5U8U
Dihydrolipoamide dehydrogenase (LpdG) from Pseudomonas aeruginosa
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 |
| A | 0141115 | biological_process | symbiont-mediated suppression of host complement activation by inactivation of complement proteins |
| A | 0141117 | biological_process | symbiont-mediated suppression of host complement activation by recruitment of complement control protein |
| 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 |
| B | 0141115 | biological_process | symbiont-mediated suppression of host complement activation by inactivation of complement proteins |
| B | 0141117 | biological_process | symbiont-mediated suppression of host complement activation by recruitment of complement control protein |
| 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 |
| C | 0141115 | biological_process | symbiont-mediated suppression of host complement activation by inactivation of complement proteins |
| C | 0141117 | biological_process | symbiont-mediated suppression of host complement activation by recruitment of complement control protein |
| 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 |
| D | 0141115 | biological_process | symbiont-mediated suppression of host complement activation by inactivation of complement proteins |
| D | 0141117 | biological_process | symbiont-mediated suppression of host complement activation by recruitment of complement control protein |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 37 |
| Details | binding site for residue FAD A 501 |
| Chain | Residue |
| A | ILE10 |
| A | CYS49 |
| A | GLY53 |
| A | CYS54 |
| A | LYS58 |
| A | GLY120 |
| A | HIS121 |
| A | GLY122 |
| A | ALA150 |
| A | SER151 |
| A | GLY152 |
| A | GLY11 |
| A | SER153 |
| A | ILE192 |
| A | ARG279 |
| A | GLY318 |
| A | ASP319 |
| A | MET325 |
| A | LEU326 |
| A | ALA327 |
| A | HIS328 |
| A | TYR358 |
| A | GLY13 |
| A | DMS504 |
| A | HOH664 |
| A | HOH668 |
| A | HOH671 |
| A | HOH698 |
| A | HOH912 |
| B | HIS451 |
| B | PRO452 |
| A | PRO14 |
| A | GLY15 |
| A | GLU34 |
| A | TYR36 |
| A | GLY47 |
| A | THR48 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue DMS A 502 |
| Chain | Residue |
| A | ASN397 |
| A | ASP398 |
| A | THR399 |
| A | HOH614 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue DMS A 503 |
| Chain | Residue |
| A | ILE353 |
| A | SER355 |
| A | HOH663 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue DMS A 504 |
| Chain | Residue |
| A | TYR36 |
| A | GLY47 |
| A | THR48 |
| A | VAL52 |
| A | FAD501 |
| A | HOH687 |
| A | HOH723 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue DMS A 505 |
| Chain | Residue |
| A | TYR65 |
| A | GLU69 |
| A | ALA73 |
| A | ASN397 |
| A | ASP398 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue DMS A 506 |
| Chain | Residue |
| A | PHE385 |
| A | ALA389 |
| A | GLY391 |
| A | HIS471 |
| A | HOH608 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue DMS A 507 |
| Chain | Residue |
| A | ASP214 |
| A | LYS215 |
| A | PHE216 |
| A | LEU241 |
| A | HOH669 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue DMS A 508 |
| Chain | Residue |
| A | TYR17 |
| A | ALA327 |
| A | SER331 |
| A | HOH659 |
| B | HIS451 |
| B | HIS471 |
| B | HOH607 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue DMS A 509 |
| Chain | Residue |
| A | HIS451 |
| A | HIS471 |
| A | HOH612 |
| B | TYR17 |
| B | ALA327 |
| B | SER331 |
| site_id | AD1 |
| Number of Residues | 37 |
| Details | binding site for residue FAD B 501 |
| Chain | Residue |
| B | SER151 |
| B | GLY152 |
| B | SER153 |
| B | ARG279 |
| B | GLY318 |
| B | ASP319 |
| B | MET325 |
| B | LEU326 |
| B | ALA327 |
| B | HIS328 |
| B | TYR358 |
| B | DMS502 |
| B | HOH665 |
| B | HOH677 |
| B | HOH718 |
| B | HOH785 |
| B | HOH941 |
| 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 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue DMS B 502 |
| Chain | Residue |
| B | TYR36 |
| B | GLY47 |
| B | VAL52 |
| B | FAD501 |
| B | HOH666 |
| B | HOH780 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue DMS B 503 |
| Chain | Residue |
| B | ASN397 |
| B | ASP398 |
| B | THR399 |
| B | HOH639 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue DMS B 504 |
| Chain | Residue |
| B | TYR65 |
| B | GLU69 |
| B | ALA73 |
| B | ASN397 |
| B | ASP398 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue DMS B 505 |
| Chain | Residue |
| B | PRO160 |
| B | PRO162 |
| B | ALA247 |
| B | SER248 |
| B | HOH710 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue DMS B 506 |
| Chain | Residue |
| B | LEU326 |
| B | ILE353 |
| B | SER355 |
| B | HOH622 |
| site_id | AD7 |
| Number of Residues | 5 |
| Details | binding site for residue DMS B 507 |
| Chain | Residue |
| B | GLY383 |
| B | THR384 |
| B | ILE472 |
| B | ALA473 |
| B | HOH914 |
| site_id | AD8 |
| Number of Residues | 5 |
| Details | binding site for residue DMS B 508 |
| Chain | Residue |
| B | PHE385 |
| B | ALA389 |
| B | GLY391 |
| B | HIS471 |
| B | HOH625 |
| site_id | AD9 |
| Number of Residues | 3 |
| Details | binding site for residue DMS B 509 |
| Chain | Residue |
| B | ASP304 |
| B | ASP305 |
| B | HOH641 |
| site_id | AE1 |
| Number of Residues | 5 |
| Details | binding site for residue DMS B 510 |
| Chain | Residue |
| B | TYR67 |
| B | THR85 |
| B | ILE86 |
| B | LEU203 |
| B | HOH1190 |
| site_id | AE2 |
| Number of Residues | 3 |
| Details | binding site for residue DMS B 511 |
| Chain | Residue |
| B | PHE216 |
| B | LEU241 |
| B | HOH684 |
| site_id | AE3 |
| Number of Residues | 4 |
| Details | binding site for residue DMS B 512 |
| Chain | Residue |
| B | ALA212 |
| B | LEU213 |
| B | ASP214 |
| B | HOH800 |
| site_id | AE4 |
| Number of Residues | 39 |
| 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 | GLY53 |
| C | CYS54 |
| C | LYS58 |
| C | GLY120 |
| C | HIS121 |
| C | GLY122 |
| C | ALA150 |
| C | SER151 |
| C | GLY152 |
| C | SER153 |
| C | SER171 |
| C | ARG279 |
| C | GLY318 |
| C | ASP319 |
| C | MET325 |
| C | LEU326 |
| C | ALA327 |
| C | HIS328 |
| C | TYR358 |
| C | DMS505 |
| C | HOH605 |
| C | HOH680 |
| C | HOH684 |
| C | HOH709 |
| C | HOH839 |
| C | HOH952 |
| D | HIS451 |
| D | PRO452 |
| site_id | AE5 |
| Number of Residues | 4 |
| Details | binding site for residue DMS C 502 |
| Chain | Residue |
| C | ASN397 |
| C | ASP398 |
| C | THR399 |
| C | HOH636 |
| site_id | AE6 |
| Number of Residues | 4 |
| Details | binding site for residue DMS C 503 |
| Chain | Residue |
| C | GLY383 |
| C | THR384 |
| C | ALA464 |
| C | ILE472 |
| site_id | AE7 |
| Number of Residues | 5 |
| Details | binding site for residue DMS C 504 |
| Chain | Residue |
| C | ALA389 |
| C | GLY391 |
| C | HIS471 |
| C | HOH736 |
| C | HOH1013 |
| site_id | AE8 |
| Number of Residues | 6 |
| Details | binding site for residue DMS C 505 |
| Chain | Residue |
| C | TYR36 |
| C | GLY47 |
| C | VAL52 |
| C | FAD501 |
| C | HOH678 |
| C | HOH703 |
| site_id | AE9 |
| Number of Residues | 6 |
| Details | binding site for residue DMS C 506 |
| Chain | Residue |
| C | ILE239 |
| C | ARG240 |
| C | LEU241 |
| C | HOH727 |
| C | HOH895 |
| C | HOH1107 |
| site_id | AF1 |
| Number of Residues | 3 |
| Details | binding site for residue DMS C 507 |
| Chain | Residue |
| C | ASP214 |
| C | PHE216 |
| C | HOH758 |
| site_id | AF2 |
| Number of Residues | 4 |
| Details | binding site for residue DMS C 508 |
| Chain | Residue |
| C | TYR65 |
| C | GLU69 |
| C | ALA73 |
| C | ASN397 |
| site_id | AF3 |
| Number of Residues | 6 |
| Details | binding site for residue DMS C 509 |
| Chain | Residue |
| C | TYR17 |
| C | ALA327 |
| C | SER331 |
| D | HIS451 |
| D | HIS471 |
| D | HOH612 |
| site_id | AF4 |
| Number of Residues | 4 |
| Details | binding site for residue DMS C 510 |
| Chain | Residue |
| C | ARG202 |
| C | GLN235 |
| C | LEU237 |
| C | HOH631 |
| site_id | AF5 |
| Number of Residues | 4 |
| Details | binding site for residue DMS C 511 |
| Chain | Residue |
| C | ALA212 |
| C | LEU213 |
| C | ASP214 |
| C | HOH804 |
| site_id | AF6 |
| 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 | ILE33 |
| D | GLU34 |
| D | TYR36 |
| D | GLY47 |
| D | THR48 |
| D | CYS49 |
| D | GLY53 |
| D | CYS54 |
| D | LYS58 |
| D | GLY120 |
| D | HIS121 |
| D | GLY122 |
| D | ALA150 |
| D | SER151 |
| D | GLY152 |
| D | SER153 |
| D | ILE192 |
| D | ARG279 |
| D | GLY318 |
| D | ASP319 |
| D | MET325 |
| D | LEU326 |
| D | ALA327 |
| D | HIS328 |
| D | TYR358 |
| D | DMS503 |
| D | HOH663 |
| D | HOH680 |
| D | HOH702 |
| D | HOH761 |
| D | HOH978 |
| site_id | AF7 |
| Number of Residues | 7 |
| Details | binding site for residue DMS D 502 |
| Chain | Residue |
| D | GLY383 |
| D | THR384 |
| D | ALA464 |
| D | ILE472 |
| D | ALA473 |
| D | ARG475 |
| D | HOH891 |
| site_id | AF8 |
| Number of Residues | 6 |
| Details | binding site for residue DMS D 503 |
| Chain | Residue |
| D | TYR36 |
| D | GLY47 |
| D | VAL52 |
| D | FAD501 |
| D | HOH664 |
| D | HOH683 |
| site_id | AF9 |
| Number of Residues | 4 |
| Details | binding site for residue DMS D 504 |
| Chain | Residue |
| D | LEU326 |
| D | ILE353 |
| D | SER355 |
| D | HOH712 |
| site_id | AG1 |
| Number of Residues | 4 |
| Details | binding site for residue DMS D 505 |
| Chain | Residue |
| D | GLU332 |
| D | GLN347 |
| D | ASN349 |
| D | HOH657 |
| site_id | AG2 |
| Number of Residues | 5 |
| Details | binding site for residue DMS D 506 |
| Chain | Residue |
| D | TYR65 |
| D | ALA73 |
| D | HIS360 |
| D | ASN397 |
| D | ASP398 |
| site_id | AG3 |
| Number of Residues | 5 |
| Details | binding site for residue DMS D 507 |
| Chain | Residue |
| D | PRO160 |
| D | PRO162 |
| D | ALA247 |
| D | SER248 |
| D | HOH632 |
| site_id | AG4 |
| Number of Residues | 7 |
| Details | binding site for residue DMS D 508 |
| Chain | Residue |
| C | HIS451 |
| C | HIS471 |
| C | HOH644 |
| D | TYR17 |
| D | ALA327 |
| D | SER331 |
| D | HOH679 |
| site_id | AG5 |
| Number of Residues | 6 |
| Details | binding site for residue DMS D 509 |
| Chain | Residue |
| D | ALA389 |
| D | SER390 |
| D | GLY391 |
| D | HIS451 |
| D | HIS471 |
| D | HOH624 |
| site_id | AG6 |
| Number of Residues | 2 |
| Details | binding site for residue DMS D 510 |
| Chain | Residue |
| D | PHE216 |
| D | HOH755 |
| site_id | AG7 |
| Number of Residues | 4 |
| Details | binding site for residue DMS D 511 |
| Chain | Residue |
| D | ALA212 |
| D | LEU213 |
| D | ASP214 |
| D | HOH817 |
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 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 112 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
