7L4L

Crosslinked Crystal Structure of Type II Fatty Acid Synthase Ketosynthase, FabF, and C8-crypto Acyl Carrier Protein, AcpP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004315	molecular_function	3-oxoacyl-[acyl-carrier-protein] synthase 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	0009409	biological_process	response to cold
A	0016740	molecular_function	transferase activity
A	0016746	molecular_function	acyltransferase activity
A	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
A	0019367	biological_process	fatty acid elongation, saturated fatty acid
A	0042803	molecular_function	protein homodimerization activity
A	1903966	biological_process	monounsaturated fatty acid biosynthetic process
B	0004315	molecular_function	3-oxoacyl-[acyl-carrier-protein] synthase 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	0009409	biological_process	response to cold
B	0016740	molecular_function	transferase activity
B	0016746	molecular_function	acyltransferase activity
B	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
B	0019367	biological_process	fatty acid elongation, saturated fatty acid
B	0042803	molecular_function	protein homodimerization activity
B	1903966	biological_process	monounsaturated fatty acid biosynthetic process
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
D	0000035	molecular_function	acyl binding
D	0000036	molecular_function	acyl carrier activity
D	0005515	molecular_function	protein binding
D	0005737	cellular_component	cytoplasm
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	0008289	molecular_function	lipid binding
D	0008610	biological_process	lipid biosynthetic process
D	0009245	biological_process	lipid A biosynthetic process
D	0009410	biological_process	response to xenobiotic stimulus
D	0016020	cellular_component	membrane
D	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	ASP31-LEU46

---

site_id	PS00606
Number of Residues	17
Details	KS3_1 Ketosynthase family 3 (KS3) active site signature. GPSisIAtACTSGvhNI

Chain	Residue	Details
A	GLY154-ILE170

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	818
Details	Domain: {"description":"Ketosynthase family 3 (KS3)","evidences":[{"source":"PROSITE-ProRule","id":"PRU01348","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"For beta-ketoacyl synthase activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU01348","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10037680","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9482715","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Active site: {"description":"For beta-ketoacyl synthase activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU01348","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16710421","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19233644","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19581087","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2GFX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3G0Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3G11","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3HNZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3I8P","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16710421","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19233644","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2GFX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3G0Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3G11","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
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	MCSA1
Number of Residues	6
Details	M-CSA 574

Chain	Residue	Details
A	CYS163	covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor
A	HIS303	activator, proton acceptor, proton donor
A	GLU314	electrostatic stabiliser
A	LYS335	electrostatic stabiliser
A	HIS340	electrostatic stabiliser, hydrogen bond donor
A	PHE400	electrostatic stabiliser

---

site_id	MCSA2
Number of Residues	6
Details	M-CSA 574

Chain	Residue	Details
B	CYS163	covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor
B	HIS303	activator, proton acceptor, proton donor
B	GLU314	electrostatic stabiliser
B	LYS335	electrostatic stabiliser
B	HIS340	electrostatic stabiliser, hydrogen bond donor
B	PHE400	electrostatic stabiliser

---