5TR3
2.5 Angstrom Resolution Crystal Structure of Dihydrolipoyl Dehydrogenase from Pseudomonas putida in Complex with FAD.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004148 | molecular_function | dihydrolipoyl dehydrogenase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004148 | molecular_function | dihydrolipoyl dehydrogenase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 34 |
| Details | binding site for residue FAD A 501 |
| Chain | Residue |
| A | ILE10 |
| A | THR48 |
| A | CYS49 |
| A | GLY53 |
| A | CYS54 |
| A | LYS58 |
| A | GLY120 |
| A | HIS121 |
| A | GLY122 |
| A | ALA150 |
| A | SER151 |
| A | GLY11 |
| A | GLY152 |
| A | SER153 |
| A | SER171 |
| A | ILE192 |
| A | ARG279 |
| A | GLY318 |
| A | ASP319 |
| A | MET325 |
| A | LEU326 |
| A | ALA327 |
| A | GLY13 |
| A | TYR358 |
| A | HOH642 |
| A | HOH684 |
| B | HIS451 |
| B | PRO452 |
| A | PRO14 |
| A | GLY15 |
| A | GLU34 |
| A | LYS35 |
| A | TYR36 |
| A | GLY47 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue TRS A 502 |
| Chain | Residue |
| A | GLU436 |
| B | GLU83 |
| B | MET447 |
| site_id | AC3 |
| Number of Residues | 35 |
| Details | binding site for residue FAD B 501 |
| Chain | Residue |
| A | HIS451 |
| A | PRO452 |
| B | ILE10 |
| B | GLY11 |
| B | GLY13 |
| B | PRO14 |
| B | GLY15 |
| B | GLU34 |
| B | LYS35 |
| B | TYR36 |
| B | GLY47 |
| B | THR48 |
| B | CYS49 |
| B | GLY53 |
| B | CYS54 |
| B | SER57 |
| B | LYS58 |
| B | GLY120 |
| B | HIS121 |
| B | GLY122 |
| B | ALA150 |
| B | SER151 |
| B | GLY152 |
| B | SER171 |
| B | ILE192 |
| B | GLY318 |
| B | ASP319 |
| B | MET325 |
| B | LEU326 |
| B | ALA327 |
| B | HIS328 |
| B | TYR358 |
| B | HOH614 |
| B | HOH628 |
| B | HOH655 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | binding site for residue GOL B 502 |
| Chain | Residue |
| B | GLY323 |
Functional Information from PROSITE/UniProt
| site_id | PS00076 |
| Number of Residues | 11 |
| Details | PYRIDINE_REDOX_1 Pyridine nucleotide-disulphide oxidoreductases class-I active site. GGtCLnvGCIP |
| Chain | Residue | Details |
| A | GLY46-PRO56 |
