2FHS

Structure of Acyl Carrier Protein Bound to FabI, the Enoyl Reductase from Escherichia Coli

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	0000035	molecular_function	acyl binding
C	0000036	molecular_function	acyl carrier activity
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
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	0008289	molecular_function	lipid binding
C	0008610	biological_process	lipid biosynthetic process
C	0009245	biological_process	lipid A biosynthetic process
C	0009410	biological_process	response to xenobiotic stimulus
C	0016020	cellular_component	membrane
C	0031177	molecular_function	phosphopantetheine binding

Functional Information from PROSITE/UniProt

site_id	PS00012
Number of Residues	16
Details	PHOSPHOPANTETHEINE Phosphopantetheine attachment site. DLGADSLDTVELVMAL

Chain	Residue	Details
C	ASP32-LEU47

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	16
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	2
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	Site: {"description":"Involved in acyl-ACP binding"}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"O-(pantetheine 4'-phosphoryl)serine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00258","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"4882207","evidenceCode":"ECO:0000269"}]}

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

Chain	Residue	Details
B	GLU150

---

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
A	TYR156
A	LYS163

---

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
B	TYR156
B	LYS163

---

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

Chain	Residue	Details
A	MET159
A	LYS163

---

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

Chain	Residue	Details
B	MET159
B	LYS163

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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

---