4NR0
Crystal structure of the Pseudomonas aeruginosa Enoyl-Acyl Carrier Protein Reductase (FabI) in complex with NAD+ and triclosan
Functional 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 | 32 |
Details | BINDING SITE FOR RESIDUE NAD A 301 |
Chain | Residue |
A | GLY13 |
A | VAL67 |
A | SER93 |
A | VAL94 |
A | GLY95 |
A | ILE121 |
A | LEU147 |
A | SER148 |
A | LYS166 |
A | ALA192 |
A | GLY193 |
A | VAL14 |
A | PRO194 |
A | ILE195 |
A | THR197 |
A | LEU198 |
A | ALA199 |
A | TCL302 |
A | HOH401 |
A | HOH420 |
A | HOH432 |
A | HOH433 |
A | ALA15 |
A | HOH438 |
A | HOH442 |
A | HOH529 |
A | SER19 |
A | ILE20 |
A | GLN40 |
A | LEU44 |
A | CYS65 |
A | ASP66 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE TCL A 302 |
Chain | Residue |
A | GLY95 |
A | ALA97 |
A | LEU102 |
A | TYR149 |
A | TYR159 |
A | ALA199 |
A | NAD301 |
site_id | AC3 |
Number of Residues | 33 |
Details | BINDING SITE FOR RESIDUE NAD B 301 |
Chain | Residue |
B | GLY13 |
B | VAL14 |
B | ALA15 |
B | SER19 |
B | ILE20 |
B | GLN40 |
B | LEU44 |
B | CYS65 |
B | ASP66 |
B | VAL67 |
B | SER93 |
B | VAL94 |
B | GLY95 |
B | ILE121 |
B | LEU147 |
B | SER148 |
B | TYR149 |
B | LYS166 |
B | ALA192 |
B | GLY193 |
B | PRO194 |
B | ILE195 |
B | THR197 |
B | LEU198 |
B | ALA199 |
B | TCL302 |
B | HOH401 |
B | HOH416 |
B | HOH438 |
B | HOH449 |
B | HOH450 |
B | HOH451 |
B | HOH522 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE TCL B 302 |
Chain | Residue |
B | GLY95 |
B | ALA97 |
B | TYR149 |
B | TYR159 |
B | ALA199 |
B | NAD301 |
site_id | AC5 |
Number of Residues | 32 |
Details | BINDING SITE FOR RESIDUE NAD C 301 |
Chain | Residue |
C | ILE195 |
C | THR197 |
C | LEU198 |
C | ALA199 |
C | TCL302 |
C | HOH410 |
C | HOH426 |
C | HOH433 |
C | HOH450 |
C | HOH452 |
C | HOH467 |
C | GLY13 |
C | VAL14 |
C | ALA15 |
C | SER19 |
C | ILE20 |
C | GLN40 |
C | LEU44 |
C | CYS65 |
C | ASP66 |
C | VAL67 |
C | SER93 |
C | VAL94 |
C | GLY95 |
C | ILE121 |
C | LEU147 |
C | SER148 |
C | TYR149 |
C | LYS166 |
C | ALA192 |
C | GLY193 |
C | PRO194 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE TCL C 302 |
Chain | Residue |
C | GLY95 |
C | ALA97 |
C | LEU102 |
C | TYR149 |
C | TYR159 |
C | ALA199 |
C | MET209 |
C | NAD301 |
site_id | AC7 |
Number of Residues | 32 |
Details | BINDING SITE FOR RESIDUE NAD D 301 |
Chain | Residue |
D | GLY13 |
D | VAL14 |
D | ALA15 |
D | SER19 |
D | ILE20 |
D | GLN40 |
D | LEU44 |
D | CYS65 |
D | ASP66 |
D | VAL67 |
D | SER93 |
D | VAL94 |
D | GLY95 |
D | ILE121 |
D | LEU147 |
D | SER148 |
D | LYS166 |
D | ALA192 |
D | GLY193 |
D | PRO194 |
D | ILE195 |
D | THR197 |
D | LEU198 |
D | ALA199 |
D | TCL302 |
D | HOH419 |
D | HOH420 |
D | HOH421 |
D | HOH423 |
D | HOH448 |
D | HOH453 |
D | HOH551 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE TCL D 302 |
Chain | Residue |
D | GLY95 |
D | ALA97 |
D | LEU102 |
D | TYR149 |
D | TYR159 |
D | ALA199 |
D | ALA200 |
D | NAD301 |
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 | TYR149 | |
A | TYR159 | |
B | TYR149 | |
B | TYR159 | |
C | TYR149 | |
C | TYR159 | |
D | TYR149 | |
D | TYR159 |
site_id | SWS_FT_FI2 |
Number of Residues | 32 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | GLY13 | |
B | SER19 | |
B | GLN40 | |
B | ASP66 | |
B | VAL94 | |
B | ALA97 | |
B | LYS166 | |
B | ILE195 | |
C | GLY13 | |
C | SER19 | |
C | GLN40 | |
A | SER19 | |
C | ASP66 | |
C | VAL94 | |
C | ALA97 | |
C | LYS166 | |
C | ILE195 | |
D | GLY13 | |
D | SER19 | |
D | GLN40 | |
D | ASP66 | |
D | VAL94 | |
A | GLN40 | |
D | ALA97 | |
D | LYS166 | |
D | ILE195 | |
A | ASP66 | |
A | VAL94 | |
A | ALA97 | |
A | LYS166 | |
A | ILE195 | |
B | GLY13 |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | SITE: Involved in acyl-ACP binding => ECO:0000250 |
Chain | Residue | Details |
A | LYS204 | |
D | LYS204 | |
D | ARG207 | |
D | LYS208 | |
A | ARG207 | |
A | LYS208 | |
B | LYS204 | |
B | ARG207 | |
B | LYS208 | |
C | LYS204 | |
C | ARG207 | |
C | LYS208 |