
G	NAD301

site_id	AD1
Number of Residues	30
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	PHE149
C	LYS165
C	PRO193
C	ILE194
C	THR196
C	ALA198
C	53K302
C	HOH408
C	HOH421
C	HOH445
C	HOH459
C	HOH469
C	HOH483
C	HOH490
C	HOH513

site_id	AD2
Number of Residues	11
Details	binding site for residue 53K C 302

Chain	Residue
C	GLY96
C	PHE97
C	MET98
C	MET103
C	PHE149
C	PRO156
C	TYR158
C	ALA198
C	VAL203
C	GLN214
C	NAD301

site_id	AD3
Number of Residues	3
Details	binding site for residue CL C 303

Chain	Residue
C	LEU61
C	GLU62
C	ARG77

site_id	AD4
Number of Residues	31
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	LYS165
D	ALA191
D	GLY192
D	PRO193
D	ILE194
D	THR196
D	ALA198
D	53K302
D	HOH410
D	HOH433
D	HOH456
D	HOH471
D	HOH489
D	HOH497
D	HOH519
D	HOH534

site_id	AD5
Number of Residues	13
Details	binding site for residue 53K D 302

Chain	Residue
D	GLY96
D	PHE97
D	MET103
D	PHE149
D	MET155
D	PRO156
D	TYR158
D	MET161
D	ALA198
D	MET199
D	ILE202
D	GLN214
D	NAD301

site_id	AD6
Number of Residues	6
Details	binding site for residue NA D 303

Chain	Residue
D	GLN100
D	MET103
D	ASN106
D	HOH408
D	HOH531
D	HOH553

site_id	AD7
Number of Residues	30
Details	binding site for residue NAD F 301

Chain	Residue
F	GLY14
F	ILE15
F	ILE16
F	SER20
F	ILE21
F	PHE41
F	LEU63
F	ASP64
F	VAL65
F	SER94
F	ILE95
F	GLY96
F	ILE122
F	MET147
F	ASP148
F	LYS165
F	ALA191
F	GLY192
F	PRO193
F	ILE194
F	THR196
F	ALA198
F	53K302
F	HOH405
F	HOH440
F	HOH451
F	HOH454
F	HOH469
F	HOH489
F	HOH503

site_id	AD8
Number of Residues	13
Details	binding site for residue 53K F 302

Chain	Residue
F	GLY96
F	PHE97
F	MET103
F	PHE149
F	MET155
F	PRO156
F	TYR158
F	MET161
F	ALA198
F	MET199
F	ILE202
F	GLN214
F	NAD301

site_id	AD9
Number of Residues	6
Details	binding site for residue NA F 303

Chain	Residue
F	GLN100
F	MET103
F	ASN106
F	HOH446
F	HOH517
F	HOH526

site_id	AE1
Number of Residues	32
Details	binding site for residue NAD H 301

Chain	Residue
H	GLY14
H	ILE15
H	ILE16
H	SER20
H	ILE21
H	PHE41
H	LEU63
H	ASP64
H	VAL65
H	SER94
H	ILE95
H	GLY96
H	ILE122
H	MET147
H	ASP148
H	LYS165
H	ALA191
H	GLY192
H	PRO193
H	ILE194
H	THR196
H	LEU197
H	ALA198
H	53K302
H	HOH409
H	HOH440
H	HOH451
H	HOH457
H	HOH465
H	HOH482
H	HOH497
H	HOH523

site_id	AE2
Number of Residues	13
Details	binding site for residue 53K H 302

Chain	Residue
H	GLY96
H	PHE97
H	MET103
H	PHE149
H	MET155
H	PRO156
H	TYR158
H	MET161
H	ALA198
H	MET199
H	ILE202
H	GLN214
H	NAD301

site_id	AE3
Number of Residues	6
Details	binding site for residue NA H 303

Chain	Residue
H	GLN100
H	MET103
H	ASN106
H	HOH417
H	HOH526
H	HOH531

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	48
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P9WGR1

Chain	Residue	Details
A	SER20
B	TYR158
B	LYS165
B	ILE194
E	SER20
E	ASP64
E	ILE95
E	TYR158
E	LYS165
E	ILE194
G	SER20
A	ASP64
G	ASP64
G	ILE95
G	TYR158
G	LYS165
G	ILE194
C	SER20
C	ASP64
C	ILE95
C	TYR158
C	LYS165
A	ILE95
C	ILE194
D	SER20
D	ASP64
D	ILE95
D	TYR158
D	LYS165
D	ILE194
F	SER20
F	ASP64
F	ILE95
A	TYR158
F	TYR158
F	LYS165
F	ILE194
H	SER20
H	ASP64
H	ILE95
H	TYR158
H	LYS165
H	ILE194
A	LYS165
A	ILE194
B	SER20
B	ASP64
B	ILE95

site_id	SWS_FT_FI2
Number of Residues	8
Details	SITE: May act as an intermediate that passes the hydride ion from NADH to the substrate => ECO:0000250\|UniProtKB:P9WGR1

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

site_id	SWS_FT_FI3
Number of Residues	8
Details	SITE: Transition state stabilizer => ECO:0000250\|UniProtKB:P9WGR1

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

site_id	SWS_FT_FI4
Number of Residues	8
Details	MOD_RES: Phosphothreonine => ECO:0000250\|UniProtKB:P9WGR1

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

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