3FNF
Crystal structure of InhA bound to triclosan derivative
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004318 | molecular_function | enoyl-[acyl-carrier-protein] reductase (NADH) activity |
A | 0005504 | molecular_function | fatty acid binding |
A | 0005886 | cellular_component | plasma membrane |
A | 0006633 | biological_process | fatty acid biosynthetic process |
A | 0009274 | cellular_component | peptidoglycan-based cell wall |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0030497 | biological_process | fatty acid elongation |
A | 0046677 | biological_process | response to antibiotic |
A | 0050343 | molecular_function | trans-2-enoyl-CoA reductase (NADH) activity |
A | 0070403 | molecular_function | NAD+ binding |
A | 0071768 | biological_process | mycolic acid biosynthetic process |
B | 0004318 | molecular_function | enoyl-[acyl-carrier-protein] reductase (NADH) activity |
B | 0005504 | molecular_function | fatty acid binding |
B | 0005886 | cellular_component | plasma membrane |
B | 0006633 | biological_process | fatty acid biosynthetic process |
B | 0009274 | cellular_component | peptidoglycan-based cell wall |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0030497 | biological_process | fatty acid elongation |
B | 0046677 | biological_process | response to antibiotic |
B | 0050343 | molecular_function | trans-2-enoyl-CoA reductase (NADH) activity |
B | 0070403 | molecular_function | NAD+ binding |
B | 0071768 | biological_process | mycolic acid biosynthetic process |
C | 0004318 | molecular_function | enoyl-[acyl-carrier-protein] reductase (NADH) activity |
C | 0005504 | molecular_function | fatty acid binding |
C | 0005886 | cellular_component | plasma membrane |
C | 0006633 | biological_process | fatty acid biosynthetic process |
C | 0009274 | cellular_component | peptidoglycan-based cell wall |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0030497 | biological_process | fatty acid elongation |
C | 0046677 | biological_process | response to antibiotic |
C | 0050343 | molecular_function | trans-2-enoyl-CoA reductase (NADH) activity |
C | 0070403 | molecular_function | NAD+ binding |
C | 0071768 | biological_process | mycolic acid biosynthetic process |
D | 0004318 | molecular_function | enoyl-[acyl-carrier-protein] reductase (NADH) activity |
D | 0005504 | molecular_function | fatty acid binding |
D | 0005886 | cellular_component | plasma membrane |
D | 0006633 | biological_process | fatty acid biosynthetic process |
D | 0009274 | cellular_component | peptidoglycan-based cell wall |
D | 0016491 | molecular_function | oxidoreductase activity |
D | 0030497 | biological_process | fatty acid elongation |
D | 0046677 | biological_process | response to antibiotic |
D | 0050343 | molecular_function | trans-2-enoyl-CoA reductase (NADH) activity |
D | 0070403 | molecular_function | NAD+ binding |
D | 0071768 | biological_process | mycolic acid biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE NAD A 300 |
Chain | Residue |
A | GLY14 |
A | SER94 |
A | ILE95 |
A | GLY96 |
A | ILE122 |
A | MET147 |
A | ASP148 |
A | PHE149 |
A | LYS165 |
A | ALA191 |
A | GLY192 |
A | ILE15 |
A | PRO193 |
A | ILE194 |
A | THR196 |
A | ALA198 |
A | HOH270 |
A | HOH299 |
A | HOH306 |
A | HOH325 |
A | JPM400 |
A | ILE16 |
A | SER20 |
A | ILE21 |
A | PHE41 |
A | LEU63 |
A | ASP64 |
A | VAL65 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE JPM A 400 |
Chain | Residue |
A | GLY96 |
A | MET98 |
A | PHE149 |
A | TYR158 |
A | MET161 |
A | ALA198 |
A | GLU219 |
A | NAD300 |
site_id | AC3 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE NAD B 310 |
Chain | Residue |
B | GLY14 |
B | ILE15 |
B | ILE16 |
B | SER20 |
B | ILE21 |
B | PHE41 |
B | LEU63 |
B | ASP64 |
B | VAL65 |
B | SER94 |
B | ILE95 |
B | GLY96 |
B | MET147 |
B | ASP148 |
B | PHE149 |
B | MET161 |
B | LYS165 |
B | GLY192 |
B | PRO193 |
B | ILE194 |
B | THR196 |
B | LEU197 |
B | ALA198 |
B | HOH270 |
B | HOH278 |
B | HOH300 |
B | HOH301 |
B | JPM410 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE JPM B 410 |
Chain | Residue |
B | GLY96 |
B | MET98 |
B | MET103 |
B | PHE149 |
B | TYR158 |
B | MET161 |
B | ALA198 |
B | MET199 |
B | NAD310 |
site_id | AC5 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE NAD C 320 |
Chain | Residue |
C | HOH314 |
C | JPM420 |
C | GLY14 |
C | ILE15 |
C | ILE16 |
C | SER20 |
C | ILE21 |
C | PHE41 |
C | LEU63 |
C | ASP64 |
C | VAL65 |
C | SER94 |
C | ILE95 |
C | GLY96 |
C | ILE122 |
C | MET147 |
C | ASP148 |
C | LYS165 |
C | ALA191 |
C | GLY192 |
C | PRO193 |
C | ILE194 |
C | THR196 |
C | ALA198 |
C | HOH279 |
C | HOH288 |
C | HOH293 |
C | HOH308 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE JPM C 420 |
Chain | Residue |
C | GLY96 |
C | MET98 |
C | PHE149 |
C | TYR158 |
C | ALA198 |
C | LEU218 |
C | NAD320 |
site_id | AC7 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE NAD D 330 |
Chain | Residue |
D | GLY14 |
D | ILE15 |
D | ILE16 |
D | SER20 |
D | ILE21 |
D | PHE41 |
D | LEU63 |
D | ASP64 |
D | VAL65 |
D | SER94 |
D | ILE95 |
D | GLY96 |
D | MET147 |
D | ASP148 |
D | PHE149 |
D | MET161 |
D | LYS165 |
D | GLY192 |
D | PRO193 |
D | ILE194 |
D | THR196 |
D | LEU197 |
D | ALA198 |
D | HOH271 |
D | HOH288 |
D | HOH322 |
D | HOH324 |
D | JPM430 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE JPM D 430 |
Chain | Residue |
D | GLY96 |
D | MET98 |
D | MET103 |
D | PHE149 |
D | TYR158 |
D | ALA198 |
D | MET199 |
D | NAD330 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10336454, ECO:0000269|PubMed:16647717, ECO:0000269|PubMed:7886450, ECO:0007744|PDB:1BVR, ECO:0007744|PDB:1ENY, ECO:0007744|PDB:2AQ8 |
Chain | Residue | Details |
A | SER20 | |
B | ILE194 | |
C | SER20 | |
C | ASP64 | |
C | ILE95 | |
C | LYS165 | |
C | ILE194 | |
D | SER20 | |
D | ASP64 | |
D | ILE95 | |
D | LYS165 | |
A | ASP64 | |
D | ILE194 | |
A | ILE95 | |
A | LYS165 | |
A | ILE194 | |
B | SER20 | |
B | ASP64 | |
B | ILE95 | |
B | LYS165 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10336454 |
Chain | Residue | Details |
A | TYR158 | |
B | TYR158 | |
C | TYR158 | |
D | TYR158 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | SITE: May act as an intermediate that passes the hydride ion from NADH to the substrate => ECO:0000305|PubMed:10336454 |
Chain | Residue | Details |
A | PHE149 | |
B | PHE149 | |
C | PHE149 | |
D | PHE149 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | SITE: Transition state stabilizer => ECO:0000305|PubMed:10521269 |
Chain | Residue | Details |
A | TYR158 | |
B | TYR158 | |
C | TYR158 | |
D | TYR158 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:20864541, ECO:0000269|PubMed:21143326 |
Chain | Residue | Details |
A | THR266 | |
B | THR266 | |
C | THR266 | |
D | THR266 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1qsg |
Chain | Residue | Details |
A | TYR158 | |
A | LYS165 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1qsg |
Chain | Residue | Details |
B | TYR158 | |
B | LYS165 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1qsg |
Chain | Residue | Details |
C | TYR158 | |
C | LYS165 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1qsg |
Chain | Residue | Details |
D | TYR158 | |
D | LYS165 |
site_id | CSA5 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1qsg |
Chain | Residue | Details |
A | MET161 | |
A | LYS165 |
site_id | CSA6 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1qsg |
Chain | Residue | Details |
B | MET161 | |
B | LYS165 |
site_id | CSA7 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1qsg |
Chain | Residue | Details |
C | MET161 | |
C | LYS165 |
site_id | CSA8 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1qsg |
Chain | Residue | Details |
D | MET161 | |
D | LYS165 |