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 |