4JRO
Crystal structure of 3-oxoacyl-[acyl-carrier protein]reductase (FabG)from Listeria monocytogenes in complex with NADP+
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004316 | molecular_function | 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity |
| A | 0006631 | biological_process | fatty acid metabolic process |
| A | 0006633 | biological_process | fatty acid biosynthetic process |
| A | 0008610 | biological_process | lipid biosynthetic process |
| A | 0046394 | biological_process | carboxylic acid biosynthetic process |
| A | 0051287 | molecular_function | NAD binding |
| B | 0004316 | molecular_function | 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity |
| B | 0006631 | biological_process | fatty acid metabolic process |
| B | 0006633 | biological_process | fatty acid biosynthetic process |
| B | 0008610 | biological_process | lipid biosynthetic process |
| B | 0046394 | biological_process | carboxylic acid biosynthetic process |
| B | 0051287 | molecular_function | NAD binding |
| C | 0004316 | molecular_function | 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity |
| C | 0006631 | biological_process | fatty acid metabolic process |
| C | 0006633 | biological_process | fatty acid biosynthetic process |
| C | 0008610 | biological_process | lipid biosynthetic process |
| C | 0046394 | biological_process | carboxylic acid biosynthetic process |
| C | 0051287 | molecular_function | NAD binding |
| D | 0004316 | molecular_function | 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity |
| D | 0006631 | biological_process | fatty acid metabolic process |
| D | 0006633 | biological_process | fatty acid biosynthetic process |
| D | 0008610 | biological_process | lipid biosynthetic process |
| D | 0046394 | biological_process | carboxylic acid biosynthetic process |
| D | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE NAP B 301 |
| Chain | Residue |
| B | GLY12 |
| B | SER39 |
| B | ALA62 |
| B | ASN63 |
| B | VAL64 |
| B | ASN90 |
| B | ALA91 |
| B | GLY92 |
| B | ILE113 |
| B | ALA141 |
| B | SER142 |
| B | SER14 |
| B | TYR155 |
| B | LYS159 |
| B | PRO185 |
| B | GLY186 |
| B | ILE188 |
| B | HOH414 |
| B | ARG15 |
| B | GLY16 |
| B | ILE17 |
| B | ASN35 |
| B | TYR36 |
| B | ASN37 |
| B | GLY38 |
| site_id | AC2 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NAP C 301 |
| Chain | Residue |
| C | GLY12 |
| C | SER14 |
| C | ARG15 |
| C | GLY16 |
| C | ILE17 |
| C | ASN35 |
| C | TYR36 |
| C | ASN37 |
| C | GLY38 |
| C | SER39 |
| C | ALA62 |
| C | ASN63 |
| C | VAL64 |
| C | ASN90 |
| C | ALA91 |
| C | GLY92 |
| C | ILE93 |
| C | ILE113 |
| C | MET140 |
| C | ALA141 |
| C | SER142 |
| C | TYR155 |
| C | LYS159 |
| C | PRO185 |
| C | GLY186 |
| C | ILE188 |
| C | THR190 |
| C | HOH455 |
| C | HOH518 |
| C | HOH535 |
| site_id | AC3 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAP D 301 |
| Chain | Residue |
| D | GLY12 |
| D | SER14 |
| D | ARG15 |
| D | GLY16 |
| D | ILE17 |
| D | ASN35 |
| D | TYR36 |
| D | ASN37 |
| D | GLY38 |
| D | SER39 |
| D | ALA62 |
| D | ASN63 |
| D | VAL64 |
| D | ASN90 |
| D | ALA91 |
| D | GLY92 |
| D | ILE113 |
| D | ALA141 |
| D | SER142 |
| D | TYR155 |
| D | LYS159 |
| D | PRO185 |
| D | GLY186 |
| D | ILE188 |
| D | HOH509 |
| D | HOH542 |
| D | HOH544 |
| D | HOH547 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. SvvglignagQanYVASKAGViGLTkTTA |
| Chain | Residue | Details |
| A | SER142-ALA170 |
