2EQ6
Crystal structure of lipoamide dehydrogenase from thermus thermophilus HB8
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 40 |
| Details | BINDING SITE FOR RESIDUE FAD A 1482 |
| Chain | Residue |
| A | ILE15 |
| A | CYS47 |
| A | GLY51 |
| A | CYS52 |
| A | THR55 |
| A | LYS56 |
| A | GLY117 |
| A | PHE118 |
| A | ALA119 |
| A | ALA146 |
| A | THR147 |
| A | GLY16 |
| A | GLY148 |
| A | SER166 |
| A | ARG274 |
| A | ARG277 |
| A | GLY313 |
| A | ASP314 |
| A | LEU320 |
| A | LEU321 |
| A | ALA322 |
| A | HIS323 |
| A | GLY18 |
| A | TYR353 |
| A | HOH1483 |
| A | HOH1485 |
| A | HOH1495 |
| A | HOH1506 |
| A | HOH1527 |
| A | HOH1530 |
| A | HOH1541 |
| A | HOH1648 |
| A | HOH1732 |
| A | PRO19 |
| B | HIS446 |
| A | GLY20 |
| A | GLU39 |
| A | ALA40 |
| A | GLU42 |
| A | GLY45 |
| site_id | AC2 |
| Number of Residues | 40 |
| Details | BINDING SITE FOR RESIDUE FAD B 2482 |
| Chain | Residue |
| A | HIS446 |
| B | ILE15 |
| B | GLY16 |
| B | GLY18 |
| B | PRO19 |
| B | GLY20 |
| B | GLU39 |
| B | ALA40 |
| B | GLU42 |
| B | GLY45 |
| B | CYS47 |
| B | GLY51 |
| B | CYS52 |
| B | THR55 |
| B | LYS56 |
| B | GLY117 |
| B | PHE118 |
| B | ALA119 |
| B | ALA146 |
| B | THR147 |
| B | GLY148 |
| B | SER166 |
| B | ARG274 |
| B | ARG277 |
| B | GLY313 |
| B | ASP314 |
| B | LEU320 |
| B | LEU321 |
| B | ALA322 |
| B | HIS323 |
| B | ALA325 |
| B | TYR353 |
| B | HOH2483 |
| B | HOH2485 |
| B | HOH2496 |
| B | HOH2503 |
| B | HOH2537 |
| B | HOH2538 |
| B | HOH2549 |
| B | HOH2755 |
Functional Information from PROSITE/UniProt
| site_id | PS00076 |
| Number of Residues | 11 |
| Details | PYRIDINE_REDOX_1 Pyridine nucleotide-disulphide oxidoreductases class-I active site. GGvCLnvGCIP |
| Chain | Residue | Details |
| A | GLY44-PRO54 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| A | CYS47 | |
| A | CYS52 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| B | CYS47 | |
| B | CYS52 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| A | GLU451 | |
| A | HIS446 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| B | GLU451 | |
| B | HIS446 |
