Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5VRN

CRYSTAL STRUCTURE OF THE INHA FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH AN12855, EBSI 4333.

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	27
Details	binding site for residue 9JM A 300

Chain	Residue
A	GLY14
A	SER94
A	ILE95
A	GLY96
A	ILE122
A	MET147
A	ASP148
A	PHE149
A	TYR158
A	LYS165
A	ALA191
A	ILE15
A	PRO193
A	ILE194
A	THR196
A	MET199
A	LEU218
A	GLU219
A	HOH423
A	HOH430
A	ILE16
A	SER20
A	ILE21
A	PHE41
A	LEU63
A	ASP64
A	VAL65

site_id	AC2
Number of Residues	26
Details	binding site for residue 9JM B 300

Chain	Residue
B	GLY14
B	ILE16
B	SER20
B	ILE21
B	PHE41
B	LEU63
B	ASP64
B	VAL65
B	SER94
B	ILE95
B	GLY96
B	MET147
B	ASP148
B	PHE149
B	TYR158
B	LYS165
B	ALA191
B	GLY192
B	PRO193
B	ILE194
B	THR196
B	MET199
B	LEU218
B	GLU219
B	HOH401
B	HOH414

site_id	AC3
Number of Residues	29
Details	binding site for residue 9JM C 300

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	TYR158
C	MET161
C	LYS165
C	ALA191
C	PRO193
C	ILE194
C	THR196
C	MET199
C	ILE215
C	LEU218
C	GLU219
C	HOH412
C	HOH415

site_id	AC4
Number of Residues	21
Details	binding site for residue 9JM D 300

Chain	Residue
D	PRO193
D	ILE194
D	THR196
D	HOH406
D	GLY14
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

site_id	AC5
Number of Residues	21
Details	binding site for residue 9JM E 300

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	PRO193
E	ILE194
E	THR196
E	HOH401

site_id	AC6
Number of Residues	22
Details	binding site for residue 9JM F 300

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	LYS165
F	ALA191
F	GLY192
F	PRO193
F	ILE194
F	THR196

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)