3URH
Crystal structure of a dihydrolipoamide dehydrogenase from Sinorhizobium meliloti 1021
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 | 35 |
Details | BINDING SITE FOR RESIDUE FAD A 500 |
Chain | Residue |
A | ILE8 |
A | ARG34 |
A | GLY39 |
A | THR40 |
A | CYS41 |
A | GLY45 |
A | CYS46 |
A | LYS50 |
A | GLY112 |
A | THR113 |
A | GLY114 |
A | GLY9 |
A | ALA142 |
A | THR143 |
A | GLY144 |
A | SER145 |
A | SER165 |
A | ARG275 |
A | GLY314 |
A | ASP315 |
A | MSE321 |
A | LEU322 |
A | SER10 |
A | ALA323 |
A | HIS324 |
A | TYR354 |
A | HOH476 |
A | HOH495 |
B | HIS447 |
A | GLY11 |
A | PRO12 |
A | GLY13 |
A | VAL31 |
A | GLU32 |
A | LYS33 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 501 |
Chain | Residue |
A | ARG296 |
A | ARG318 |
A | GLY319 |
A | HOH595 |
B | LYS286 |
site_id | AC3 |
Number of Residues | 34 |
Details | BINDING SITE FOR RESIDUE FAD B 500 |
Chain | Residue |
A | HIS447 |
B | ILE8 |
B | GLY9 |
B | SER10 |
B | GLY11 |
B | PRO12 |
B | GLY13 |
B | VAL31 |
B | GLU32 |
B | LYS33 |
B | ARG34 |
B | GLY39 |
B | THR40 |
B | CYS41 |
B | GLY45 |
B | CYS46 |
B | LYS50 |
B | GLY112 |
B | THR113 |
B | GLY114 |
B | ALA142 |
B | THR143 |
B | GLY144 |
B | SER145 |
B | ILE186 |
B | ARG275 |
B | GLY314 |
B | ASP315 |
B | MSE321 |
B | LEU322 |
B | ALA323 |
B | HIS324 |
B | TYR354 |
B | HOH503 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 B 501 |
Chain | Residue |
A | HOH606 |
B | ASP280 |
B | GLY281 |
B | LEU282 |
B | GLY283 |
B | HOH563 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO B 502 |
Chain | Residue |
B | GLY184 |
B | VAL185 |
B | ILE186 |
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 | GLY38-PRO48 |