Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6R9W

Crystal structure of InhA in complex with AP-124 inhibitor

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	0030497	biological_process	fatty acid elongation
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	0030497	biological_process	fatty acid elongation
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	0030497	biological_process	fatty acid elongation
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	0030497	biological_process	fatty acid elongation
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	0030497	biological_process	fatty acid elongation
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	0030497	biological_process	fatty acid elongation
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	11
Details	binding site for residue JVZ A 301

Chain	Residue
A	GLN100
A	LEU218
A	HOH536
A	MET103
A	MET155
A	PRO156
A	TYR158
A	ALA198
A	ILE202
A	LEU207
A	ILE215

site_id	AC2
Number of Residues	33
Details	binding site for residue NAD A 302

Chain	Residue
A	GLY14
A	ILE15
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	ALA191
A	GLY192
A	PRO193
A	ILE194
A	THR196
A	HOH411
A	HOH430
A	HOH435
A	HOH439
A	HOH464
A	HOH487
A	HOH518
A	HOH522
A	HOH542
A	HOH551
A	HOH552

site_id	AC3
Number of Residues	27
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	HOH408
B	HOH413
B	HOH475
B	HOH487
B	HOH518
B	HOH528

site_id	AC4
Number of Residues	37
Details	binding site for residue NAD C 301

Chain	Residue
C	HOH462
C	HOH464
C	HOH481
C	HOH506
C	HOH507
C	HOH515
C	HOH517
C	HOH520
C	HOH523
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	ALA191
C	GLY192
C	PRO193
C	ILE194
C	THR196
C	HOH402
C	HOH410
C	HOH414
C	HOH419
C	HOH433
C	HOH451

site_id	AC5
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	PHE149
D	LYS165
D	ALA191
D	GLY192
D	PRO193
D	ILE194
D	THR196
D	HOH407
D	HOH424
D	HOH427
D	HOH437
D	HOH458
D	HOH466
D	HOH468
D	HOH501
D	HOH515

site_id	AC6
Number of Residues	26
Details	binding site for residue NAD E 301

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	GLY192
E	PRO193
E	ILE194
E	THR196
E	HOH423
E	HOH424
E	HOH443
E	HOH478
E	HOH489

site_id	AC7
Number of Residues	24
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	HOH409
F	HOH426
F	HOH457
F	HOH462

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

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