2GFY

Structure of E. coli FabF(K335A) mutant with covalently linked dodecanoic acid

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE DAO A 1001

Chain	Residue
A	GLY107
A	ILE108
A	ILE138
A	ALA162
A	CYS163
A	PHE202
A	GLY399
A	PHE400

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	GLY154-ILE170

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	409
Details	Domain: {"description":"Ketosynthase family 3 (KS3)","evidences":[{"source":"PROSITE-ProRule","id":"PRU01348","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
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

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site_id	SWS_FT_FI3
Number of Residues	2
Details	Active site: {"description":"For beta-ketoacyl synthase activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU01348","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	3
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

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site_id	SWS_FT_FI5
Number of Residues	2
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

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Catalytic Information from CSA

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

Chain	Residue	Details
A	HIS340
A	PHE400
A	HIS303
A	CYS163

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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	ALA335	electrostatic stabiliser
A	HIS340	electrostatic stabiliser, hydrogen bond donor
A	PHE400	electrostatic stabiliser

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