4OXN
Substrate-like binding mode of inhibitor PT155 to the Mycobacterium tuberculosis enoyl-ACP reductase InhA
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 | 0006629 | biological_process | lipid metabolic process |
| A | 0006631 | biological_process | fatty acid metabolic process |
| 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 | 0006629 | biological_process | lipid metabolic process |
| B | 0006631 | biological_process | fatty acid metabolic process |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 32 |
| Details | binding site for residue NAD A 301 |
| 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 | 1S5302 |
| A | HOH405 |
| A | HOH420 |
| A | HOH422 |
| A | HOH426 |
| A | HOH432 |
| A | ILE16 |
| A | HOH457 |
| A | HOH459 |
| A | HOH462 |
| A | SER20 |
| A | ILE21 |
| A | PHE41 |
| A | LEU63 |
| A | ASP64 |
| A | VAL65 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue 1S5 A 302 |
| Chain | Residue |
| A | GLY96 |
| A | MET98 |
| A | MET103 |
| A | MET155 |
| A | TYR158 |
| A | MET199 |
| A | NAD301 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 303 |
| Chain | Residue |
| A | GLU62 |
| A | ARG77 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue 2NV A 304 |
| Chain | Residue |
| A | SER19 |
| A | HIS24 |
| A | ARG195 |
| A | LYS233 |
| A | ASP234 |
| A | ALA235 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue 2NV A 305 |
| Chain | Residue |
| A | GLY221 |
| A | GLN224 |
| A | ARG225 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue 2NV A 307 |
| Chain | Residue |
| A | THR2 |
| A | TRP249 |
| B | THR2 |
| B | TRP249 |
| site_id | AC7 |
| 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 | 1S5302 |
| B | HOH420 |
| B | HOH422 |
| B | HOH427 |
| B | HOH432 |
| B | HOH441 |
| B | HOH443 |
| B | HOH455 |
| B | HOH460 |
| B | HOH476 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | binding site for residue 1S5 B 302 |
| Chain | Residue |
| B | GLY96 |
| B | MET98 |
| B | MET103 |
| B | ALA157 |
| B | TYR158 |
| B | MET199 |
| B | NAD301 |
| B | 2NV305 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue EPE B 303 |
| Chain | Residue |
| B | HIS70 |
| B | ASP42 |
| B | ARG43 |
| B | LEU44 |
| B | ARG45 |
| B | GLU62 |
| site_id | AD1 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 304 |
| Chain | Residue |
| B | GLU62 |
| B | ARG77 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue 2NV B 305 |
| Chain | Residue |
| B | PHE41 |
| B | PHE97 |
| B | MET98 |
| B | 1S5302 |
| B | HOH440 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue 2NV B 306 |
| Chain | Residue |
| B | ARG43 |
| B | LEU197 |
| B | GLY204 |
| B | ALA206 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue 2NV B 307 |
| Chain | Residue |
| A | PHE109 |
| A | ASP110 |
| B | GLU68 |
| B | TYR125 |
| B | LYS132 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue 2NV B 308 |
| Chain | Residue |
| A | TYR125 |
| A | LYS132 |
| B | PHE109 |
| B | ASP110 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10336454","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16647717","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7886450","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BVR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ENY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2AQ8","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10336454","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Site: {"description":"May act as an intermediate that passes the hydride ion from NADH to the substrate","evidences":[{"source":"PubMed","id":"10336454","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"10521269","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"20864541","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21143326","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
