4OXK
Multiple binding modes of inhibitor PT155 to the Mycobacterium tuberculosis enoyl-ACP reductase InhA within a tetramer
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 | 33 |
| 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 | 1S5301 |
| A | HOH403 |
| A | HOH404 |
| A | HOH407 |
| A | HOH422 |
| A | HOH423 |
| A | ILE16 |
| A | HOH427 |
| A | HOH441 |
| A | HOH479 |
| A | HOH493 |
| A | SER20 |
| A | ILE21 |
| A | PHE41 |
| A | LEU63 |
| A | ASP64 |
| A | VAL65 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue 1S5 A 301 |
| Chain | Residue |
| A | GLY96 |
| A | MET98 |
| A | PRO156 |
| A | ALA157 |
| A | TYR158 |
| A | MET161 |
| A | ALA198 |
| A | MET199 |
| A | LEU218 |
| A | NAD300 |
| site_id | AC3 |
| Number of Residues | 32 |
| Details | binding site for residue NAD B 301 |
| 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 | ILE122 |
| B | MET147 |
| B | ASP148 |
| B | PHE149 |
| B | LYS165 |
| B | ALA191 |
| B | GLY192 |
| B | PRO193 |
| B | ILE194 |
| B | THR196 |
| B | ALA198 |
| B | 1S5302 |
| B | HOH409 |
| B | HOH422 |
| B | HOH429 |
| B | HOH431 |
| B | HOH433 |
| B | HOH440 |
| B | HOH483 |
| B | HOH493 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | binding site for residue 1S5 B 302 |
| Chain | Residue |
| B | GLY96 |
| B | PHE97 |
| B | MET98 |
| B | MET103 |
| B | PHE149 |
| B | PRO156 |
| B | TYR158 |
| B | ALA198 |
| B | MET199 |
| B | ALA201 |
| B | NAD301 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue 2NV B 303 |
| Chain | Residue |
| B | GLY221 |
| B | ARG225 |
| B | 2NV304 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue 2NV B 304 |
| Chain | Residue |
| B | GLN214 |
| B | 2NV303 |
| site_id | AC7 |
| Number of Residues | 33 |
| Details | binding site for residue NAD C 300 |
| Chain | Residue |
| C | VAL65 |
| C | SER94 |
| C | ILE95 |
| C | GLY96 |
| C | ILE122 |
| C | MET147 |
| C | ASP148 |
| C | PHE149 |
| C | LYS165 |
| C | ALA191 |
| C | GLY192 |
| C | PRO193 |
| C | ILE194 |
| C | THR196 |
| C | ALA198 |
| C | 1S5301 |
| C | HOH410 |
| C | HOH415 |
| C | HOH418 |
| C | HOH421 |
| C | HOH427 |
| C | HOH436 |
| C | HOH440 |
| C | HOH470 |
| C | HOH488 |
| C | GLY14 |
| C | ILE15 |
| C | ILE16 |
| C | SER20 |
| C | ILE21 |
| C | PHE41 |
| C | LEU63 |
| C | ASP64 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | binding site for residue 1S5 C 301 |
| Chain | Residue |
| C | GLY96 |
| C | MET98 |
| C | MET103 |
| C | PRO156 |
| C | TYR158 |
| C | ILE194 |
| C | ALA198 |
| C | MET199 |
| C | NAD300 |
| C | HOH471 |
| site_id | AC9 |
| Number of Residues | 32 |
| Details | binding site for residue NAD D 300 |
| 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 | ILE122 |
| D | MET147 |
| D | ASP148 |
| D | PHE149 |
| D | LYS165 |
| D | ALA191 |
| D | GLY192 |
| D | PRO193 |
| D | ILE194 |
| D | THR196 |
| D | ALA198 |
| D | 1S5301 |
| D | HOH412 |
| D | HOH414 |
| D | HOH418 |
| D | HOH424 |
| D | HOH427 |
| D | HOH458 |
| D | HOH475 |
| D | HOH480 |
| site_id | AD1 |
| Number of Residues | 10 |
| Details | binding site for residue 1S5 D 301 |
| Chain | Residue |
| D | GLY96 |
| D | MET98 |
| D | MET103 |
| D | PRO156 |
| D | TYR158 |
| D | ILE194 |
| D | ALA198 |
| D | MET199 |
| D | NAD300 |
| D | HOH529 |
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 |
