2GFW
Structure of wild type E. coli FabF (KASII)
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 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 |
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 |
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 |
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 |
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 |
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 |
site_id | CSA2 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1kas |
Chain | Residue | Details |
A | LYS335 | |
A | HIS340 | |
A | PHE400 | |
A | HIS303 | |
A | CYS163 | |
A | PHE398 |
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 |