3GR6
Crystal structure of the staphylococcus aureus enoyl-acyl carrier protein reductase (fabI) in complex with NADP and triclosan
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004318 | molecular_function | enoyl-[acyl-carrier-protein] reductase (NADH) activity |
| A | 0006633 | biological_process | fatty acid biosynthetic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0030497 | biological_process | fatty acid elongation |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0050661 | molecular_function | NADP binding |
| A | 0141148 | molecular_function | enoyl-[acyl-carrier-protein] reductase (NADPH) activity |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0004318 | molecular_function | enoyl-[acyl-carrier-protein] reductase (NADH) activity |
| D | 0006633 | biological_process | fatty acid biosynthetic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0030497 | biological_process | fatty acid elongation |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0050661 | molecular_function | NADP binding |
| D | 0141148 | molecular_function | enoyl-[acyl-carrier-protein] reductase (NADPH) activity |
| G | 0000166 | molecular_function | nucleotide binding |
| G | 0004318 | molecular_function | enoyl-[acyl-carrier-protein] reductase (NADH) activity |
| G | 0006633 | biological_process | fatty acid biosynthetic process |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0030497 | biological_process | fatty acid elongation |
| G | 0042802 | molecular_function | identical protein binding |
| G | 0050661 | molecular_function | NADP binding |
| G | 0141148 | molecular_function | enoyl-[acyl-carrier-protein] reductase (NADPH) activity |
| J | 0000166 | molecular_function | nucleotide binding |
| J | 0004318 | molecular_function | enoyl-[acyl-carrier-protein] reductase (NADH) activity |
| J | 0006633 | biological_process | fatty acid biosynthetic process |
| J | 0016491 | molecular_function | oxidoreductase activity |
| J | 0030497 | biological_process | fatty acid elongation |
| J | 0042802 | molecular_function | identical protein binding |
| J | 0050661 | molecular_function | NADP binding |
| J | 0141148 | molecular_function | enoyl-[acyl-carrier-protein] reductase (NADPH) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAP A 361 |
| Chain | Residue |
| A | GLY13 |
| A | ASP66 |
| A | VAL67 |
| A | SER93 |
| A | ILE94 |
| A | ALA95 |
| A | THR145 |
| A | THR146 |
| A | TYR147 |
| A | LYS164 |
| A | ALA190 |
| A | ILE14 |
| A | GLY191 |
| A | PRO192 |
| A | ILE193 |
| A | THR195 |
| A | LEU196 |
| A | SER197 |
| A | HOH260 |
| A | HOH262 |
| A | TCL371 |
| A | ALA15 |
| A | SER19 |
| A | ILE20 |
| A | ARG40 |
| A | LYS41 |
| A | SER44 |
| A | ILE65 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE TCL A 371 |
| Chain | Residue |
| A | ALA95 |
| A | ALA97 |
| A | TYR147 |
| A | TYR157 |
| A | MET160 |
| A | SER197 |
| A | ALA198 |
| A | VAL201 |
| A | PHE204 |
| A | NAP361 |
| site_id | AC3 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NAP D 257 |
| Chain | Residue |
| D | GLY13 |
| D | ILE14 |
| D | ALA15 |
| D | SER19 |
| D | ILE20 |
| D | ARG40 |
| D | LYS41 |
| D | SER44 |
| D | ILE65 |
| D | ASP66 |
| D | VAL67 |
| D | SER93 |
| D | ILE94 |
| D | ALA95 |
| D | ILE120 |
| D | THR145 |
| D | THR146 |
| D | TYR147 |
| D | LYS164 |
| D | ALA190 |
| D | GLY191 |
| D | PRO192 |
| D | ILE193 |
| D | THR195 |
| D | LEU196 |
| D | SER197 |
| D | TCL258 |
| D | HOH263 |
| D | HOH272 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE TCL D 258 |
| Chain | Residue |
| D | ALA97 |
| D | TYR147 |
| D | TYR157 |
| D | MET160 |
| D | LYS164 |
| D | SER197 |
| D | ALA198 |
| D | VAL201 |
| D | NAP257 |
| site_id | AC5 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE NAP G 257 |
| Chain | Residue |
| G | HOH274 |
| G | GLY13 |
| G | ILE14 |
| G | ALA15 |
| G | SER19 |
| G | ILE20 |
| G | ARG40 |
| G | ILE65 |
| G | ASP66 |
| G | VAL67 |
| G | SER93 |
| G | ILE94 |
| G | ALA95 |
| G | THR145 |
| G | THR146 |
| G | TYR147 |
| G | LYS164 |
| G | ALA190 |
| G | GLY191 |
| G | PRO192 |
| G | ILE193 |
| G | THR195 |
| G | SER197 |
| G | TCL258 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE TCL G 258 |
| Chain | Residue |
| G | ALA95 |
| G | PHE96 |
| G | ALA97 |
| G | TYR147 |
| G | TYR157 |
| G | MET160 |
| G | LYS164 |
| G | SER197 |
| G | ALA198 |
| G | VAL201 |
| G | PHE204 |
| G | NAP257 |
| site_id | AC7 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE NAP J 257 |
| Chain | Residue |
| J | GLY13 |
| J | ILE14 |
| J | SER19 |
| J | ILE20 |
| J | ARG40 |
| J | LYS41 |
| J | SER44 |
| J | ILE65 |
| J | ASP66 |
| J | VAL67 |
| J | SER93 |
| J | ILE94 |
| J | ALA95 |
| J | THR145 |
| J | THR146 |
| J | TYR147 |
| J | LYS164 |
| J | ALA190 |
| J | GLY191 |
| J | PRO192 |
| J | ILE193 |
| J | THR195 |
| J | SER197 |
| J | TCL258 |
| J | HOH268 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE TCL J 258 |
| Chain | Residue |
| J | ALA97 |
| J | TYR147 |
| J | TYR157 |
| J | MET160 |
| J | SER197 |
| J | ALA198 |
| J | VAL201 |
| J | PHE204 |
| J | NAP257 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250 |
| Chain | Residue | Details |
| A | TYR147 | |
| A | TYR157 | |
| D | TYR147 | |
| D | TYR157 | |
| G | TYR147 | |
| G | TYR157 | |
| J | TYR147 | |
| J | TYR157 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 28 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19768684 |
| Chain | Residue | Details |
| A | GLY13 | |
| D | ARG40 | |
| D | ASP66 | |
| D | ILE94 | |
| D | LYS164 | |
| D | ILE193 | |
| G | GLY13 | |
| G | SER19 | |
| G | ARG40 | |
| G | ASP66 | |
| G | ILE94 | |
| A | SER19 | |
| G | LYS164 | |
| G | ILE193 | |
| J | GLY13 | |
| J | SER19 | |
| J | ARG40 | |
| J | ASP66 | |
| J | ILE94 | |
| J | LYS164 | |
| J | ILE193 | |
| A | ARG40 | |
| A | ASP66 | |
| A | ILE94 | |
| A | LYS164 | |
| A | ILE193 | |
| D | GLY13 | |
| D | SER19 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | ALA97 | |
| D | ALA97 | |
| G | ALA97 | |
| J | ALA97 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | SITE: Critical for cofactor specificity => ECO:0000250 |
| Chain | Residue | Details |
| A | ARG40 | |
| A | LYS41 | |
| D | ARG40 | |
| D | LYS41 | |
| G | ARG40 | |
| G | LYS41 | |
| J | ARG40 | |
| J | LYS41 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| A | LYS164 | |
| A | TYR157 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| D | LYS164 | |
| D | TYR157 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| G | LYS164 | |
| G | TYR157 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| J | LYS164 | |
| J | TYR157 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| A | LYS164 | |
| A | MET160 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| D | LYS164 | |
| D | MET160 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| G | LYS164 | |
| G | MET160 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| J | LYS164 | |
| J | MET160 |
