2GFX
Structure of E. coli FabF(C163Q) in complex with Platensimycin
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 | 17 |
| Details | BINDING SITE FOR RESIDUE PMN A 1001 |
| Chain | Residue |
| A | GLN163 |
| A | ALA309 |
| A | GLY310 |
| A | HIS340 |
| A | PHE398 |
| A | GLY399 |
| A | PHE400 |
| A | HOH1010 |
| A | HOH1072 |
| A | ALA205 |
| A | ARG206 |
| A | THR270 |
| A | SER271 |
| A | PRO272 |
| A | HIS303 |
| A | THR307 |
| A | PRO308 |
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 | GLN163 |
| 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 |
