5KMS
The structure of type II NADH dehydrogenase from Caldalkalibacillus thermarum complexed with NAD+ at 2.5 angstrom 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 | 32 |
| Details | binding site for residue FAD A 601 |
| Chain | Residue |
| A | GLY10 |
| A | THR46 |
| A | ASP79 |
| A | THR80 |
| A | VAL81 |
| A | LEU107 |
| A | GLY108 |
| A | ILE126 |
| A | ASN265 |
| A | ILE267 |
| A | GLY298 |
| A | ALA11 |
| A | ASP299 |
| A | PRO314 |
| A | THR315 |
| A | ALA316 |
| A | GLN317 |
| A | LYS376 |
| A | NAD602 |
| A | HOH703 |
| A | HOH705 |
| A | HOH716 |
| A | GLY12 |
| A | HOH723 |
| A | HOH725 |
| A | HOH738 |
| A | TYR13 |
| A | GLY14 |
| A | ASN37 |
| A | LYS38 |
| A | TYR43 |
| A | THR45 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | binding site for residue NAD A 602 |
| Chain | Residue |
| A | PHE114 |
| A | ILE116 |
| A | GLY162 |
| A | GLY164 |
| A | PHE165 |
| A | THR166 |
| A | VAL197 |
| A | GLU198 |
| A | ALA199 |
| A | PRO205 |
| A | PRO231 |
| A | ILE232 |
| A | THR259 |
| A | GLY260 |
| A | PRO313 |
| A | PRO314 |
| A | THR349 |
| A | VAL350 |
| A | FAD601 |
| A | HOH708 |
| A | HOH714 |
| A | HOH732 |
| site_id | AC3 |
| Number of Residues | 34 |
| 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 | LEU107 |
| B | GLY108 |
| B | ILE126 |
| B | PHE165 |
| B | ASN265 |
| B | ILE267 |
| B | GLY298 |
| B | ASP299 |
| B | PRO314 |
| B | THR315 |
| B | ALA316 |
| B | GLN317 |
| B | ALA319 |
| B | THR349 |
| B | LYS376 |
| B | HOH713 |
| B | HOH714 |
| B | HOH716 |
| B | HOH718 |
| B | HOH723 |
| B | HOH731 |
| B | HOH743 |
| site_id | AC4 |
| Number of Residues | 31 |
| Details | binding site for residue FAD C 601 |
| Chain | Residue |
| C | VAL81 |
| C | GLY106 |
| C | LEU107 |
| C | GLY108 |
| C | ILE126 |
| C | PHE165 |
| C | ASN265 |
| C | ILE267 |
| C | GLY298 |
| C | ASP299 |
| C | PRO314 |
| C | THR315 |
| C | ALA316 |
| C | GLN317 |
| C | LYS376 |
| C | HOH719 |
| C | HOH722 |
| C | HOH728 |
| C | HOH737 |
| C | HOH741 |
| C | GLY10 |
| C | GLY12 |
| C | TYR13 |
| C | GLY14 |
| C | ASN37 |
| C | LYS38 |
| C | TYR43 |
| C | THR45 |
| C | THR46 |
| C | ASP79 |
| C | THR80 |
| site_id | AC5 |
| Number of Residues | 26 |
| Details | binding site for residue FAD D 601 |
| Chain | Residue |
| D | GLY10 |
| D | GLY12 |
| D | TYR13 |
| D | GLY14 |
| D | ASN37 |
| D | LYS38 |
| D | TYR43 |
| D | THR45 |
| D | THR46 |
| D | VAL81 |
| D | LEU107 |
| D | GLY108 |
| D | ILE126 |
| D | PHE165 |
| D | THR166 |
| D | ASN265 |
| D | ILE267 |
| D | GLY298 |
| D | ASP299 |
| D | PRO314 |
| D | THR315 |
| D | ALA316 |
| D | GLN317 |
| D | ALA319 |
| D | LYS376 |
| D | HOH705 |
