1N1E
Crystal structure of Leishmania mexicana Glycerol-3-phosphate dehydrogenase complexed with DHAP and NAD
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006072 | biological_process | glycerol-3-phosphate metabolic process |
| 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 |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0006072 | biological_process | glycerol-3-phosphate metabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| B | 0020015 | cellular_component | glycosome |
| B | 0046168 | biological_process | glycerol-3-phosphate catabolic process |
| B | 0051287 | molecular_function | NAD binding |
| B | 0141152 | molecular_function | glycerol-3-phosphate dehydrogenase (NAD+) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE NDE A 400 |
| Chain | Residue |
| A | SER23 |
| A | PHE97 |
| A | THR124 |
| A | LYS125 |
| A | GLY153 |
| A | SER155 |
| A | PHE156 |
| A | ALA157 |
| A | LYS210 |
| A | ASN211 |
| A | THR267 |
| A | GLY24 |
| A | SER273 |
| A | ARG274 |
| A | ASN275 |
| A | ALA297 |
| A | VAL298 |
| A | GLU300 |
| A | HOH428 |
| A | HOH460 |
| A | HOH463 |
| A | HOH466 |
| A | ALA25 |
| A | HOH467 |
| A | HOH469 |
| A | HOH471 |
| A | HOH486 |
| A | HOH525 |
| A | HOH535 |
| A | PHE26 |
| A | HIS45 |
| A | MET46 |
| A | PHE63 |
| A | VAL92 |
| A | PRO94 |
| site_id | AC2 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NDE B 401 |
| Chain | Residue |
| B | SER23 |
| B | GLY24 |
| B | ALA25 |
| B | PHE26 |
| B | HIS45 |
| B | PHE63 |
| B | VAL92 |
| B | PRO94 |
| B | PHE97 |
| B | THR124 |
| B | LYS125 |
| B | GLY153 |
| B | SER155 |
| B | PHE156 |
| B | ALA157 |
| B | LYS210 |
| B | ASN211 |
| B | THR267 |
| B | SER273 |
| B | ARG274 |
| B | ASN275 |
| B | ALA297 |
| B | VAL298 |
| B | GLU300 |
| B | HOH417 |
| B | HOH468 |
| B | HOH473 |
| B | HOH475 |
| B | HOH479 |
| B | HOH525 |
| B | HOH560 |
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 | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000305 |
| Chain | Residue | Details |
| A | LYS210 | |
| B | LYS210 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10801498, ECO:0000269|PubMed:12758080 |
| Chain | Residue | Details |
| A | GLY22 | |
| A | ALA157 | |
| A | VAL298 | |
| A | GLU300 | |
| B | GLY22 | |
| B | ALA157 | |
| B | VAL298 | |
| B | GLU300 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | PHE97 | |
| A | ARG274 | |
| B | PHE97 | |
| B | ARG274 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12758080 |
| Chain | Residue | Details |
| A | LYS125 | |
| B | 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 | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1evy |
| Chain | Residue | Details |
| B | LYS210 | |
| B | 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 |
| site_id | MCSA2 |
| Number of Residues | 2 |
| Details | M-CSA 593 |
| Chain | Residue | Details |
| B | LYS210 | proton acceptor, proton donor |
| B | THR267 | electrostatic stabiliser |
