5CPF

Compensation of the effect of isoleucine to alanine mutation by designed inhibition in the InhA enzyme

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	23
Details	binding site for residue NAD A 300

Chain	Residue
A	GLY14
A	SER94
A	ILE95
A	GLY96
A	ILE122
A	MET147
A	ASP148
A	LYS165
A	ALA191
A	GLY192
A	PRO193
A	ILE15
A	ILE194
A	THR196
A	ALA198
A	53K301
A	ILE16
A	SER20
A	ILE21
A	PHE41
A	LEU63
A	ASP64
A	VAL65

---

site_id	AC2
Number of Residues	9
Details	binding site for residue 53K A 301

Chain	Residue
A	GLY96
A	PHE97
A	MET98
A	MET103
A	PRO156
A	ALA157
A	TYR158
A	MET199
A	NAD300

---

site_id	AC3
Number of Residues	25
Details	binding site for residue NAD B 300

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	MET161
B	LYS165
B	ALA191
B	GLY192
B	PRO193
B	ILE194
B	THR196
B	ALA198
B	53K301

---

site_id	AC4
Number of Residues	14
Details	binding site for residue 53K B 301

Chain	Residue
B	GLY96
B	PHE97
B	MET98
B	PHE149
B	MET155
B	PRO156
B	ALA157
B	TYR158
B	MET161
B	PRO193
B	ALA198
B	MET199
B	LEU218
B	NAD300

---

site_id	AC5
Number of Residues	23
Details	binding site for residue NAD 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	MET161
C	LYS165
C	ALA191
C	GLY192
C	PRO193
C	ILE194
C	THR196
C	53K301

---

site_id	AC6
Number of Residues	12
Details	binding site for residue 53K C 301

Chain	Residue
C	PRO156
C	ALA157
C	TYR158
C	MET161
C	PRO193
C	LEU218
C	NAD300
C	GLY96
C	PHE97
C	MET98
C	MET103
C	PHE149

---

site_id	AC7
Number of Residues	10
Details	binding site for residue 53K D 301

Chain	Residue
D	GLY96
D	PHE97
D	MET98
D	PRO156
D	TYR158
D	MET161
D	ALA198
D	MET199
D	ILE202
D	NAD302

---

site_id	AC8
Number of Residues	22
Details	binding site for residue NAD D 302

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	GLY192
D	PRO193
D	ILE194
D	THR196
D	ALA198
D	53K301

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P9WGR1

Chain	Residue	Details
A	SER20
B	TYR158
B	LYS165
B	ILE194
C	SER20
C	ASP64
C	ILE95
C	TYR158
C	LYS165
C	ILE194
D	SER20
A	ASP64
D	ASP64
D	ILE95
D	TYR158
D	LYS165
D	ILE194
A	ILE95
A	TYR158
A	LYS165
A	ILE194
B	SER20
B	ASP64
B	ILE95

---

site_id	SWS_FT_FI2
Number of Residues	4
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
C	PHE149
D	PHE149

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	SITE: Transition state stabilizer => ECO:0000250|UniProtKB:P9WGR1

Chain	Residue	Details
A	TYR158
B	TYR158
C	TYR158
D	TYR158

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P9WGR1

Chain	Residue	Details
A	THR266
B	THR266
C	THR266
D	THR266

---