Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6TBB

Crystal structure of S. aureus FabI in complex with NADPH and kalimantacin A (batumin)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
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	0030497	biological_process	fatty acid elongation
A	0042802	molecular_function	identical protein binding
A	0050661	molecular_function	NADP binding
A	0141148	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADPH) activity
B	0000166	molecular_function	nucleotide binding
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	0030497	biological_process	fatty acid elongation
B	0042802	molecular_function	identical protein binding
B	0050661	molecular_function	NADP binding
B	0141148	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADPH) activity
C	0000166	molecular_function	nucleotide binding
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	0030497	biological_process	fatty acid elongation
C	0042802	molecular_function	identical protein binding
C	0050661	molecular_function	NADP binding
C	0141148	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADPH) activity
D	0000166	molecular_function	nucleotide binding
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	0030497	biological_process	fatty acid elongation
D	0042802	molecular_function	identical protein binding
D	0050661	molecular_function	NADP binding
D	0141148	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADPH) activity
E	0000166	molecular_function	nucleotide binding
E	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
E	0006633	biological_process	fatty acid biosynthetic process
E	0016491	molecular_function	oxidoreductase activity
E	0030497	biological_process	fatty acid elongation
E	0042802	molecular_function	identical protein binding
E	0050661	molecular_function	NADP binding
E	0141148	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADPH) activity
F	0000166	molecular_function	nucleotide binding
F	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
F	0006633	biological_process	fatty acid biosynthetic process
F	0016491	molecular_function	oxidoreductase activity
F	0030497	biological_process	fatty acid elongation
F	0042802	molecular_function	identical protein binding
F	0050661	molecular_function	NADP binding
F	0141148	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADPH) activity
G	0000166	molecular_function	nucleotide binding
G	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
G	0006633	biological_process	fatty acid biosynthetic process
G	0016491	molecular_function	oxidoreductase activity
G	0030497	biological_process	fatty acid elongation
G	0042802	molecular_function	identical protein binding
G	0050661	molecular_function	NADP binding
G	0141148	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADPH) activity
H	0000166	molecular_function	nucleotide binding
H	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
H	0006633	biological_process	fatty acid biosynthetic process
H	0016491	molecular_function	oxidoreductase activity
H	0030497	biological_process	fatty acid elongation
H	0042802	molecular_function	identical protein binding
H	0050661	molecular_function	NADP binding
H	0141148	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADPH) activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	26
Details	binding site for residue NDP A 301

Chain	Residue
A	GLY13
A	ASP66
A	VAL67
A	SER93
A	ILE94
A	ALA95
A	ILE120
A	THR145
A	THR146
A	TYR147
A	LYS164
A	ILE14
A	ALA190
A	PRO192
A	ILE193
A	THR195
A	LEU196
A	SER197
A	KAL302
A	ALA15
A	SER19
A	ILE20
A	ARG40
A	LYS41
A	SER44
A	ILE65

site_id	AC2
Number of Residues	10
Details	binding site for residue KAL A 302

Chain	Residue
A	ALA95
A	PHE96
A	ALA97
A	GLN155
A	ASN156
A	TYR157
A	LYS164
A	SER197
A	VAL201
A	NDP301

site_id	AC3
Number of Residues	26
Details	binding site for residue NDP B 301

Chain	Residue
B	GLY13
B	ILE14
B	ALA15
B	SER19
B	ILE20
B	ARG40
B	LYS41
B	ARG43
B	SER44
B	ILE65
B	ASP66
B	VAL67
B	SER93
B	ILE94
B	ALA95
B	ILE120
B	THR145
B	THR146
B	LYS164
B	ALA190
B	GLY191
B	PRO192
B	ILE193
B	THR195
B	SER197
B	KAL302

site_id	AC4
Number of Residues	10
Details	binding site for residue KAL B 302

Chain	Residue
B	ALA95
B	PHE96
B	ALA97
B	GLN155
B	ASN156
B	TYR157
B	SER197
B	VAL201
B	ILE207
B	NDP301

site_id	AC5
Number of Residues	26
Details	binding site for residue NDP C 301

Chain	Residue
C	GLY13
C	ILE14
C	ALA15
C	SER19
C	ILE20
C	ARG40
C	LYS41
C	SER44
C	ILE65
C	ASP66
C	VAL67
C	SER93
C	ILE94
C	ALA95
C	ILE120
C	THR145
C	THR146
C	LYS164
C	ALA190
C	GLY191
C	PRO192
C	ILE193
C	THR195
C	LEU196
C	SER197
C	KAL302

site_id	AC6
Number of Residues	11
Details	binding site for residue KAL C 302

Chain	Residue
C	PHE96
C	ALA97
C	MET99
C	TYR147
C	GLN155
C	ASN156
C	TYR157
C	SER197
C	VAL201
C	NDP301
C	ALA95

site_id	AC7
Number of Residues	26
Details	binding site for residue NDP D 301

Chain	Residue
D	GLY13
D	ILE14
D	ALA15
D	SER19
D	ILE20
D	ARG40
D	LYS41
D	ARG43
D	SER44
D	ILE65
D	ASP66
D	VAL67
D	SER93
D	ILE94
D	ALA95
D	THR145
D	THR146
D	LYS164
D	ALA190
D	GLY191
D	PRO192
D	ILE193
D	THR195
D	LEU196
D	SER197
D	KAL302

site_id	AC8
Number of Residues	11
Details	binding site for residue KAL D 302

Chain	Residue
D	ALA95
D	PHE96
D	ALA97
D	LEU102
D	VAL154
D	TYR157
D	LYS164
D	SER197
D	VAL201
D	ILE207
D	NDP301

site_id	AC9
Number of Residues	25
Details	binding site for residue NDP E 301

Chain	Residue
E	GLY13
E	ILE14
E	ALA15
E	SER19
E	ILE20
E	ARG40
E	LYS41
E	SER44
E	ILE65
E	ASP66
E	VAL67
E	SER93
E	ILE94
E	ALA95
E	THR145
E	THR146
E	LYS164
E	ALA190
E	GLY191
E	PRO192
E	ILE193
E	THR195
E	LEU196
E	SER197
E	KAL302

site_id	AD1
Number of Residues	10
Details	binding site for residue KAL E 302

Chain	Residue
E	ALA95
E	PHE96
E	ALA97
E	GLN155
E	ASN156
E	TYR157
E	SER197
E	ALA198
E	VAL201
E	NDP301

site_id	AD2
Number of Residues	26
Details	binding site for residue NDP F 301

Chain	Residue
F	GLY13
F	ILE14
F	ALA15
F	SER19
F	ILE20
F	ARG40
F	LYS41
F	SER44
F	ILE65
F	ASP66
F	VAL67
F	SER93
F	ILE94
F	ALA95
F	ILE120
F	THR145
F	THR146
F	LYS164
F	ALA190
F	GLY191
F	PRO192
F	ILE193
F	THR195
F	LEU196
F	SER197
F	KAL302

site_id	AD3
Number of Residues	11
Details	binding site for residue KAL F 302

Chain	Residue
F	ALA95
F	PHE96
F	ALA97
F	MET99
F	TYR147
F	GLN155
F	ASN156
F	TYR157
F	SER197
F	VAL201
F	NDP301

site_id	AD4
Number of Residues	26
Details	binding site for residue NDP G 301

Chain	Residue
G	GLY13
G	ILE14
G	ALA15
G	SER19
G	ILE20
G	ARG40
G	LYS41
G	SER44
G	ILE65
G	ASP66
G	VAL67
G	SER93
G	ILE94
G	ALA95
G	ILE120
G	THR145
G	THR146
G	TYR147
G	LYS164
G	ALA190
G	GLY191
G	PRO192
G	ILE193
G	THR195
G	SER197
G	KAL302

site_id	AD5
Number of Residues	11
Details	binding site for residue KAL G 302

Chain	Residue
G	ALA95
G	PHE96
G	ALA97
G	MET99
G	GLN155
G	ASN156
G	TYR157
G	SER197
G	VAL201
G	PHE204
G	NDP301

site_id	AD6
Number of Residues	26
Details	binding site for residue NDP H 301

Chain	Residue
H	GLY13
H	ILE14
H	ALA15
H	SER19
H	ILE20
H	ARG40
H	LYS41
H	SER44
H	ILE65
H	ASP66
H	VAL67
H	SER93
H	ILE94
H	ALA95
H	ILE120
H	THR145
H	THR146
H	TYR147
H	LYS164
H	ALA190
H	GLY191
H	PRO192
H	ILE193
H	THR195
H	SER197
H	KAL302

site_id	AD7
Number of Residues	10
Details	binding site for residue KAL H 302

Chain	Residue
H	ALA95
H	PHE96
H	ALA97
H	MET99
H	GLN155
H	TYR157
H	SER197
H	ALA198
H	VAL201
H	NDP301

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	ACT_SITE: Proton acceptor => ECO:0000250

Chain	Residue	Details
A	TYR147
E	TYR157
F	TYR147
F	TYR157
G	TYR147
G	TYR157
H	TYR147
H	TYR157
A	TYR157
B	TYR147
B	TYR157
C	TYR147
C	TYR157
D	TYR147
D	TYR157
E	TYR147

site_id	SWS_FT_FI2
Number of Residues	56
Details	BINDING: BINDING => ECO:0000269\|PubMed:19768684

Chain	Residue	Details
A	GLY13
B	ARG40
B	ASP66
B	ILE94
B	LYS164
B	ILE193
C	GLY13
C	SER19
C	ARG40
C	ASP66
C	ILE94
A	SER19
C	LYS164
C	ILE193
D	GLY13
D	SER19
D	ARG40
D	ASP66
D	ILE94
D	LYS164
D	ILE193
E	GLY13
A	ARG40
E	SER19
E	ARG40
E	ASP66
E	ILE94
E	LYS164
E	ILE193
F	GLY13
F	SER19
F	ARG40
F	ASP66
A	ASP66
F	ILE94
F	LYS164
F	ILE193
G	GLY13
G	SER19
G	ARG40
G	ASP66
G	ILE94
G	LYS164
G	ILE193
A	ILE94
H	GLY13
H	SER19
H	ARG40
H	ASP66
H	ILE94
H	LYS164
H	ILE193
A	LYS164
A	ILE193
B	GLY13
B	SER19

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	ALA97
B	ALA97
C	ALA97
D	ALA97
E	ALA97
F	ALA97
G	ALA97
H	ALA97

site_id	SWS_FT_FI4
Number of Residues	16
Details	SITE: Critical for cofactor specificity => ECO:0000250

Chain	Residue	Details
A	ARG40
E	LYS41
F	ARG40
F	LYS41
G	ARG40
G	LYS41
H	ARG40
H	LYS41
A	LYS41
B	ARG40
B	LYS41
C	ARG40
C	LYS41
D	ARG40
D	LYS41
E	ARG40

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