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	0006633	biological_process	fatty acid biosynthetic process
A	0009409	biological_process	response to cold
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	0044281	biological_process	small molecule metabolic process
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	1
Details	ACT_SITE: For beta-ketoacyl synthase activity => ECO:0000255|PROSITE-ProRule:PRU01348, ECO:0000269|PubMed:10037680, ECO:0000305|PubMed:9482715

Chain	Residue	Details
A	THR164

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site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: For beta-ketoacyl synthase activity => ECO:0000255|PROSITE-ProRule:PRU01348

Chain	Residue	Details
A	GLY304
A	LEU341

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site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:16710421, ECO:0000269|PubMed:19233644, ECO:0000269|PubMed:19581087, ECO:0007744|PDB:2GFX, ECO:0007744|PDB:3G0Y, ECO:0007744|PDB:3G11, ECO:0007744|PDB:3HNZ, ECO:0007744|PDB:3I8P

Chain	Residue	Details
A	SER271
A	PRO308

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site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:16710421, ECO:0000269|PubMed:19233644, ECO:0007744|PDB:2GFX, ECO:0007744|PDB:3G0Y, ECO:0007744|PDB:3G11

Chain	Residue	Details
A	GLY304
A	LEU341

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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	THR164	covalently attached, electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor
A	GLY304	activator, proton acceptor, proton donor
A	ALA315	electrostatic stabiliser
A	SER336	electrostatic stabiliser
A	LEU341	electrostatic stabiliser, hydrogen bond donor
A	GLY401	electrostatic stabiliser

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