3SJ7
Structure of beta-ketoacetyl-CoA reductase (FabG) from Staphylococcus aureus complex with NADPH
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004316 | molecular_function | 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006631 | biological_process | fatty acid metabolic process |
| A | 0006633 | biological_process | fatty acid biosynthetic process |
| A | 0008610 | biological_process | lipid biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| A | 0030497 | biological_process | fatty acid elongation |
| A | 0046394 | biological_process | carboxylic acid biosynthetic process |
| A | 0051287 | molecular_function | NAD binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004316 | molecular_function | 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006631 | biological_process | fatty acid metabolic process |
| B | 0006633 | biological_process | fatty acid biosynthetic process |
| B | 0008610 | biological_process | lipid biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| B | 0030497 | biological_process | fatty acid elongation |
| B | 0046394 | biological_process | carboxylic acid biosynthetic process |
| B | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NDP A 245 |
| Chain | Residue |
| A | GLY9 |
| A | ALA59 |
| A | ASN60 |
| A | VAL61 |
| A | ASN87 |
| A | ALA88 |
| A | GLY89 |
| A | ILE90 |
| A | THR110 |
| A | SER138 |
| A | SER139 |
| A | SER11 |
| A | TYR152 |
| A | LYS156 |
| A | PRO182 |
| A | GLY183 |
| A | ILE185 |
| A | PG4246 |
| A | HOH298 |
| A | ARG12 |
| A | ILE14 |
| A | ASN32 |
| A | TYR33 |
| A | ALA34 |
| A | GLY35 |
| A | SER36 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PG4 A 246 |
| Chain | Residue |
| A | SER139 |
| A | ASN146 |
| A | GLN149 |
| A | TYR152 |
| A | PHE184 |
| A | MET201 |
| A | NDP245 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PG4 A 247 |
| Chain | Residue |
| A | PRO124 |
| A | LEU127 |
| A | ARG128 |
| A | ARG130 |
| B | SER194 |
| B | ASP195 |
| B | GLU196 |
| site_id | AC4 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE NDP B 245 |
| Chain | Residue |
| B | GLY9 |
| B | SER11 |
| B | ARG12 |
| B | ILE14 |
| B | ALA34 |
| B | GLY35 |
| B | SER36 |
| B | ALA59 |
| B | ASN60 |
| B | VAL61 |
| B | ASN87 |
| B | ALA88 |
| B | LYS100 |
| B | GLN102 |
| B | THR110 |
| B | SER138 |
| B | SER139 |
| B | TYR152 |
| B | LYS156 |
| B | PRO182 |
| B | GLY183 |
| B | ILE185 |
| B | PG4246 |
| B | HOH286 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PG4 B 246 |
| Chain | Residue |
| B | VAL141 |
| B | ASN146 |
| B | PHE184 |
| B | GLN204 |
| B | MET242 |
| B | NDP245 |
| B | HOH284 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SvvgavgnpgQanYVATKAGViGLTkSAA |
| Chain | Residue | Details |
| A | SER139-ALA167 |
