Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4TRM

Structure of the apo form of InhA from Mycobacterium tuberculosis

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
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	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	2
Details	binding site for residue MES A 301

Chain	Residue
A	LYS181
A	TYR182

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
B	ILE194
C	ASP64
C	ILE95
C	LYS165
C	ILE194
D	SER20
D	ASP64
D	ILE95
D	LYS165
D	ILE194
E	SER20
E	ASP64
E	ILE95
E	LYS165
E	ILE194
F	SER20
F	ASP64
F	ILE95
F	LYS165
F	ILE194
A	ASP64
A	ILE95
A	LYS165
A	ILE194
B	SER20
B	ASP64
B	ILE95
B	LYS165
A	SER20
C	SER20

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

Chain	Residue	Details
A	TYR158
B	TYR158
C	TYR158
D	TYR158
E	TYR158
F	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
C	PHE149
D	PHE149
E	PHE149
F	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
C	TYR158
D	TYR158
E	TYR158
F	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
C	THR266
D	THR266
E	THR266
F	THR266

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