5KMR
The structure of type II NADH dehydrogenase from Caldalkalibacillus thermarum complexed with NAD+ at 3.0 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 | 26 |
Details | binding site for residue FAD B 601 |
Chain | Residue |
B | GLY10 |
B | THR46 |
B | HIS49 |
B | ASP79 |
B | VAL81 |
B | LEU107 |
B | GLY108 |
B | ILE126 |
B | ASN265 |
B | ILE267 |
B | GLY298 |
B | ALA11 |
B | ASP299 |
B | PRO314 |
B | THR315 |
B | ALA316 |
B | GLN317 |
B | ALA319 |
B | LYS376 |
B | GLY12 |
B | TYR13 |
B | GLY14 |
B | ASN37 |
B | LYS38 |
B | TYR43 |
B | THR45 |
site_id | AC2 |
Number of Residues | 28 |
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 | GLY106 |
A | LEU107 |
A | GLY108 |
A | ILE126 |
A | ASN265 |
A | ILE267 |
A | GLY298 |
A | ASP299 |
A | PRO314 |
A | THR315 |
A | ALA316 |
A | GLN317 |
A | ALA319 |
A | LYS376 |
A | NAD602 |
A | HOH705 |
site_id | AC3 |
Number of Residues | 17 |
Details | binding site for residue NAD A 602 |
Chain | Residue |
A | ILE116 |
A | GLY162 |
A | GLY164 |
A | PHE165 |
A | THR166 |
A | VAL197 |
A | GLU198 |
A | ALA199 |
A | PRO205 |
A | ILE232 |
A | TRP258 |
A | GLY260 |
A | GLY261 |
A | PRO313 |
A | PRO314 |
A | VAL350 |
A | FAD601 |
site_id | AC4 |
Number of Residues | 22 |
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 | VAL81 |
C | LEU107 |
C | GLY108 |
C | ILE126 |
C | ILE267 |
C | GLY298 |
C | ASP299 |
C | PRO314 |
C | THR315 |
C | ALA316 |
C | GLN317 |
C | ALA319 |
C | NAD602 |
site_id | AC5 |
Number of Residues | 17 |
Details | binding site for residue NAD C 602 |
Chain | Residue |
C | ALA199 |
C | ALA200 |
C | PRO205 |
C | ILE232 |
C | THR259 |
C | GLY260 |
C | GLY261 |
C | PRO313 |
C | PRO314 |
C | FAD601 |
C | HOH701 |
C | PHE114 |
C | GLY162 |
C | PHE165 |
C | THR166 |
C | VAL197 |
C | GLU198 |
site_id | AC6 |
Number of Residues | 27 |
Details | binding site for residue FAD D 601 |
Chain | Residue |
D | GLY10 |
D | ALA11 |
D | GLY12 |
D | TYR13 |
D | GLY14 |
D | ASN37 |
D | LYS38 |
D | TYR43 |
D | THR45 |
D | THR46 |
D | ASP79 |
D | VAL81 |
D | GLY106 |
D | LEU107 |
D | GLY108 |
D | ILE126 |
D | ASN265 |
D | ILE267 |
D | GLY298 |
D | ASP299 |
D | PRO314 |
D | THR315 |
D | ALA316 |
D | GLN317 |
D | ALA319 |
D | LYS376 |
D | NAD602 |
site_id | AC7 |
Number of Residues | 20 |
Details | binding site for residue NAD D 602 |
Chain | Residue |
D | PHE114 |
D | ILE116 |
D | GLY162 |
D | GLY164 |
D | PHE165 |
D | THR166 |
D | GLU169 |
D | VAL197 |
D | GLU198 |
D | ALA199 |
D | PRO205 |
D | PRO231 |
D | ILE232 |
D | GLY260 |
D | GLY261 |
D | VAL262 |
D | PRO313 |
D | PRO314 |
D | VAL350 |
D | FAD601 |