6AWA
1.83 Angstrom Resolution Crystal Structure of Dihydrolipoyl Dehydrogenase from Pseudomonas putida in Complex with FAD and Adenosine-5'-monophosphate.
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 | 17 |
| Details | binding site for residue AMP A 501 |
| Chain | Residue |
| A | ILE187 |
| A | ALA276 |
| A | VAL277 |
| A | GLY278 |
| A | HOH616 |
| A | HOH625 |
| A | HOH629 |
| A | HOH648 |
| A | HOH703 |
| A | GLY188 |
| A | LEU210 |
| A | GLU211 |
| A | ALA212 |
| A | LEU213 |
| A | ALA243 |
| A | ARG244 |
| A | VAL245 |
| site_id | AC2 |
| Number of Residues | 37 |
| Details | binding site for residue FAD A 502 |
| Chain | Residue |
| A | ILE10 |
| A | GLY11 |
| A | GLY13 |
| A | PRO14 |
| A | GLY15 |
| A | ILE33 |
| A | GLU34 |
| A | LYS35 |
| A | GLY47 |
| A | THR48 |
| A | CYS49 |
| A | GLY53 |
| A | CYS54 |
| A | SER57 |
| A | LYS58 |
| A | GLY120 |
| A | HIS121 |
| A | GLY122 |
| A | ALA150 |
| A | SER151 |
| A | GLY152 |
| A | SER153 |
| A | ILE192 |
| A | ARG279 |
| A | GLY318 |
| A | ASP319 |
| A | MET325 |
| A | LEU326 |
| A | ALA327 |
| A | HIS328 |
| A | TYR358 |
| A | HOH656 |
| A | HOH666 |
| A | HOH729 |
| A | HOH741 |
| B | HIS451 |
| B | PRO452 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 503 |
| Chain | Residue |
| A | PHE177 |
| A | GLN178 |
| A | ALA179 |
| A | LYS272 |
| A | HOH641 |
| A | HOH742 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 504 |
| Chain | Residue |
| A | LYS123 |
| A | ALA288 |
| A | SER289 |
| site_id | AC5 |
| Number of Residues | 15 |
| Details | binding site for residue AMP B 501 |
| Chain | Residue |
| B | ILE187 |
| B | GLY188 |
| B | LEU210 |
| B | GLU211 |
| B | ALA212 |
| B | LEU213 |
| B | ALA243 |
| B | VAL245 |
| B | VAL277 |
| B | GLY278 |
| B | HOH606 |
| B | HOH607 |
| B | HOH671 |
| B | HOH774 |
| B | HOH796 |
| site_id | AC6 |
| Number of Residues | 38 |
| Details | binding site for residue FAD B 502 |
| Chain | Residue |
| B | SER151 |
| B | GLY152 |
| B | ILE192 |
| B | ARG279 |
| B | GLY318 |
| B | ASP319 |
| B | MET325 |
| B | LEU326 |
| B | ALA327 |
| B | HIS328 |
| B | TYR358 |
| B | HOH615 |
| B | HOH627 |
| B | HOH658 |
| B | HOH681 |
| B | HOH773 |
| B | HOH797 |
| A | HIS451 |
| A | PRO452 |
| B | ILE10 |
| B | GLY11 |
| B | GLY13 |
| B | PRO14 |
| B | GLY15 |
| B | ILE33 |
| B | GLU34 |
| B | LYS35 |
| B | GLY47 |
| B | THR48 |
| B | CYS49 |
| B | GLY53 |
| B | CYS54 |
| B | SER57 |
| B | LYS58 |
| B | GLY120 |
| B | HIS121 |
| B | GLY122 |
| B | ALA150 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 503 |
| Chain | Residue |
| B | LYS123 |
| B | ALA288 |
| B | SER289 |
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 |
