Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1I01

CRYSTAL STRUCTURE OF BETA-KETOACYL [ACYL CARRIER PROTEIN] REDUCTASE FROM E. COLI.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004316	molecular_function	3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity
A	0005829	cellular_component	cytosol
A	0006633	biological_process	fatty acid biosynthetic process
A	0008610	biological_process	lipid biosynthetic process
A	0009102	biological_process	biotin biosynthetic process
A	0016491	molecular_function	oxidoreductase activity
A	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A	0030497	biological_process	fatty acid elongation
A	0042802	molecular_function	identical protein binding
A	0046872	molecular_function	metal ion binding
A	0050661	molecular_function	NADP binding
A	0051287	molecular_function	NAD binding
B	0004316	molecular_function	3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity
B	0005829	cellular_component	cytosol
B	0006633	biological_process	fatty acid biosynthetic process
B	0008610	biological_process	lipid biosynthetic process
B	0009102	biological_process	biotin biosynthetic process
B	0016491	molecular_function	oxidoreductase activity
B	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B	0030497	biological_process	fatty acid elongation
B	0042802	molecular_function	identical protein binding
B	0046872	molecular_function	metal ion binding
B	0050661	molecular_function	NADP binding
B	0051287	molecular_function	NAD binding
C	0004316	molecular_function	3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity
C	0005829	cellular_component	cytosol
C	0006633	biological_process	fatty acid biosynthetic process
C	0008610	biological_process	lipid biosynthetic process
C	0009102	biological_process	biotin biosynthetic process
C	0016491	molecular_function	oxidoreductase activity
C	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C	0030497	biological_process	fatty acid elongation
C	0042802	molecular_function	identical protein binding
C	0046872	molecular_function	metal ion binding
C	0050661	molecular_function	NADP binding
C	0051287	molecular_function	NAD binding
D	0004316	molecular_function	3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity
D	0005829	cellular_component	cytosol
D	0006633	biological_process	fatty acid biosynthetic process
D	0008610	biological_process	lipid biosynthetic process
D	0009102	biological_process	biotin biosynthetic process
D	0016491	molecular_function	oxidoreductase activity
D	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D	0030497	biological_process	fatty acid elongation
D	0042802	molecular_function	identical protein binding
D	0046872	molecular_function	metal ion binding
D	0050661	molecular_function	NADP binding
D	0051287	molecular_function	NAD binding
E	0004316	molecular_function	3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity
E	0005829	cellular_component	cytosol
E	0006633	biological_process	fatty acid biosynthetic process
E	0008610	biological_process	lipid biosynthetic process
E	0009102	biological_process	biotin biosynthetic process
E	0016491	molecular_function	oxidoreductase activity
E	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
E	0030497	biological_process	fatty acid elongation
E	0042802	molecular_function	identical protein binding
E	0046872	molecular_function	metal ion binding
E	0050661	molecular_function	NADP binding
E	0051287	molecular_function	NAD binding
F	0004316	molecular_function	3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity
F	0005829	cellular_component	cytosol
F	0006633	biological_process	fatty acid biosynthetic process
F	0008610	biological_process	lipid biosynthetic process
F	0009102	biological_process	biotin biosynthetic process
F	0016491	molecular_function	oxidoreductase activity
F	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
F	0030497	biological_process	fatty acid elongation
F	0042802	molecular_function	identical protein binding
F	0046872	molecular_function	metal ion binding
F	0050661	molecular_function	NADP binding
F	0051287	molecular_function	NAD binding
G	0004316	molecular_function	3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity
G	0005829	cellular_component	cytosol
G	0006633	biological_process	fatty acid biosynthetic process
G	0008610	biological_process	lipid biosynthetic process
G	0009102	biological_process	biotin biosynthetic process
G	0016491	molecular_function	oxidoreductase activity
G	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
G	0030497	biological_process	fatty acid elongation
G	0042802	molecular_function	identical protein binding
G	0046872	molecular_function	metal ion binding
G	0050661	molecular_function	NADP binding
G	0051287	molecular_function	NAD binding
H	0004316	molecular_function	3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity
H	0005829	cellular_component	cytosol
H	0006633	biological_process	fatty acid biosynthetic process
H	0008610	biological_process	lipid biosynthetic process
H	0009102	biological_process	biotin biosynthetic process
H	0016491	molecular_function	oxidoreductase activity
H	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
H	0030497	biological_process	fatty acid elongation
H	0042802	molecular_function	identical protein binding
H	0046872	molecular_function	metal ion binding
H	0050661	molecular_function	NADP binding
H	0051287	molecular_function	NAD binding

Functional Information from PROSITE/UniProt

site_id	PS00061
Number of Residues	29
Details	ADH_SHORT Short-chain dehydrogenases/reductases family signature. SvvgtmgnggQanYAAAKAGLiGFSkSLA

Chain	Residue	Details
A	SER138-ALA166

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	ACT_SITE: Proton acceptor => ECO:0000255\|PROSITE-ProRule:PRU10001

Chain	Residue	Details
A	TYR151
B	TYR151
C	TYR151
D	TYR151
E	TYR151
F	TYR151
G	TYR151
H	TYR151

site_id	SWS_FT_FI2
Number of Residues	32
Details	BINDING: BINDING => ECO:0000269\|PubMed:15016358, ECO:0007744\|PDB:1Q7B, ECO:0007744\|PDB:1Q7C

Chain	Residue	Details
A	GLY12
C	THR37
C	ASN59
C	TYR151
D	GLY12
D	THR37
D	ASN59
D	TYR151
E	GLY12
E	THR37
E	ASN59
A	THR37
E	TYR151
F	GLY12
F	THR37
F	ASN59
F	TYR151
G	GLY12
G	THR37
G	ASN59
G	TYR151
H	GLY12
A	ASN59
H	THR37
H	ASN59
H	TYR151
A	TYR151
B	GLY12
B	THR37
B	ASN59
B	TYR151
C	GLY12

site_id	SWS_FT_FI3
Number of Residues	40
Details	BINDING:

Chain	Residue	Details
A	GLY50
B	THR234
C	GLY50
C	GLY53
C	ASN145
C	GLU233
C	THR234
D	GLY50
D	GLY53
D	ASN145
D	GLU233
A	GLY53
D	THR234
E	GLY50
E	GLY53
E	ASN145
E	GLU233
E	THR234
F	GLY50
F	GLY53
F	ASN145
F	GLU233
A	ASN145
F	THR234
G	GLY50
G	GLY53
G	ASN145
G	GLU233
G	THR234
H	GLY50
H	GLY53
H	ASN145
H	GLU233
A	GLU233
H	THR234
A	THR234
B	GLY50
B	GLY53
B	ASN145
B	GLU233

site_id	SWS_FT_FI4
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:15016358, ECO:0007744\|PDB:1Q7B

Chain	Residue	Details
A	ASN86
B	ASN86
C	ASN86
D	ASN86
E	ASN86
F	ASN86
G	ASN86
H	ASN86

site_id	SWS_FT_FI5
Number of Residues	8
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	SER138
B	SER138
C	SER138
D	SER138
E	SER138
F	SER138
G	SER138
H	SER138

site_id	SWS_FT_FI6
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:15016358

Chain	Residue	Details
A	ILE184
B	ILE184
C	ILE184
D	ILE184
E	ILE184
F	ILE184
G	ILE184
H	ILE184

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1ybv

Chain	Residue	Details
A	LYS155
A	SER138
A	ASN110

site_id	CSA10
Number of Residues	2
Details	Annotated By Reference To The Literature 1ybv

Chain	Residue	Details
E	LYS155
E	GLN148

site_id	CSA11
Number of Residues	1
Details	Annotated By Reference To The Literature 1ybv

Chain	Residue	Details
A	LYS155

site_id	CSA12
Number of Residues	2
Details	Annotated By Reference To The Literature 1ybv

Chain	Residue	Details
B	LYS155
B	TYR151

site_id	CSA13
Number of Residues	2
Details	Annotated By Reference To The Literature 1ybv

Chain	Residue	Details
C	LYS155
C	TYR151

site_id	CSA14
Number of Residues	2
Details	Annotated By Reference To The Literature 1ybv

Chain	Residue	Details
D	LYS155
D	TYR151

site_id	CSA15
Number of Residues	2
Details	Annotated By Reference To The Literature 1ybv

Chain	Residue	Details
E	LYS155
E	TYR151

site_id	CSA16
Number of Residues	1
Details	Annotated By Reference To The Literature 1ybv

Chain	Residue	Details
F	LYS155

site_id	CSA17
Number of Residues	2
Details	Annotated By Reference To The Literature 1ybv

Chain	Residue	Details
G	LYS155
G	TYR151

site_id	CSA18
Number of Residues	2
Details	Annotated By Reference To The Literature 1ybv

Chain	Residue	Details
H	LYS155
H	TYR151

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1ybv

Chain	Residue	Details
B	LYS155
B	SER138
B	TYR151
B	ASN110

site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 1ybv

Chain	Residue	Details
C	LYS155
C	SER138
C	TYR151
C	ASN110

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1ybv

Chain	Residue	Details
D	LYS155
D	SER138
D	TYR151
D	ASN110

site_id	CSA5
Number of Residues	4
Details	Annotated By Reference To The Literature 1ybv

Chain	Residue	Details
E	LYS155
E	SER138
E	TYR151
E	ASN110

site_id	CSA6
Number of Residues	3
Details	Annotated By Reference To The Literature 1ybv

Chain	Residue	Details
F	LYS155
F	SER138
F	ASN110

site_id	CSA7
Number of Residues	3
Details	Annotated By Reference To The Literature 1ybv

Chain	Residue	Details
G	LYS155
G	TYR151
G	ASN110

site_id	CSA8
Number of Residues	3
Details	Annotated By Reference To The Literature 1ybv

Chain	Residue	Details
H	LYS155
H	TYR151
H	ASN110

site_id	CSA9
Number of Residues	2
Details	Annotated By Reference To The Literature 1ybv

Chain	Residue	Details
B	LYS155
B	GLN148

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