5U8V
Dihydrolipoamide dehydrogenase (LpdG) from Pseudomonas aeruginosa bound to 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 | 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 | 39 |
| Details | binding site for residue FAD A 501 |
| Chain | Residue |
| A | ILE10 |
| A | CYS49 |
| A | GLY53 |
| A | CYS54 |
| A | SER57 |
| 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 | HIS328 |
| A | TYR358 |
| A | DMS503 |
| A | HOH666 |
| A | HOH671 |
| A | HOH672 |
| A | HOH697 |
| A | HOH823 |
| B | HIS451 |
| B | PRO452 |
| A | PRO14 |
| A | GLY15 |
| A | GLU34 |
| A | TYR36 |
| A | GLY47 |
| A | THR48 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | binding site for residue NAD A 502 |
| Chain | Residue |
| A | ILE187 |
| A | GLY188 |
| A | GLY190 |
| A | VAL191 |
| A | ILE192 |
| A | LEU210 |
| A | GLU211 |
| A | ALA212 |
| A | LEU213 |
| A | ALA243 |
| A | VAL245 |
| A | ALA276 |
| A | VAL277 |
| A | GLY278 |
| A | HOH607 |
| A | HOH608 |
| A | HOH624 |
| A | HOH635 |
| A | HOH791 |
| A | HOH819 |
| A | HOH848 |
| A | HOH876 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue DMS A 503 |
| Chain | Residue |
| A | TYR36 |
| A | GLY47 |
| A | THR48 |
| A | VAL52 |
| A | FAD501 |
| A | HOH653 |
| A | HOH734 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue DMS A 504 |
| Chain | Residue |
| A | ALA324 |
| A | ILE353 |
| A | SER355 |
| A | HOH634 |
| A | HOH851 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue DMS A 505 |
| Chain | Residue |
| A | ASN397 |
| A | ASP398 |
| A | THR399 |
| A | HOH613 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue DMS A 506 |
| Chain | Residue |
| A | PRO162 |
| A | ALA247 |
| A | SER248 |
| A | HOH678 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue DMS A 507 |
| Chain | Residue |
| A | PHE385 |
| A | ALA389 |
| A | GLY391 |
| A | HIS471 |
| A | HOH605 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue DMS A 508 |
| Chain | Residue |
| A | TYR17 |
| A | ALA327 |
| A | SER331 |
| B | HIS451 |
| B | HIS471 |
| B | DMS510 |
| B | HOH609 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue DMS A 509 |
| Chain | Residue |
| A | TYR65 |
| A | GLU69 |
| A | ALA73 |
| A | ALA396 |
| A | ASN397 |
| A | ASP398 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue DMS A 510 |
| Chain | Residue |
| A | LYS215 |
| A | PHE216 |
| A | HOH852 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue DMS B 501 |
| Chain | Residue |
| A | HIS451 |
| A | HIS471 |
| A | HOH612 |
| B | TYR17 |
| B | ALA327 |
| B | SER331 |
| site_id | AD3 |
| Number of Residues | 40 |
| Details | binding site for residue FAD B 502 |
| 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 | LYS58 |
| B | GLY120 |
| B | HIS121 |
| B | GLY122 |
| B | ALA150 |
| B | SER151 |
| B | GLY152 |
| B | SER153 |
| B | SER171 |
| B | ILE192 |
| B | ARG279 |
| B | GLY318 |
| B | ASP319 |
| B | MET325 |
| B | LEU326 |
| B | ALA327 |
| B | HIS328 |
| B | TYR358 |
| B | DMS504 |
| B | HOH687 |
| B | HOH689 |
| B | HOH690 |
| B | HOH799 |
| B | HOH814 |
| B | HOH940 |
| site_id | AD4 |
| Number of Residues | 22 |
| Details | binding site for residue NAD B 503 |
| Chain | Residue |
| B | ILE187 |
| B | GLY188 |
| B | GLY190 |
| B | VAL191 |
| B | ILE192 |
| B | LEU210 |
| B | GLU211 |
| B | ALA212 |
| B | LEU213 |
| B | ALA243 |
| B | ARG244 |
| B | VAL245 |
| B | ALA276 |
| B | VAL277 |
| B | GLY278 |
| B | HOH641 |
| B | HOH713 |
| B | HOH730 |
| B | HOH816 |
| B | HOH831 |
| B | HOH914 |
| B | HOH915 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue DMS B 504 |
| Chain | Residue |
| B | TYR36 |
| B | GLY47 |
| B | VAL52 |
| B | FAD502 |
| B | HOH679 |
| B | HOH771 |
| site_id | AD6 |
| Number of Residues | 6 |
| Details | binding site for residue DMS B 505 |
| Chain | Residue |
| B | PRO159 |
| B | PRO160 |
| B | PRO162 |
| B | ALA247 |
| B | SER248 |
| B | HOH644 |
| site_id | AD7 |
| Number of Residues | 4 |
| Details | binding site for residue DMS B 506 |
| Chain | Residue |
| B | ASN397 |
| B | ASP398 |
| B | THR399 |
| B | HOH626 |
| site_id | AD8 |
| Number of Residues | 2 |
| Details | binding site for residue DMS B 507 |
| Chain | Residue |
| B | GLY383 |
| B | THR384 |
| site_id | AD9 |
| Number of Residues | 5 |
| Details | binding site for residue DMS B 508 |
| Chain | Residue |
| B | ALA324 |
| B | LEU326 |
| B | ILE353 |
| B | SER355 |
| B | HOH606 |
| site_id | AE1 |
| Number of Residues | 3 |
| Details | binding site for residue DMS B 509 |
| Chain | Residue |
| B | PHE216 |
| B | LEU241 |
| B | HOH656 |
| site_id | AE2 |
| Number of Residues | 7 |
| Details | binding site for residue DMS B 510 |
| Chain | Residue |
| A | DMS508 |
| B | ALA389 |
| B | SER390 |
| B | GLY391 |
| B | HIS451 |
| B | HIS471 |
| B | HOH699 |
| site_id | AE3 |
| Number of Residues | 42 |
| 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 | SER153 |
| C | SER171 |
| C | ILE192 |
| C | ARG279 |
| C | GLY318 |
| C | ASP319 |
| C | MET325 |
| C | LEU326 |
| C | ALA327 |
| C | HIS328 |
| C | TYR358 |
| C | DMS507 |
| C | HOH603 |
| C | HOH670 |
| C | HOH676 |
| C | HOH730 |
| C | HOH788 |
| C | HOH921 |
| D | HIS451 |
| D | PRO452 |
| site_id | AE4 |
| Number of Residues | 17 |
| Details | binding site for residue NAD C 502 |
| Chain | Residue |
| C | ILE187 |
| C | GLY188 |
| C | GLY190 |
| C | VAL191 |
| C | ILE192 |
| C | LEU210 |
| C | GLU211 |
| C | ALA212 |
| C | LEU213 |
| C | ALA276 |
| C | VAL277 |
| C | GLY278 |
| C | HOH606 |
| C | HOH672 |
| C | HOH736 |
| C | HOH794 |
| C | HOH819 |
| site_id | AE5 |
| Number of Residues | 4 |
| Details | binding site for residue DMS C 503 |
| Chain | Residue |
| C | ASN397 |
| C | ASP398 |
| C | THR399 |
| C | HOH636 |
| site_id | AE6 |
| Number of Residues | 5 |
| Details | binding site for residue DMS C 504 |
| Chain | Residue |
| C | ALA389 |
| C | GLY391 |
| C | HIS451 |
| C | HIS471 |
| C | HOH692 |
| site_id | AE7 |
| Number of Residues | 4 |
| Details | binding site for residue DMS C 505 |
| Chain | Residue |
| C | TYR65 |
| C | GLU69 |
| C | ALA73 |
| C | ASN397 |
| site_id | AE8 |
| Number of Residues | 4 |
| Details | binding site for residue DMS C 506 |
| Chain | Residue |
| C | GLY383 |
| C | THR384 |
| C | ILE472 |
| C | HOH698 |
| site_id | AE9 |
| Number of Residues | 6 |
| Details | binding site for residue DMS C 507 |
| Chain | Residue |
| C | TYR36 |
| C | GLY47 |
| C | VAL52 |
| C | FAD501 |
| C | HOH771 |
| C | HOH1068 |
| site_id | AF1 |
| Number of Residues | 6 |
| Details | binding site for residue DMS C 508 |
| Chain | Residue |
| C | TYR17 |
| C | ALA327 |
| C | SER331 |
| D | HIS451 |
| D | HIS471 |
| D | HOH630 |
| site_id | AF2 |
| Number of Residues | 3 |
| Details | binding site for residue DMS C 509 |
| Chain | Residue |
| C | ASP214 |
| C | PHE216 |
| C | HOH711 |
| site_id | AF3 |
| Number of Residues | 4 |
| Details | binding site for residue DMS C 510 |
| Chain | Residue |
| C | ILE239 |
| C | ARG240 |
| C | LEU241 |
| C | HOH667 |
| site_id | AF4 |
| Number of Residues | 4 |
| Details | binding site for residue DMS C 511 |
| Chain | Residue |
| C | ALA212 |
| C | LEU213 |
| C | ASP214 |
| C | HOH643 |
| site_id | AF5 |
| Number of Residues | 38 |
| Details | binding site for residue FAD D 501 |
| Chain | Residue |
| C | HIS451 |
| C | PRO452 |
| D | ILE10 |
| D | GLY11 |
| D | GLY13 |
| D | PRO14 |
| D | GLY15 |
| D | GLU34 |
| D | TYR36 |
| D | GLY47 |
| D | THR48 |
| D | CYS49 |
| D | GLY53 |
| D | CYS54 |
| D | SER57 |
| D | LYS58 |
| D | GLY120 |
| D | HIS121 |
| D | GLY122 |
| D | ALA150 |
| D | SER151 |
| D | GLY152 |
| D | SER153 |
| D | SER171 |
| D | ILE192 |
| D | ARG279 |
| D | GLY318 |
| D | ASP319 |
| D | MET325 |
| D | LEU326 |
| D | ALA327 |
| D | HIS328 |
| D | TYR358 |
| D | DMS505 |
| D | HOH664 |
| D | HOH686 |
| D | HOH722 |
| D | HOH952 |
| site_id | AF6 |
| Number of Residues | 23 |
| Details | binding site for residue NAD D 502 |
| Chain | Residue |
| D | ILE187 |
| D | GLY188 |
| D | GLY190 |
| D | VAL191 |
| D | ILE192 |
| D | LEU210 |
| D | GLU211 |
| D | ALA212 |
| D | ALA243 |
| D | ARG244 |
| D | VAL245 |
| D | ALA276 |
| D | VAL277 |
| D | GLY278 |
| D | HOH602 |
| D | HOH607 |
| D | HOH671 |
| D | HOH691 |
| D | HOH820 |
| D | HOH834 |
| D | HOH867 |
| D | HOH901 |
| D | HOH978 |
| site_id | AF7 |
| Number of Residues | 6 |
| Details | binding site for residue DMS D 503 |
| Chain | Residue |
| D | PRO159 |
| D | PRO160 |
| D | PRO162 |
| D | ALA247 |
| D | SER248 |
| D | HOH609 |
| site_id | AF8 |
| Number of Residues | 5 |
| Details | binding site for residue DMS D 504 |
| Chain | Residue |
| D | TYR65 |
| D | ALA73 |
| D | HIS360 |
| D | ASN397 |
| D | ASP398 |
| site_id | AF9 |
| Number of Residues | 5 |
| Details | binding site for residue DMS D 505 |
| Chain | Residue |
| D | TYR36 |
| D | GLY47 |
| D | VAL52 |
| D | FAD501 |
| D | HOH750 |
| site_id | AG1 |
| Number of Residues | 7 |
| Details | binding site for residue DMS D 506 |
| Chain | Residue |
| C | HIS451 |
| C | HIS471 |
| C | HOH627 |
| D | TYR17 |
| D | ALA327 |
| D | SER331 |
| D | HOH639 |
| site_id | AG2 |
| Number of Residues | 6 |
| Details | binding site for residue DMS D 507 |
| Chain | Residue |
| D | GLY383 |
| D | THR384 |
| D | ALA464 |
| D | ILE472 |
| D | ALA473 |
| D | HOH954 |
| site_id | AG3 |
| Number of Residues | 6 |
| Details | binding site for residue DMS D 508 |
| Chain | Residue |
| D | ALA389 |
| D | SER390 |
| D | GLY391 |
| D | HIS451 |
| D | HIS471 |
| D | HOH619 |
| site_id | AG4 |
| Number of Residues | 4 |
| Details | binding site for residue DMS D 509 |
| Chain | Residue |
| D | LYS215 |
| D | PHE216 |
| D | LEU241 |
| D | HOH839 |
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 |
