6CMZ
2.3 Angstrom Resolution Crystal Structure of Dihydrolipoamide Dehydrogenase from Burkholderia cenocepacia in Complex with FAD and NAD
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004148 | molecular_function | dihydrolipoyl dehydrogenase (NADH) activity |
| A | 0006103 | biological_process | 2-oxoglutarate metabolic process |
| 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 (NADH) activity |
| B | 0006103 | biological_process | 2-oxoglutarate metabolic process |
| 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 |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004148 | molecular_function | dihydrolipoyl dehydrogenase (NADH) activity |
| C | 0006103 | biological_process | 2-oxoglutarate metabolic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0004148 | molecular_function | dihydrolipoyl dehydrogenase (NADH) activity |
| D | 0006103 | biological_process | 2-oxoglutarate metabolic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
| D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 501 |
| Chain | Residue |
| A | GLY436 |
| B | ARG23 |
| site_id | AC2 |
| Number of Residues | 38 |
| Details | binding site for residue FAD A 502 |
| Chain | Residue |
| A | GLY41 |
| A | THR42 |
| A | CYS43 |
| A | GLY47 |
| A | CYS48 |
| A | SER51 |
| A | LYS52 |
| A | GLY116 |
| A | GLU117 |
| A | ALA118 |
| A | ALA145 |
| A | THR146 |
| A | GLY147 |
| A | SER148 |
| A | TYR185 |
| A | ILE186 |
| A | ARG271 |
| A | ARG274 |
| A | PHE278 |
| A | GLY309 |
| A | GLY12 |
| A | ASP310 |
| A | MET316 |
| A | LEU317 |
| A | ALA318 |
| A | HIS319 |
| A | HOH614 |
| A | HOH617 |
| A | HOH625 |
| A | HOH650 |
| B | HIS442 |
| A | GLY14 |
| B | PRO443 |
| A | PRO15 |
| A | GLY16 |
| A | VAL34 |
| A | GLU35 |
| A | ARG36 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | binding site for residue FAD A 503 |
| Chain | Residue |
| A | VAL151 |
| A | VAL181 |
| A | GLY182 |
| A | GLY184 |
| A | GLU205 |
| A | ALA206 |
| A | PRO212 |
| A | HIS237 |
| A | VAL239 |
| A | ALA268 |
| A | VAL269 |
| A | GLY270 |
| A | ARG290 |
| A | FMN505 |
| A | HOH611 |
| A | HOH686 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue NAD A 504 |
| Chain | Residue |
| A | LEU233 |
| A | TRP234 |
| A | GLN258 |
| A | HOH660 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue FMN A 505 |
| Chain | Residue |
| A | LEU153 |
| A | PRO154 |
| A | FAD503 |
| B | ARG290 |
| B | ADP502 |
| site_id | AC6 |
| Number of Residues | 37 |
| Details | binding site for residue FAD B 501 |
| Chain | Residue |
| B | HOH607 |
| B | HOH630 |
| B | HOH637 |
| A | HIS442 |
| A | PRO443 |
| B | GLY12 |
| B | GLY14 |
| B | PRO15 |
| B | GLY16 |
| B | GLU35 |
| B | ARG36 |
| B | GLY41 |
| B | THR42 |
| B | CYS43 |
| B | GLY47 |
| B | CYS48 |
| B | SER51 |
| B | LYS52 |
| B | GLY116 |
| B | GLU117 |
| B | ALA118 |
| B | ALA145 |
| B | THR146 |
| B | GLY147 |
| B | SER165 |
| B | TYR185 |
| B | ILE186 |
| B | ARG271 |
| B | ARG274 |
| B | PHE278 |
| B | GLY309 |
| B | ASP310 |
| B | MET316 |
| B | LEU317 |
| B | ALA318 |
| B | HIS319 |
| B | HOH604 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | binding site for residue ADP B 502 |
| Chain | Residue |
| A | FMN505 |
| B | VAL151 |
| B | LEU153 |
| B | GLY182 |
| B | ALA183 |
| B | GLY184 |
| B | GLU205 |
| B | ALA206 |
| B | PRO212 |
| B | ALA268 |
| B | VAL269 |
| B | GLY270 |
| B | HOH628 |
| B | HOH638 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | binding site for residue CL C 501 |
| Chain | Residue |
| C | ARG455 |
| site_id | AC9 |
| Number of Residues | 36 |
| Details | binding site for residue FAD C 502 |
| Chain | Residue |
| C | ILE11 |
| C | GLY12 |
| C | GLY14 |
| C | PRO15 |
| C | GLY16 |
| C | GLU35 |
| C | ARG36 |
| C | GLY41 |
| C | THR42 |
| C | CYS43 |
| C | GLY47 |
| C | CYS48 |
| C | SER51 |
| C | LYS52 |
| C | GLY116 |
| C | GLU117 |
| C | ALA118 |
| C | ALA145 |
| C | THR146 |
| C | GLY147 |
| C | TYR185 |
| C | ILE186 |
| C | ARG271 |
| C | ARG274 |
| C | PHE278 |
| C | GLY309 |
| C | ASP310 |
| C | MET316 |
| C | LEU317 |
| C | ALA318 |
| C | HIS319 |
| C | HOH605 |
| C | HOH608 |
| C | HOH646 |
| D | HIS442 |
| D | PRO443 |
| site_id | AD1 |
| Number of Residues | 12 |
| Details | binding site for residue ADP C 503 |
| Chain | Residue |
| C | GLY182 |
| C | GLY184 |
| C | GLU205 |
| C | ALA206 |
| C | PRO212 |
| C | LYS238 |
| C | VAL239 |
| C | ALA268 |
| C | VAL269 |
| C | GLY270 |
| C | HOH637 |
| C | HOH640 |
| site_id | AD2 |
| Number of Residues | 9 |
| Details | binding site for residue MLT D 501 |
| Chain | Residue |
| C | ARG383 |
| C | GLY414 |
| C | LEU445 |
| D | GLU353 |
| D | GLY414 |
| D | SER416 |
| D | GLU417 |
| D | HOH633 |
| D | HOH639 |
| site_id | AD3 |
| Number of Residues | 34 |
| Details | binding site for residue FAD D 502 |
| Chain | Residue |
| C | HIS442 |
| C | PRO443 |
| D | GLY12 |
| D | GLY14 |
| D | PRO15 |
| D | GLY16 |
| D | GLU35 |
| D | ARG36 |
| D | GLY41 |
| D | THR42 |
| D | CYS43 |
| D | GLY47 |
| D | CYS48 |
| D | LYS52 |
| D | GLY116 |
| D | GLU117 |
| D | ALA118 |
| D | ALA145 |
| D | THR146 |
| D | GLY147 |
| D | TYR185 |
| D | ARG271 |
| D | ARG274 |
| D | PHE278 |
| D | GLY309 |
| D | ASP310 |
| D | MET316 |
| D | LEU317 |
| D | ALA318 |
| D | HIS319 |
| D | HOH609 |
| D | HOH614 |
| D | HOH637 |
| D | HOH638 |
| site_id | AD4 |
| Number of Residues | 11 |
| Details | binding site for residue ADP D 503 |
| Chain | Residue |
| D | GLY182 |
| D | GLY184 |
| D | GLU205 |
| D | ALA206 |
| D | PRO212 |
| D | VAL239 |
| D | ALA268 |
| D | VAL269 |
| D | GLY270 |
| D | HOH612 |
| D | HOH628 |
Functional Information from PROSITE/UniProt
| site_id | PS00076 |
| Number of Residues | 11 |
| Details | PYRIDINE_REDOX_1 Pyridine nucleotide-disulphide oxidoreductases class-I active site. GGtCLniGCIP |
| Chain | Residue | Details |
| A | GLY40-PRO50 |
| site_id | PS00435 |
| Number of Residues | 11 |
| Details | PEROXIDASE_1 Peroxidases proximal heme-ligand signature. TVEVVSAGHAV |
| Chain | Residue | Details |
| A | THR125-VAL135 |
