1YWG
The structure of glyceraldehyde-3-phosphate dehydrogenase from Plasmodium falciparum
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| O | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| O | 0005737 | cellular_component | cytoplasm |
| O | 0005829 | cellular_component | cytosol |
| O | 0006006 | biological_process | glucose metabolic process |
| O | 0006096 | biological_process | glycolytic process |
| O | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| O | 0050661 | molecular_function | NADP binding |
| O | 0051287 | molecular_function | NAD binding |
| P | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| P | 0005737 | cellular_component | cytoplasm |
| P | 0005829 | cellular_component | cytosol |
| P | 0006006 | biological_process | glucose metabolic process |
| P | 0006096 | biological_process | glycolytic process |
| P | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| P | 0050661 | molecular_function | NADP binding |
| P | 0051287 | molecular_function | NAD binding |
| Q | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| Q | 0005737 | cellular_component | cytoplasm |
| Q | 0005829 | cellular_component | cytosol |
| Q | 0006006 | biological_process | glucose metabolic process |
| Q | 0006096 | biological_process | glycolytic process |
| Q | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| Q | 0050661 | molecular_function | NADP binding |
| Q | 0051287 | molecular_function | NAD binding |
| R | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| R | 0005737 | cellular_component | cytoplasm |
| R | 0005829 | cellular_component | cytosol |
| R | 0006006 | biological_process | glucose metabolic process |
| R | 0006096 | biological_process | glycolytic process |
| R | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| R | 0050661 | molecular_function | NADP binding |
| R | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAD O 401 |
| Chain | Residue |
| O | ASN9 |
| O | PHE37 |
| O | GLU79 |
| O | LYS80 |
| O | SER98 |
| O | THR99 |
| O | PHE102 |
| O | SER122 |
| O | ALA123 |
| O | CYS153 |
| O | THR183 |
| O | GLY10 |
| O | ALA184 |
| O | ASN319 |
| O | TYR323 |
| O | HOH406 |
| O | HOH415 |
| O | HOH469 |
| O | HOH541 |
| O | HOH544 |
| O | HOH586 |
| O | HOH639 |
| O | PHE11 |
| O | HOH659 |
| O | HOH700 |
| O | GLY12 |
| O | ARG13 |
| O | ILE14 |
| O | ASN34 |
| O | ASP35 |
| O | PRO36 |
| site_id | AC2 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NAD P 402 |
| Chain | Residue |
| P | ASN9 |
| P | GLY10 |
| P | PHE11 |
| P | GLY12 |
| P | ARG13 |
| P | ILE14 |
| P | ASN34 |
| P | ASP35 |
| P | PRO36 |
| P | PHE37 |
| P | GLU79 |
| P | LYS80 |
| P | SER98 |
| P | THR99 |
| P | PHE102 |
| P | SER122 |
| P | ALA123 |
| P | CYS153 |
| P | ALA184 |
| P | ASN319 |
| P | TYR323 |
| P | HOH492 |
| P | HOH493 |
| P | HOH563 |
| P | HOH665 |
| P | HOH711 |
| site_id | AC3 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAD Q 403 |
| Chain | Residue |
| P | HOH655 |
| Q | ASN9 |
| Q | GLY10 |
| Q | PHE11 |
| Q | GLY12 |
| Q | ARG13 |
| Q | ILE14 |
| Q | ASN34 |
| Q | ASP35 |
| Q | PRO36 |
| Q | PHE37 |
| Q | GLU79 |
| Q | LYS80 |
| Q | SER98 |
| Q | THR99 |
| Q | PHE102 |
| Q | SER122 |
| Q | ALA123 |
| Q | CYS153 |
| Q | ALA184 |
| Q | ASN319 |
| Q | TYR323 |
| Q | HOH429 |
| Q | HOH436 |
| Q | HOH498 |
| Q | HOH511 |
| Q | HOH716 |
| Q | HOH831 |
| site_id | AC4 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NAD R 404 |
| Chain | Residue |
| R | PHE102 |
| R | SER122 |
| R | ALA123 |
| R | CYS153 |
| R | ALA184 |
| R | ASN319 |
| R | TYR323 |
| R | HOH442 |
| R | HOH471 |
| R | HOH577 |
| R | HOH734 |
| R | HOH736 |
| R | HOH789 |
| R | ASN9 |
| R | GLY10 |
| R | PHE11 |
| R | GLY12 |
| R | ARG13 |
| R | ILE14 |
| R | ASN34 |
| R | ASP35 |
| R | PRO36 |
| R | PHE37 |
| R | GLU79 |
| R | LYS80 |
| R | SER98 |
| R | THR99 |
Functional Information from PROSITE/UniProt
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1szj |
| Chain | Residue | Details |
| O | HIS180 | |
| O | CYS153 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1szj |
| Chain | Residue | Details |
| P | HIS180 | |
| P | CYS153 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1szj |
| Chain | Residue | Details |
| Q | HIS180 | |
| Q | CYS153 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1szj |
| Chain | Residue | Details |
| R | HIS180 | |
| R | CYS153 |






