Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1DFI

X-RAY STRUCTURE OF ESCHERICHIA COLI ENOYL REDUCTASE WITH BOUND NAD

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
A	0005515	molecular_function	protein binding
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	0016020	cellular_component	membrane
A	0016491	molecular_function	oxidoreductase activity
A	0030497	biological_process	fatty acid elongation
A	0032991	cellular_component	protein-containing complex
A	0042802	molecular_function	identical protein binding
A	0046677	biological_process	response to antibiotic
A	0051289	biological_process	protein homotetramerization
A	0070404	molecular_function	NADH binding
A	1902494	cellular_component	catalytic complex
B	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
B	0005515	molecular_function	protein binding
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	0016020	cellular_component	membrane
B	0016491	molecular_function	oxidoreductase activity
B	0030497	biological_process	fatty acid elongation
B	0032991	cellular_component	protein-containing complex
B	0042802	molecular_function	identical protein binding
B	0046677	biological_process	response to antibiotic
B	0051289	biological_process	protein homotetramerization
B	0070404	molecular_function	NADH binding
B	1902494	cellular_component	catalytic complex
C	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
C	0005515	molecular_function	protein binding
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	0016020	cellular_component	membrane
C	0016491	molecular_function	oxidoreductase activity
C	0030497	biological_process	fatty acid elongation
C	0032991	cellular_component	protein-containing complex
C	0042802	molecular_function	identical protein binding
C	0046677	biological_process	response to antibiotic
C	0051289	biological_process	protein homotetramerization
C	0070404	molecular_function	NADH binding
C	1902494	cellular_component	catalytic complex
D	0004318	molecular_function	enoyl-[acyl-carrier-protein] reductase (NADH) activity
D	0005515	molecular_function	protein binding
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	0016020	cellular_component	membrane
D	0016491	molecular_function	oxidoreductase activity
D	0030497	biological_process	fatty acid elongation
D	0032991	cellular_component	protein-containing complex
D	0042802	molecular_function	identical protein binding
D	0046677	biological_process	response to antibiotic
D	0051289	biological_process	protein homotetramerization
D	0070404	molecular_function	NADH binding
D	1902494	cellular_component	catalytic complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	20
Details	BINDING SITE FOR RESIDUE NAD A 501

Chain	Residue
A	GLY13
A	SER91
A	ILE92
A	LEU144
A	SER145
A	LYS163
A	ALA189
A	ILE192
A	LEU195
A	HOH539
A	HOH541
A	VAL14
A	HOH591
A	ALA15
A	SER19
A	ILE20
A	GLN40
A	CYS63
A	ASP64
A	VAL65

site_id	AC2
Number of Residues	17
Details	BINDING SITE FOR RESIDUE NAD B 501

Chain	Residue
B	GLY13
B	ALA15
B	SER19
B	ILE20
B	ALA21
B	GLN40
B	CYS63
B	ASP64
B	VAL65
B	SER91
B	ILE92
B	LEU144
B	SER145
B	LYS163
B	ALA189
B	GLY190
B	HOH528

site_id	AC3
Number of Residues	20
Details	BINDING SITE FOR RESIDUE NAD C 501

Chain	Residue
C	GLY13
C	ALA15
C	ILE20
C	GLN40
C	CYS63
C	ASP64
C	VAL65
C	SER91
C	ILE92
C	GLY93
C	LEU144
C	SER145
C	LYS163
C	ALA189
C	GLY190
C	ILE192
C	LEU195
C	HOH512
C	HOH551
C	HOH580

site_id	AC4
Number of Residues	21
Details	BINDING SITE FOR RESIDUE NAD D 501

Chain	Residue
D	GLY13
D	ALA15
D	SER19
D	ILE20
D	GLN40
D	CYS63
D	ASP64
D	VAL65
D	SER91
D	LEU144
D	SER145
D	LYS163
D	ALA189
D	GLY190
D	PRO191
D	ILE192
D	LEU195
D	HOH526
D	HOH535
D	HOH561
D	HOH564

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10201369","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10398587","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10493822","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10595560","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11514139","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12109908","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12699381","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8953047","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {}

Chain

Residue

Details

Catalytic Information from CSA

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

Chain	Residue	Details
A	GLU150

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

Chain	Residue	Details
B	MET159
B	LYS163

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

Chain	Residue	Details
C	MET159
C	LYS163

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

Chain	Residue	Details
D	MET159
D	LYS163

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

Chain	Residue	Details
B	GLU150

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

Chain	Residue	Details
C	GLU150

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

Chain	Residue	Details
D	GLU150

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
A	TYR156
A	LYS163

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

Chain	Residue	Details
B	TYR156
B	LYS163

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

Chain	Residue	Details
C	TYR156
C	LYS163

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

Chain	Residue	Details
D	TYR156
D	LYS163

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

Chain	Residue	Details
A	MET159
A	LYS163

site_id	MCSA1
Number of Residues	2
Details	M-CSA 606

Chain	Residue	Details
A	TYR156	proton acceptor, proton donor
A	LYS163	electrostatic stabiliser

site_id	MCSA2
Number of Residues	2
Details	M-CSA 606

Chain	Residue	Details
B	TYR156	proton acceptor, proton donor
B	LYS163	electrostatic stabiliser

site_id	MCSA3
Number of Residues	2
Details	M-CSA 606

Chain	Residue	Details
C	TYR156	proton acceptor, proton donor
C	LYS163	electrostatic stabiliser

site_id	MCSA4
Number of Residues	2
Details	M-CSA 606

Chain	Residue	Details
D	TYR156	proton acceptor, proton donor
D	LYS163	electrostatic stabiliser

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)