2YQU
Crystal structures and evolutionary relationship of two different lipoamide dehydrogenase(E3s) from Thermus thermophilus
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CO3 B 1501 |
| Chain | Residue |
| B | SER423 |
| B | ASP426 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE CO3 A 1502 |
| Chain | Residue |
| B | HOH1945 |
| A | PRO11 |
| A | ALA310 |
| A | SER314 |
| A | HOH1693 |
| A | HOH1829 |
| A | HOH2036 |
| B | HIS434 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE CO3 B 1503 |
| Chain | Residue |
| A | HIS434 |
| A | HOH1757 |
| A | HOH1816 |
| B | ALA310 |
| B | HIS311 |
| B | SER314 |
| B | HOH1878 |
| B | HOH1940 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 B 1701 |
| Chain | Residue |
| B | ARG396 |
| B | LYS421 |
| B | HOH1780 |
| B | HOH1888 |
| site_id | AC5 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE FAD A 1601 |
| Chain | Residue |
| A | GLY8 |
| A | GLY10 |
| A | PRO11 |
| A | GLY12 |
| A | GLU31 |
| A | LYS32 |
| A | GLU33 |
| A | GLY38 |
| A | THR39 |
| A | CYS40 |
| A | ARG42 |
| A | GLY44 |
| A | CYS45 |
| A | SER48 |
| A | LYS49 |
| A | GLY109 |
| A | THR110 |
| A | ALA111 |
| A | ALA136 |
| A | THR137 |
| A | GLY138 |
| A | ILE178 |
| A | ARG262 |
| A | TYR265 |
| A | GLY301 |
| A | ASP302 |
| A | MET308 |
| A | LEU309 |
| A | ALA310 |
| A | ALA313 |
| A | HOH1610 |
| A | HOH1692 |
| A | HOH1944 |
| A | HOH2033 |
| B | HIS434 |
| B | PRO435 |
| site_id | AC6 |
| Number of Residues | 38 |
| Details | BINDING SITE FOR RESIDUE FAD B 1602 |
| Chain | Residue |
| A | HIS434 |
| A | PRO435 |
| B | GLY8 |
| B | GLY10 |
| B | PRO11 |
| B | GLY12 |
| B | GLU31 |
| B | LYS32 |
| B | GLU33 |
| B | GLY38 |
| B | THR39 |
| B | CYS40 |
| B | ARG42 |
| B | GLY44 |
| B | CYS45 |
| B | SER48 |
| B | LYS49 |
| B | GLY109 |
| B | THR110 |
| B | ALA111 |
| B | ALA136 |
| B | THR137 |
| B | GLY138 |
| B | ILE178 |
| B | ARG262 |
| B | TYR265 |
| B | GLY301 |
| B | ASP302 |
| B | MET308 |
| B | LEU309 |
| B | ALA310 |
| B | HIS311 |
| B | ALA313 |
| B | HOH1704 |
| B | HOH1706 |
| B | HOH1983 |
| B | HOH2072 |
| B | HOH2129 |
Functional Information from PROSITE/UniProt
| site_id | PS00076 |
| Number of Residues | 11 |
| Details | PYRIDINE_REDOX_1 Pyridine nucleotide-disulphide oxidoreductases class-I active site. GGtCLrvGCIP |
| Chain | Residue | Details |
| A | GLY37-PRO47 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| A | GLU439 | |
| A | HIS434 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| B | GLU439 | |
| B | HIS434 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| A | CYS40 | |
| A | CYS45 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| B | CYS40 | |
| B | CYS45 |
