2PD4
Crystal Structure of the Helicobacter pylori Enoyl-Acyl Carrier Protein Reductase in Complex with Hydroxydiphenyl Ether Compounds, Triclosan and Diclosan
Replaces: 1JW7Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 |
| B | 0004318 | molecular_function | enoyl-[acyl-carrier-protein] reductase (NADH) activity |
| B | 0006633 | biological_process | fatty acid biosynthetic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0030497 | biological_process | fatty acid elongation |
| B | 0042802 | molecular_function | identical protein binding |
| C | 0004318 | molecular_function | enoyl-[acyl-carrier-protein] reductase (NADH) activity |
| C | 0006633 | biological_process | fatty acid biosynthetic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0030497 | biological_process | fatty acid elongation |
| C | 0042802 | molecular_function | identical protein 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAD A 1780 |
| Chain | Residue |
| A | GLY13 |
| A | VAL65 |
| A | SER91 |
| A | VAL92 |
| A | ALA93 |
| A | ILE118 |
| A | SER144 |
| A | LYS162 |
| A | ALA188 |
| A | GLY189 |
| A | PRO190 |
| A | VAL14 |
| A | ILE191 |
| A | THR193 |
| A | ALA195 |
| A | PHE202 |
| A | DCN2414 |
| A | HOH2434 |
| A | HOH2444 |
| A | ALA15 |
| A | SER19 |
| A | ILE20 |
| A | LEU40 |
| A | LEU44 |
| A | LEU63 |
| A | ASP64 |
| site_id | AC2 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NAD B 2780 |
| Chain | Residue |
| B | GLY13 |
| B | VAL14 |
| B | ALA15 |
| B | SER19 |
| B | ILE20 |
| B | LEU40 |
| B | LEU44 |
| B | LEU63 |
| B | ASP64 |
| B | VAL65 |
| B | SER91 |
| B | VAL92 |
| B | ALA93 |
| B | LEU143 |
| B | SER144 |
| B | TYR145 |
| B | LYS162 |
| B | GLY189 |
| B | PRO190 |
| B | ILE191 |
| B | THR193 |
| B | ALA195 |
| B | DCN3414 |
| B | HOH3415 |
| B | HOH3417 |
| B | HOH3443 |
| B | HOH3467 |
| site_id | AC3 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAD C 3780 |
| Chain | Residue |
| C | GLY13 |
| C | VAL14 |
| C | ALA15 |
| C | SER19 |
| C | ILE20 |
| C | LEU40 |
| C | LEU44 |
| C | LEU63 |
| C | ASP64 |
| C | VAL65 |
| C | SER91 |
| C | VAL92 |
| C | ALA93 |
| C | LEU143 |
| C | SER144 |
| C | TYR145 |
| C | LYS162 |
| C | ALA188 |
| C | GLY189 |
| C | PRO190 |
| C | ILE191 |
| C | THR193 |
| C | LEU194 |
| C | ALA195 |
| C | DCN4414 |
| C | HOH4428 |
| site_id | AC4 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAD D 4780 |
| Chain | Residue |
| D | ILE191 |
| D | THR193 |
| D | LEU194 |
| D | ALA195 |
| D | PHE202 |
| D | DCN5414 |
| D | HOH5419 |
| D | HOH5424 |
| D | GLY13 |
| D | ALA15 |
| D | SER19 |
| D | ILE20 |
| D | LEU40 |
| D | LEU44 |
| D | LEU63 |
| D | ASP64 |
| D | VAL65 |
| D | SER91 |
| D | VAL92 |
| D | ALA93 |
| D | ILE118 |
| D | LEU143 |
| D | SER144 |
| D | TYR145 |
| D | LYS162 |
| D | ALA188 |
| D | GLY189 |
| D | PRO190 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE DCN A 2414 |
| Chain | Residue |
| A | ALA93 |
| A | ALA95 |
| A | LEU100 |
| A | TYR145 |
| A | TYR155 |
| A | MET158 |
| A | ALA195 |
| A | ILE199 |
| A | PHE202 |
| A | NAD1780 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE DCN B 3414 |
| Chain | Residue |
| B | ALA93 |
| B | PHE94 |
| B | ALA95 |
| B | LEU100 |
| B | TYR145 |
| B | TYR155 |
| B | MET158 |
| B | ALA195 |
| B | ILE199 |
| B | PHE202 |
| B | NAD2780 |
| site_id | AC7 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE DCN C 4414 |
| Chain | Residue |
| C | ALA93 |
| C | PHE94 |
| C | ALA95 |
| C | LEU100 |
| C | TYR145 |
| C | TYR155 |
| C | MET158 |
| C | ALA195 |
| C | ILE199 |
| C | PHE202 |
| C | NAD3780 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE DCN D 5414 |
| Chain | Residue |
| D | ALA93 |
| D | ALA95 |
| D | LEU100 |
| D | TYR145 |
| D | TYR155 |
| D | MET158 |
| D | ALA195 |
| D | ILE199 |
| D | PHE202 |
| D | NAD4780 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250 |
| Chain | Residue | Details |
| A | TYR145 | |
| B | TYR145 | |
| C | TYR145 | |
| D | TYR145 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | TYR155 | |
| B | TYR155 | |
| C | TYR155 | |
| D | TYR155 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17879346 |
| Chain | Residue | Details |
| A | GLY13 | |
| B | VAL92 | |
| B | LYS162 | |
| B | ILE191 | |
| C | GLY13 | |
| C | SER19 | |
| C | ASP64 | |
| C | VAL92 | |
| C | LYS162 | |
| C | ILE191 | |
| D | GLY13 | |
| A | SER19 | |
| D | SER19 | |
| D | ASP64 | |
| D | VAL92 | |
| D | LYS162 | |
| D | ILE191 | |
| A | ASP64 | |
| A | VAL92 | |
| A | LYS162 | |
| A | ILE191 | |
| B | GLY13 | |
| B | SER19 | |
| B | ASP64 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ALA95 | |
| B | ALA95 | |
| C | ALA95 | |
| D | ALA95 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | SITE: Involved in acyl-ACP binding => ECO:0000250 |
| Chain | Residue | Details |
| A | ARG203 | |
| B | ARG203 | |
| C | ARG203 | |
| D | ARG203 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| A | TYR155 | |
| A | LYS162 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| B | TYR155 | |
| B | LYS162 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| C | TYR155 | |
| C | LYS162 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| D | TYR155 | |
| D | LYS162 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| A | MET158 | |
| A | LYS162 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| B | MET158 | |
| B | LYS162 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| C | MET158 | |
| C | LYS162 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1qsg |
| Chain | Residue | Details |
| D | MET158 | |
| D | LYS162 |
