3AFO
Crystal Structure of Yeast NADH Kinase complexed with NADH
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003951 | molecular_function | NAD+ kinase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0006741 | biological_process | NADP+ biosynthetic process |
| A | 0016226 | biological_process | iron-sulfur cluster assembly |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
| A | 0019674 | biological_process | NAD+ metabolic process |
| A | 0034599 | biological_process | cellular response to oxidative stress |
| A | 0042736 | molecular_function | NADH kinase activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003951 | molecular_function | NAD+ kinase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005759 | cellular_component | mitochondrial matrix |
| B | 0006741 | biological_process | NADP+ biosynthetic process |
| B | 0016226 | biological_process | iron-sulfur cluster assembly |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
| B | 0019674 | biological_process | NAD+ metabolic process |
| B | 0034599 | biological_process | cellular response to oxidative stress |
| B | 0042736 | molecular_function | NADH kinase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NAI A 1001 |
| Chain | Residue |
| A | ASP150 |
| A | ALA268 |
| A | TYR269 |
| A | SER272 |
| A | ASP330 |
| A | GLY331 |
| A | HOH3033 |
| A | HOH3134 |
| A | HOH3138 |
| A | HOH3141 |
| A | HOH3148 |
| A | GLY151 |
| A | HOH3189 |
| A | HOH3240 |
| A | HOH3244 |
| B | LEU238 |
| B | ASP256 |
| B | CYS291 |
| B | ARG293 |
| B | HOH3170 |
| A | LEU154 |
| A | GLY177 |
| A | PHE178 |
| A | ASN226 |
| A | ASP227 |
| A | THR264 |
| A | THR267 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MPD A 2001 |
| Chain | Residue |
| A | PHE178 |
| A | LEU179 |
| A | ARG204 |
| A | ASP389 |
| A | GLY393 |
| A | HOH3233 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD A 2002 |
| Chain | Residue |
| A | ALA199 |
| A | LYS200 |
| A | ALA384 |
| A | LYS385 |
| site_id | AC4 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NAI B 1001 |
| Chain | Residue |
| A | LEU238 |
| A | ASP256 |
| A | CYS291 |
| A | ARG293 |
| A | HOH3018 |
| A | HOH3073 |
| A | HOH3128 |
| A | HOH3172 |
| A | HOH3203 |
| A | HOH3220 |
| B | ASP150 |
| B | GLY151 |
| B | LEU154 |
| B | GLY177 |
| B | PHE178 |
| B | ASN226 |
| B | ASP227 |
| B | THR264 |
| B | THR267 |
| B | ALA268 |
| B | TYR269 |
| B | SER272 |
| B | ASP330 |
| B | GLY331 |
| B | HOH3042 |
| B | HOH3165 |
| B | HOH3176 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD B 2001 |
| Chain | Residue |
| B | ALA199 |
| B | LYS200 |
| B | ALA384 |
| B | LYS385 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MPD B 2002 |
| Chain | Residue |
| B | PHE178 |
| B | LEU179 |
| B | PRO181 |
| B | LEU202 |
| B | ARG204 |
| B | ASP389 |
| B | TRP390 |
| B | HOH3011 |
