3LAD
REFINED CRYSTAL STRUCTURE OF LIPOAMIDE DEHYDROGENASE FROM AZOTOBACTER VINELANDII AT 2.2 ANGSTROMS RESOLUTION. A COMPARISON WITH THE STRUCTURE OF GLUTATHIONE REDUCTASE
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 |
| 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 | 32 |
| Details | BINDING SITE FOR RESIDUE FAD A 480 |
| Chain | Residue |
| A | GLY10 |
| A | THR47 |
| A | CYS48 |
| A | GLY52 |
| A | CYS53 |
| A | SER56 |
| A | LYS57 |
| A | GLY119 |
| A | HIS120 |
| A | GLY121 |
| A | ALA149 |
| A | GLY12 |
| A | SER150 |
| A | GLY151 |
| A | ILE191 |
| A | ARG278 |
| A | LEU285 |
| A | GLY317 |
| A | ASP318 |
| A | LEU325 |
| A | ALA326 |
| A | HIS327 |
| A | PRO13 |
| A | TYR357 |
| A | HOH582 |
| B | HIS450 |
| A | GLY14 |
| A | ILE32 |
| A | GLU33 |
| A | LYS34 |
| A | TYR35 |
| A | GLY46 |
| site_id | AC2 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE FAD B 480 |
| Chain | Residue |
| A | HIS450 |
| A | PRO451 |
| B | ILE9 |
| B | GLY10 |
| B | GLY12 |
| B | PRO13 |
| B | GLY14 |
| B | ILE32 |
| B | GLU33 |
| B | LYS34 |
| B | TYR35 |
| B | GLY46 |
| B | THR47 |
| B | CYS48 |
| B | GLY52 |
| B | CYS53 |
| B | LYS57 |
| B | GLY119 |
| B | HIS120 |
| B | GLY121 |
| B | ALA149 |
| B | SER150 |
| B | GLY151 |
| B | SER152 |
| B | ILE191 |
| B | ARG278 |
| B | GLY317 |
| B | ASP318 |
| B | MET324 |
| B | LEU325 |
| B | ALA326 |
| B | HIS327 |
| B | HOH704 |
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 | GLY45-PRO55 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 36 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"1880807","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| A | GLU455 | |
| A | HIS450 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| B | GLU455 | |
| B | HIS450 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| A | CYS48 | |
| A | CYS53 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| B | CYS48 | |
| B | CYS53 |
