5U8W
Dihydrolipoamide dehydrogenase (LpdG) from Pseudomonas aeruginosa bound to NADH
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004148 | molecular_function | dihydrolipoyl dehydrogenase (NADH) activity |
| A | 0005737 | cellular_component | cytoplasm |
| 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 | 0005737 | cellular_component | cytoplasm |
| 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 | 0005737 | cellular_component | cytoplasm |
| 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 | 0005737 | cellular_component | cytoplasm |
| 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 | 40 |
| Details | binding site for residue FAD A 501 |
| Chain | Residue |
| A | ILE10 |
| A | THR48 |
| A | CYS49 |
| A | VAL52 |
| A | GLY53 |
| A | CYS54 |
| A | SER57 |
| A | LYS58 |
| A | GLY120 |
| A | HIS121 |
| A | GLY122 |
| A | GLY11 |
| A | ALA150 |
| A | SER151 |
| A | GLY152 |
| A | SER171 |
| A | ARG279 |
| A | GLY318 |
| A | ASP319 |
| A | MET325 |
| A | LEU326 |
| A | ALA327 |
| A | GLY13 |
| A | HIS328 |
| A | TYR358 |
| A | NAI502 |
| A | HOH605 |
| A | HOH645 |
| A | HOH659 |
| A | HOH661 |
| A | HOH690 |
| A | HOH870 |
| B | HIS451 |
| A | PRO14 |
| B | PRO452 |
| A | GLY15 |
| A | GLU34 |
| A | LYS35 |
| A | TYR36 |
| A | GLY47 |
| site_id | AC2 |
| Number of Residues | 29 |
| Details | binding site for residue NAI A 502 |
| Chain | Residue |
| A | ILE187 |
| A | GLY188 |
| A | GLY190 |
| A | VAL191 |
| A | ILE192 |
| A | GLU195 |
| A | LEU210 |
| A | GLU211 |
| A | ALA212 |
| A | LEU213 |
| A | ALA276 |
| A | VAL277 |
| A | GLY278 |
| A | ARG279 |
| A | MET325 |
| A | LEU326 |
| A | VAL356 |
| A | TYR358 |
| A | FAD501 |
| A | HOH610 |
| A | HOH626 |
| A | HOH632 |
| A | HOH634 |
| A | HOH644 |
| A | HOH667 |
| A | HOH683 |
| A | HOH697 |
| A | HOH710 |
| A | HOH757 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue DMS A 503 |
| Chain | Residue |
| A | ALA389 |
| A | GLY391 |
| A | HOH641 |
| A | HOH798 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue DMS A 504 |
| Chain | Residue |
| A | TYR17 |
| A | ALA327 |
| A | SER331 |
| B | HIS451 |
| B | HIS471 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue DMS A 505 |
| Chain | Residue |
| A | TYR36 |
| A | GLY47 |
| A | THR48 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue DMS A 506 |
| Chain | Residue |
| A | ASN397 |
| A | ASP398 |
| A | THR399 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue DMS A 507 |
| Chain | Residue |
| A | TYR65 |
| A | GLU69 |
| A | ALA73 |
| A | ALA396 |
| A | ASN397 |
| A | ASP398 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue DMS A 508 |
| Chain | Residue |
| A | ASP214 |
| A | PHE216 |
| A | HOH613 |
| A | HOH756 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue DMS A 509 |
| Chain | Residue |
| B | SER331 |
| A | HIS451 |
| A | HIS471 |
| A | HOH629 |
| B | TYR17 |
| B | ALA327 |
| site_id | AD1 |
| Number of Residues | 39 |
| 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 | ILE33 |
| B | GLU34 |
| 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 | SER153 |
| B | ARG279 |
| B | GLY318 |
| B | ASP319 |
| B | MET325 |
| B | LEU326 |
| B | ALA327 |
| B | HIS328 |
| B | TYR358 |
| B | NAI502 |
| B | DMS503 |
| B | HOH625 |
| B | HOH653 |
| B | HOH657 |
| B | HOH666 |
| B | HOH885 |
| site_id | AD2 |
| Number of Residues | 26 |
| Details | binding site for residue NAI B 502 |
| Chain | Residue |
| B | ILE187 |
| B | GLY188 |
| B | GLY190 |
| B | VAL191 |
| B | ILE192 |
| B | GLU195 |
| B | LEU210 |
| B | GLU211 |
| B | ALA212 |
| B | LEU213 |
| B | ALA276 |
| B | VAL277 |
| B | GLY278 |
| B | ARG279 |
| B | MET325 |
| B | LEU326 |
| B | VAL356 |
| B | TYR358 |
| B | FAD501 |
| B | HOH651 |
| B | HOH656 |
| B | HOH660 |
| B | HOH697 |
| B | HOH834 |
| B | HOH842 |
| B | HOH868 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue DMS B 503 |
| Chain | Residue |
| B | TYR36 |
| B | GLY47 |
| B | VAL52 |
| B | FAD501 |
| B | HOH645 |
| B | HOH746 |
| site_id | AD4 |
| Number of Residues | 3 |
| Details | binding site for residue DMS B 504 |
| Chain | Residue |
| B | GLY383 |
| B | THR384 |
| B | ILE472 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue DMS B 505 |
| Chain | Residue |
| B | TYR65 |
| B | GLU69 |
| B | ASN397 |
| B | ASP398 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue DMS B 506 |
| Chain | Residue |
| B | TYR302 |
| B | VAL303 |
| B | LYS308 |
| B | THR309 |
| site_id | AD7 |
| Number of Residues | 40 |
| Details | binding site for residue FAD C 501 |
| Chain | Residue |
| C | ILE10 |
| C | GLY11 |
| C | GLY13 |
| C | PRO14 |
| C | GLY15 |
| C | GLU34 |
| C | LYS35 |
| C | TYR36 |
| C | GLY47 |
| C | THR48 |
| C | CYS49 |
| C | VAL52 |
| C | GLY53 |
| C | CYS54 |
| C | SER57 |
| C | LYS58 |
| C | GLY120 |
| C | HIS121 |
| C | GLY122 |
| C | ALA150 |
| C | SER151 |
| C | GLY152 |
| C | SER171 |
| C | ARG279 |
| C | GLY318 |
| C | ASP319 |
| C | MET325 |
| C | LEU326 |
| C | ALA327 |
| C | HIS328 |
| C | TYR358 |
| C | NAI502 |
| C | DMS504 |
| C | HOH601 |
| C | HOH615 |
| C | HOH651 |
| C | HOH677 |
| C | HOH789 |
| D | HIS451 |
| D | PRO452 |
| site_id | AD8 |
| Number of Residues | 26 |
| Details | binding site for residue NAI C 502 |
| Chain | Residue |
| C | ILE187 |
| C | GLY188 |
| C | GLY190 |
| C | VAL191 |
| C | ILE192 |
| C | GLU195 |
| C | LEU210 |
| C | GLU211 |
| C | ALA212 |
| C | LEU213 |
| C | ALA276 |
| C | VAL277 |
| C | GLY278 |
| C | ARG279 |
| C | MET325 |
| C | LEU326 |
| C | VAL356 |
| C | TYR358 |
| C | FAD501 |
| C | HOH622 |
| C | HOH628 |
| C | HOH648 |
| C | HOH669 |
| C | HOH695 |
| C | HOH701 |
| C | HOH791 |
| site_id | AD9 |
| Number of Residues | 4 |
| Details | binding site for residue DMS C 503 |
| Chain | Residue |
| C | TYR17 |
| C | SER331 |
| D | HIS451 |
| D | HIS471 |
| site_id | AE1 |
| Number of Residues | 6 |
| Details | binding site for residue DMS C 504 |
| Chain | Residue |
| C | TYR36 |
| C | GLY47 |
| C | VAL52 |
| C | FAD501 |
| C | HOH620 |
| C | HOH773 |
| site_id | AE2 |
| Number of Residues | 3 |
| Details | binding site for residue DMS C 505 |
| Chain | Residue |
| C | ALA247 |
| C | SER248 |
| C | HOH606 |
| site_id | AE3 |
| Number of Residues | 5 |
| Details | binding site for residue DMS C 506 |
| Chain | Residue |
| C | TYR65 |
| C | GLU69 |
| C | ALA73 |
| C | ASN397 |
| C | ASP398 |
| site_id | AE4 |
| Number of Residues | 5 |
| Details | binding site for residue DMS C 507 |
| Chain | Residue |
| C | PHE385 |
| C | ALA389 |
| C | SER390 |
| C | GLY391 |
| C | HOH603 |
| site_id | AE5 |
| Number of Residues | 5 |
| Details | binding site for residue DMS C 508 |
| Chain | Residue |
| C | HIS451 |
| C | HIS471 |
| D | TYR17 |
| D | ALA327 |
| D | SER331 |
| site_id | AE6 |
| Number of Residues | 37 |
| Details | binding site for residue FAD D 501 |
| Chain | Residue |
| C | HIS451 |
| C | PRO452 |
| D | GLY11 |
| D | GLY13 |
| D | PRO14 |
| D | GLY15 |
| D | GLU34 |
| D | LYS35 |
| D | TYR36 |
| D | GLY47 |
| D | THR48 |
| D | CYS49 |
| D | VAL52 |
| D | GLY53 |
| D | CYS54 |
| D | LYS58 |
| D | GLY120 |
| D | HIS121 |
| D | GLY122 |
| D | ALA150 |
| D | SER151 |
| D | GLY152 |
| D | SER153 |
| D | SER171 |
| D | ARG279 |
| D | GLY318 |
| D | ASP319 |
| D | MET325 |
| D | LEU326 |
| D | ALA327 |
| D | HIS328 |
| D | TYR358 |
| D | NAI502 |
| D | DMS503 |
| D | HOH631 |
| D | HOH632 |
| D | HOH634 |
| site_id | AE7 |
| Number of Residues | 27 |
| Details | binding site for residue NAI D 502 |
| Chain | Residue |
| D | ILE187 |
| D | GLY188 |
| D | GLY190 |
| D | VAL191 |
| D | ILE192 |
| D | GLU195 |
| D | LEU210 |
| D | GLU211 |
| D | ALA212 |
| D | LEU213 |
| D | ALA243 |
| D | ARG244 |
| D | VAL245 |
| D | ALA276 |
| D | VAL277 |
| D | GLY278 |
| D | ARG279 |
| D | MET325 |
| D | LEU326 |
| D | VAL356 |
| D | TYR358 |
| D | FAD501 |
| D | HOH612 |
| D | HOH626 |
| D | HOH630 |
| D | HOH660 |
| D | HOH672 |
| site_id | AE8 |
| Number of Residues | 6 |
| Details | binding site for residue DMS D 503 |
| Chain | Residue |
| D | TYR36 |
| D | GLY47 |
| D | THR48 |
| D | VAL52 |
| D | FAD501 |
| D | HOH657 |
| site_id | AE9 |
| Number of Residues | 4 |
| Details | binding site for residue DMS D 504 |
| Chain | Residue |
| D | ASN397 |
| D | ASP398 |
| D | THR399 |
| D | HOH604 |
| site_id | AF1 |
| Number of Residues | 5 |
| Details | binding site for residue DMS D 505 |
| Chain | Residue |
| D | ALA389 |
| D | SER390 |
| D | GLY391 |
| D | HIS471 |
| D | HOH602 |
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 |
