Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005829 | cellular_component | cytosol |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0006072 | biological_process | glycerol-3-phosphate metabolic process |
A | 0006116 | biological_process | NADH oxidation |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
A | 0020015 | cellular_component | glycosome |
A | 0046168 | biological_process | glycerol-3-phosphate catabolic process |
A | 0051287 | molecular_function | NAD binding |
A | 0141152 | molecular_function | glycerol-3-phosphate dehydrogenase (NAD+) activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CFP A 367 |
Chain | Residue |
A | TRP44 |
A | MET46 |
A | PHE97 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MYS A 500 |
Chain | Residue |
A | PHE165 |
A | LEU342 |
A | HOH563 |
Functional Information from PROSITE/UniProt
site_id | PS00957 |
Number of Residues | 22 |
Details | NAD_G3PDH NAD-dependent glycerol-3-phosphate dehydrogenase signature. SAVKNVLAiGsGVanGLgMGlN |
Chain | Residue | Details |
A | SER207-ASN228 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000305 |
Chain | Residue | Details |
A | LYS210 | |
Chain | Residue | Details |
A | GLY22 | |
A | ALA157 | |
A | VAL298 | |
A | GLU300 | |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | PHE97 | |
A | ARG274 | |
Chain | Residue | Details |
A | LYS125 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1evy |
Chain | Residue | Details |
A | LYS210 | |
A | THR267 | |
site_id | MCSA1 |
Number of Residues | 2 |
Details | M-CSA 593 |
Chain | Residue | Details |
A | LYS210 | proton acceptor, proton donor |
A | THR267 | electrostatic stabiliser |