Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2B37

Crystal structure of Mycobacterium tuberculosis enoyl reductase (InhA) inhibited by 5-octyl-2-phenoxyphenol

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	0006629	biological_process	lipid metabolic process
A	0006631	biological_process	fatty acid metabolic process
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	0006629	biological_process	lipid metabolic process
B	0006631	biological_process	fatty acid metabolic process
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	0006629	biological_process	lipid metabolic process
C	0006631	biological_process	fatty acid metabolic process
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	0006629	biological_process	lipid metabolic process
D	0006631	biological_process	fatty acid metabolic process
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	0006629	biological_process	lipid metabolic process
E	0006631	biological_process	fatty acid metabolic process
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
F	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
F	0005504	molecular_function	fatty acid binding
F	0005886	cellular_component	plasma membrane
F	0006629	biological_process	lipid metabolic process
F	0006631	biological_process	fatty acid metabolic process
F	0006633	biological_process	fatty acid biosynthetic process
F	0009274	cellular_component	peptidoglycan-based cell wall
F	0016491	molecular_function	oxidoreductase activity
F	0030497	biological_process	fatty acid elongation
F	0046677	biological_process	response to antibiotic
F	0050343	molecular_function	trans-2-enoyl-CoA reductase (NADH) activity
F	0070403	molecular_function	NAD+ binding
F	0071768	biological_process	mycolic acid biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE 8PS C 300

Chain	Residue
C	GLY96
C	PHE97
C	MET103
C	MET155
C	PRO156
C	TYR158
C	MET161
C	LEU218
C	NAD403

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE 8PS D 301

Chain	Residue
D	GLY96
D	PHE97
D	MET103
D	PHE149
D	MET155
D	PRO156
D	TYR158
D	MET161
D	LEU218
D	NAD404

site_id	AC3
Number of Residues	19
Details	BINDING SITE FOR RESIDUE NAD A 401

Chain	Residue
A	GLY14
A	ILE16
A	SER20
A	ILE21
A	PHE41
A	LEU63
A	ASP64
A	VAL65
A	SER94
A	ILE95
A	GLY96
A	ILE122
A	MET147
A	ASP148
A	PHE149
A	LYS165
A	GLY192
A	PRO193
A	ILE194

site_id	AC4
Number of Residues	23
Details	BINDING SITE FOR RESIDUE NAD B 402

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	PHE149
B	TYR158
B	LYS165
B	ALA191
B	GLY192
B	PRO193
B	ILE194
B	THR196

site_id	AC5
Number of Residues	23
Details	BINDING SITE FOR RESIDUE NAD C 403

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	GLY192
C	PRO193
C	ILE194
C	THR196
C	8PS300
C	HOH404

site_id	AC6
Number of Residues	22
Details	BINDING SITE FOR RESIDUE NAD D 404

Chain	Residue
D	MET161
D	LYS165
D	GLY192
D	PRO193
D	ILE194
D	THR196
D	8PS301
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

site_id	AC7
Number of Residues	20
Details	BINDING SITE FOR RESIDUE NAD E 405

Chain	Residue
E	GLY14
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	PRO193
E	ILE194
E	THR196

site_id	AC8
Number of Residues	24
Details	BINDING SITE FOR RESIDUE NAD F 406

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	PHE149
F	TYR158
F	LYS165
F	ALA191
F	PRO193
F	ILE194
F	THR196
F	LEU197
F	MET199

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	30
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10336454","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16647717","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7886450","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BVR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ENY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2AQ8","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10336454","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	6
Details	Site: {"description":"May act as an intermediate that passes the hydride ion from NADH to the substrate","evidences":[{"source":"PubMed","id":"10336454","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	6
Details	Site: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"10521269","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	6
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"20864541","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21143326","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
A	TYR158
A	LYS165

site_id	CSA10
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
D	MET161
D	LYS165

site_id	CSA11
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
E	MET161
E	LYS165

site_id	CSA12
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
F	MET161
F	LYS165

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
B	TYR158
B	LYS165

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
C	TYR158
C	LYS165

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
D	TYR158
D	LYS165

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
E	TYR158
E	LYS165

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
F	TYR158
F	LYS165

site_id	CSA7
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
A	MET161
A	LYS165

site_id	CSA8
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
B	MET161
B	LYS165

site_id	CSA9
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
C	MET161
C	LYS165

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