5WED
Structure of bacterial type II NADH dehydrogenase from Caldalkalibacillus thermarum at 2.15A 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 | 36 |
Details | binding site for residue FAD B 601 |
Chain | Residue |
B | GLY10 |
B | HIS49 |
B | ASP79 |
B | VAL81 |
B | LEU107 |
B | GLY108 |
B | ILE126 |
B | PHE165 |
B | THR166 |
B | ASN265 |
B | ILE267 |
B | GLY12 |
B | GLY298 |
B | ASP299 |
B | PRO314 |
B | THR315 |
B | ALA316 |
B | GLN317 |
B | LYS376 |
B | HOH709 |
B | HOH716 |
B | HOH745 |
B | TYR13 |
B | HOH756 |
B | HOH757 |
B | HOH758 |
B | HOH762 |
B | HOH781 |
B | HOH782 |
B | HOH786 |
B | GLY14 |
B | ASN37 |
B | LYS38 |
B | TYR43 |
B | THR45 |
B | THR46 |
site_id | AC2 |
Number of Residues | 40 |
Details | binding site for residue FAD A 601 |
Chain | Residue |
A | GLY10 |
A | GLY12 |
A | TYR13 |
A | GLY14 |
A | ASN37 |
A | LYS38 |
A | TYR43 |
A | THR45 |
A | THR46 |
A | ASP79 |
A | THR80 |
A | VAL81 |
A | LEU107 |
A | GLY108 |
A | ILE126 |
A | PHE165 |
A | THR166 |
A | ASN265 |
A | ILE267 |
A | GLY298 |
A | ASP299 |
A | PRO314 |
A | THR315 |
A | ALA316 |
A | GLN317 |
A | THR349 |
A | LYS376 |
A | HOH704 |
A | HOH717 |
A | HOH720 |
A | HOH730 |
A | HOH739 |
A | HOH748 |
A | HOH751 |
A | HOH756 |
A | HOH771 |
A | HOH773 |
A | HOH780 |
A | HOH782 |
A | HOH791 |
site_id | AC3 |
Number of Residues | 39 |
Details | binding site for residue FAD C 601 |
Chain | Residue |
C | THR315 |
C | ALA316 |
C | GLN317 |
C | THR349 |
C | LYS376 |
C | HOH721 |
C | HOH723 |
C | HOH733 |
C | HOH747 |
C | HOH751 |
C | HOH757 |
C | HOH758 |
C | HOH762 |
C | HOH765 |
C | HOH784 |
C | HOH790 |
C | GLY10 |
C | GLY12 |
C | TYR13 |
C | GLY14 |
C | ASN37 |
C | LYS38 |
C | TYR43 |
C | THR45 |
C | THR46 |
C | ASP79 |
C | THR80 |
C | VAL81 |
C | GLY106 |
C | LEU107 |
C | GLY108 |
C | ILE126 |
C | PHE165 |
C | THR166 |
C | ASN265 |
C | ILE267 |
C | GLY298 |
C | ASP299 |
C | PRO314 |
site_id | AC4 |
Number of Residues | 34 |
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 | ASP79 |
D | VAL81 |
D | LEU107 |
D | GLY108 |
D | ILE126 |
D | PHE165 |
D | THR166 |
D | ILE267 |
D | GLY298 |
D | ASP299 |
D | PRO314 |
D | THR315 |
D | ALA316 |
D | GLN317 |
D | LYS376 |
D | HOH709 |
D | HOH713 |
D | HOH716 |
D | HOH719 |
D | HOH724 |
D | HOH733 |
D | HOH735 |
D | HOH747 |
D | HOH753 |
D | HOH755 |