2PD3
Crystal Structure of the Helicobacter pylori Enoyl-Acyl Carrier Protein Reductase in Complex with Hydroxydiphenyl Ether Compounds, Triclosan and Diclosan
Replaces: 1JVFFunctional 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 | 24 |
Details | BINDING SITE FOR RESIDUE NAD A 1780 |
Chain | Residue |
A | GLY13 |
A | VAL65 |
A | VAL92 |
A | ALA93 |
A | ILE118 |
A | LEU143 |
A | SER144 |
A | TYR145 |
A | LYS162 |
A | ALA188 |
A | PRO190 |
A | VAL14 |
A | ILE191 |
A | THR193 |
A | ALA195 |
A | TCL2414 |
A | HOH2423 |
A | ALA15 |
A | SER19 |
A | ILE20 |
A | LEU40 |
A | LEU44 |
A | LEU63 |
A | ASP64 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE TCL A 2414 |
Chain | Residue |
A | ALA93 |
A | PHE94 |
A | ALA95 |
A | TYR145 |
A | TYR155 |
A | ALA195 |
A | ILE199 |
A | PHE202 |
A | NAD1780 |
site_id | AC3 |
Number of Residues | 28 |
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 | ILE118 |
B | LEU143 |
B | SER144 |
B | TYR145 |
B | LYS162 |
B | ALA188 |
B | GLY189 |
B | PRO190 |
B | ILE191 |
B | THR193 |
B | ALA195 |
B | TCL3414 |
B | HOH3427 |
B | HOH3435 |
B | HOH3464 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE TCL B 3414 |
Chain | Residue |
B | ALA93 |
B | ALA95 |
B | LEU100 |
B | TYR145 |
B | TYR155 |
B | ALA195 |
B | NAD2780 |
site_id | AC5 |
Number of Residues | 29 |
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 | ILE118 |
C | LEU143 |
C | SER144 |
C | TYR145 |
C | LYS162 |
C | ALA188 |
C | GLY189 |
C | PRO190 |
C | ILE191 |
C | THR193 |
C | LEU194 |
C | ALA195 |
C | TCL4414 |
C | HOH4429 |
C | HOH4444 |
C | HOH4471 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE TCL C 4414 |
Chain | Residue |
C | ALA95 |
C | LEU100 |
C | TYR145 |
C | TYR155 |
C | ALA195 |
C | NAD3780 |
C | ALA93 |
C | PHE94 |
site_id | AC7 |
Number of Residues | 29 |
Details | BINDING SITE FOR RESIDUE NAD D 4780 |
Chain | Residue |
D | GLY13 |
D | VAL14 |
D | ALA15 |
D | SER19 |
D | ILE20 |
D | LEU40 |
D | LEU44 |
D | LEU63 |
D | ASP64 |
D | VAL65 |
D | VAL92 |
D | ALA93 |
D | ILE118 |
D | LEU143 |
D | SER144 |
D | TYR145 |
D | LYS162 |
D | ALA188 |
D | GLY189 |
D | PRO190 |
D | ILE191 |
D | THR193 |
D | LEU194 |
D | ALA195 |
D | TCL5414 |
D | HOH5425 |
D | HOH5427 |
D | HOH5434 |
D | HOH5450 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE TCL D 5414 |
Chain | Residue |
D | ALA93 |
D | ALA95 |
D | LEU100 |
D | TYR145 |
D | TYR155 |
D | MET158 |
D | ALA195 |
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 |