6EP8
InhA Y158F mutant in complex with NADH from Mycobacterium tuberculosis
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 301 |
| Chain | Residue |
| A | ASP223 |
| A | GLN224 |
| A | ALA226 |
| A | HOH595 |
| A | HOH598 |
| A | HOH605 |
| site_id | AC2 |
| Number of Residues | 35 |
| Details | binding site for residue NAD A 302 |
| Chain | Residue |
| A | SER20 |
| A | ILE21 |
| A | PHE41 |
| A | LEU63 |
| A | ASP64 |
| A | VAL65 |
| A | SER94 |
| A | ILE95 |
| A | GLY96 |
| A | ILE122 |
| A | MET147 |
| A | ASP148 |
| A | PHE149 |
| A | LYS165 |
| A | ALA191 |
| A | GLY192 |
| A | PRO193 |
| A | ILE194 |
| A | THR196 |
| A | HOH418 |
| A | HOH423 |
| A | HOH443 |
| A | HOH504 |
| A | HOH510 |
| A | HOH511 |
| A | HOH514 |
| A | HOH520 |
| A | HOH528 |
| A | HOH551 |
| A | HOH552 |
| A | HOH576 |
| A | HOH578 |
| A | GLY14 |
| A | ILE15 |
| A | ILE16 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue NA A 303 |
| Chain | Residue |
| A | SER19 |
| A | HIS24 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 304 |
| Chain | Residue |
| A | GLN30 |
| A | ALA34 |
| A | LEU36 |
| A | LYS57 |
| A | HOH480 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 305 |
| Chain | Residue |
| A | GLU68 |
| A | LEU71 |
| A | HOH461 |
| A | HOH548 |
| A | HOH601 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue GOL A 306 |
| Chain | Residue |
| A | GLN30 |
| A | HOH462 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 307 |
| Chain | Residue |
| A | THR2 |
| A | LEU4 |
| A | GLN32 |
| A | TRP249 |
| A | HOH403 |
| A | HOH485 |
| A | HOH488 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue GOL A 308 |
| Chain | Residue |
| A | LEU61 |
| A | GLU62 |
| A | ARG77 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 309 |
| Chain | Residue |
| A | GLY141 |
| A | GLY183 |
| A | PRO251 |
| A | HOH471 |
| A | HOH479 |
| A | HOH508 |
| A | HOH543 |
| A | HOH549 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 310 |
| Chain | Residue |
| A | GLU68 |
| A | PHE109 |
| A | ASP110 |
| A | PRO112 |
| A | TYR125 |
| A | LYS132 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 311 |
| Chain | Residue |
| A | ASP42 |
| A | ARG43 |
| A | LEU44 |
| A | ARG45 |
| A | LEU46 |
| site_id | AD3 |
| Number of Residues | 1 |
| Details | binding site for residue MPD A 312 |
| Chain | Residue |
| A | LYS181 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 5 |
| 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 | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10336454","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| 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 | 1 |
| 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 | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"20864541","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21143326","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
