Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1Q7B

The structure of betaketoacyl-[ACP] reductase from E. coli in complex with NADP+

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	0006629	biological_process	lipid metabolic process
A	0006631	biological_process	fatty acid metabolic process
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	0006629	biological_process	lipid metabolic process
B	0006631	biological_process	fatty acid metabolic process
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	0006629	biological_process	lipid metabolic process
C	0006631	biological_process	fatty acid metabolic process
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	0006629	biological_process	lipid metabolic process
D	0006631	biological_process	fatty acid metabolic process
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

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA B 9001

Chain	Residue
B	GLU233
B	THR234
B	HOH3037
C	GLU233
C	THR234
C	HOH2037

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 9002

Chain	Residue
D	GLU233
D	THR234
D	HOH1037
A	GLU233
A	THR234
A	HOH4037

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CA B 9003

Chain	Residue
B	GLY50
B	GLY53
B	HOH2063

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA C 9004

Chain	Residue
C	ASN145
C	HOH3046
C	HOH3204
C	HOH4041

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA D 9005

Chain	Residue
D	ASN145
D	HOH3041
D	HOH4046
D	HOH4056
D	HOH4213
D	HOH4214

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 9007

Chain	Residue
A	ASN145
A	HOH1046
A	HOH1056
A	HOH1159
A	HOH2041

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CA B 9008

Chain	Residue
B	ASN145
B	HOH1041
B	HOH2046

site_id	AC8
Number of Residues	26
Details	BINDING SITE FOR RESIDUE NAP A 1901

Chain	Residue
A	GLY12
A	SER14
A	ARG15
A	ILE17
A	THR37
A	LEU58
A	ASN59
A	VAL60
A	ASN86
A	ALA87
A	GLY88
A	ILE89
A	ILE136
A	GLY137
A	SER138
A	TYR151
A	LYS155
A	PRO181
A	GLY182
A	ILE184
A	THR186
A	HOH1038
A	HOH1045
A	HOH1053
A	HOH1066
A	HOH1133

site_id	AC9
Number of Residues	25
Details	BINDING SITE FOR RESIDUE NAP B 2901

Chain	Residue
B	GLY12
B	SER14
B	ARG15
B	ILE17
B	ALA36
B	THR37
B	LEU58
B	ASN59
B	VAL60
B	ASN86
B	ALA87
B	GLY88
B	ILE136
B	GLY137
B	SER138
B	TYR151
B	LYS155
B	PRO181
B	GLY182
B	ILE184
B	THR186
B	HOH2038
B	HOH2045
B	HOH2053
B	HOH2066

site_id	BC1
Number of Residues	28
Details	BINDING SITE FOR RESIDUE NAP C 3901

Chain	Residue
C	LYS155
C	PRO181
C	GLY182
C	ILE184
C	THR186
C	HOH3038
C	HOH3045
C	HOH3053
C	HOH3066
C	HOH3112
C	HOH3113
C	HOH3187
C	HOH3191
C	GLY12
C	SER14
C	ARG15
C	ILE17
C	THR37
C	LEU58
C	ASN59
C	VAL60
C	ASN86
C	ALA87
C	GLY88
C	ILE89
C	ILE136
C	GLY137
C	TYR151

site_id	BC2
Number of Residues	27
Details	BINDING SITE FOR RESIDUE NAP D 4901

Chain	Residue
D	GLY12
D	SER14
D	ARG15
D	ALA36
D	THR37
D	LEU58
D	ASN59
D	VAL60
D	ASN86
D	ALA87
D	GLY88
D	ILE89
D	ILE136
D	GLY137
D	SER138
D	TYR151
D	LYS155
D	PRO181
D	GLY182
D	ILE184
D	THR186
D	HOH4038
D	HOH4045
D	HOH4053
D	HOH4112
D	HOH4113
D	HOH4234

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	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10001","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	36
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15016358","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1Q7B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Q7C","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	20
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15016358","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1Q7B","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15016358","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1ybv

Chain	Residue	Details
A	LYS155
A	SER138
A	TYR151
A	ASN110

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

Chain	Residue	Details
B	LYS155
B	TYR151

site_id	CSA11
Number of Residues	2
Details	Annotated By Reference To The Literature 1ybv

Chain	Residue	Details
C	LYS155
C	TYR151

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

Chain	Residue	Details
D	LYS155
D	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	2
Details	Annotated By Reference To The Literature 1ybv

Chain	Residue	Details
A	LYS155
A	GLN148

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1ybv

Chain	Residue	Details
B	LYS155
B	GLN148

site_id	CSA7
Number of Residues	2
Details	Annotated By Reference To The Literature 1ybv

Chain	Residue	Details
C	LYS155
C	GLN148

site_id	CSA8
Number of Residues	2
Details	Annotated By Reference To The Literature 1ybv

Chain	Residue	Details
D	LYS155
D	GLN148

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

Chain	Residue	Details
A	LYS155
A	TYR151

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