4NWZ
Structure of bacterial type II NADH dehydrogenase from Caldalkalibacillus thermarum at 2.5A resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019646 | biological_process | aerobic electron transport chain |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019646 | biological_process | aerobic electron transport chain |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0019646 | biological_process | aerobic electron transport chain |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0019646 | biological_process | aerobic electron transport chain |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE FAD A 601 |
| Chain | Residue |
| A | ALA11 |
| A | ASP79 |
| A | THR80 |
| A | VAL81 |
| A | LEU107 |
| A | GLY108 |
| A | ILE126 |
| A | PHE165 |
| A | GLU169 |
| A | ASN265 |
| A | ILE267 |
| A | GLY12 |
| A | GLY298 |
| A | ASP299 |
| A | PRO314 |
| A | THR315 |
| A | ALA316 |
| A | GLN317 |
| A | LYS376 |
| A | HOH726 |
| A | HOH747 |
| A | HOH748 |
| A | TYR13 |
| A | HOH749 |
| A | HOH750 |
| A | HOH752 |
| A | HOH765 |
| A | GLY14 |
| A | ASN37 |
| A | LYS38 |
| A | TYR43 |
| A | THR45 |
| A | THR46 |
| site_id | AC2 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE FAD B 601 |
| Chain | Residue |
| B | GLY10 |
| B | GLY12 |
| B | TYR13 |
| B | GLY14 |
| B | ASN37 |
| B | LYS38 |
| B | TYR43 |
| B | THR45 |
| B | THR46 |
| B | ASP79 |
| B | THR80 |
| B | VAL81 |
| B | GLY106 |
| B | LEU107 |
| B | GLY108 |
| B | ILE126 |
| B | PHE165 |
| B | THR166 |
| B | ASN265 |
| B | ILE267 |
| B | GLY298 |
| B | ASP299 |
| B | PRO314 |
| B | THR315 |
| B | ALA316 |
| B | GLN317 |
| B | LYS376 |
| B | HOH732 |
| B | HOH748 |
| B | HOH750 |
| B | HOH751 |
| B | HOH769 |
| B | HOH771 |
| B | HOH773 |
| B | HOH777 |
| site_id | AC3 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE FAD C 601 |
| Chain | Residue |
| C | GLY10 |
| C | GLY12 |
| C | TYR13 |
| C | GLY14 |
| C | ASN37 |
| C | LYS38 |
| C | TYR43 |
| C | THR45 |
| C | THR46 |
| C | THR80 |
| C | VAL81 |
| C | GLY106 |
| C | LEU107 |
| C | GLY108 |
| C | ILE126 |
| C | PHE165 |
| C | GLU169 |
| C | GLY298 |
| C | ASP299 |
| C | PRO314 |
| C | THR315 |
| C | ALA316 |
| C | GLN317 |
| C | LYS376 |
| C | HOH706 |
| C | HOH716 |
| C | HOH744 |
| C | HOH745 |
| C | HOH752 |
| C | HOH753 |
| site_id | AC4 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE FAD D 601 |
| Chain | Residue |
| D | GLY12 |
| D | TYR13 |
| D | GLY14 |
| D | ASN37 |
| D | LYS38 |
| D | TYR43 |
| D | THR45 |
| D | THR46 |
| D | HIS49 |
| D | ASP79 |
| D | THR80 |
| D | VAL81 |
| D | GLY106 |
| D | GLY108 |
| D | PHE165 |
| D | THR166 |
| D | GLU169 |
| D | GLY298 |
| D | ASP299 |
| D | PRO314 |
| D | THR315 |
| D | ALA316 |
| D | GLN317 |
| D | THR349 |
| D | LYS376 |
| D | GLY10 |
