2B4R
Crystal structure of glyceraldehyde-3-phosphate dehydrogenase from Plasmodium falciparum at 2.25 Angstrom Resolution reveals intriguing extra electron density in the active site
Replaces: 1ZYAFunctional Information from GO Data
| Chain | GOid | namespace | contents |
| O | 0000166 | molecular_function | nucleotide binding |
| 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 | 0016491 | molecular_function | oxidoreductase activity |
| 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 | 0000166 | molecular_function | nucleotide 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 | 0016491 | molecular_function | oxidoreductase activity |
| 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 | 0000166 | molecular_function | nucleotide 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 | 0016491 | molecular_function | oxidoreductase activity |
| 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 | 0000166 | molecular_function | nucleotide 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 | 0016491 | molecular_function | oxidoreductase activity |
| 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 | 25 |
| Details | BINDING SITE FOR RESIDUE NAD Q 501 |
| Chain | Residue |
| P | HOH767 |
| Q | SER98 |
| Q | THR99 |
| Q | GLY100 |
| Q | PHE102 |
| Q | SER122 |
| Q | ALA123 |
| Q | CYS153 |
| Q | THR183 |
| Q | ALA184 |
| Q | ASN319 |
| Q | GLY10 |
| Q | TYR323 |
| Q | HOH513 |
| Q | HOH522 |
| Q | HOH523 |
| Q | HOH549 |
| Q | HOH550 |
| Q | PHE11 |
| Q | GLY12 |
| Q | ARG13 |
| Q | ILE14 |
| Q | ASP35 |
| Q | PRO36 |
| Q | PHE37 |
| site_id | AC2 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NAD P 701 |
| Chain | Residue |
| P | ASN9 |
| P | GLY10 |
| P | GLY12 |
| P | ARG13 |
| P | ILE14 |
| P | ASN34 |
| P | ASP35 |
| P | PRO36 |
| P | PHE37 |
| P | LYS80 |
| P | SER98 |
| P | THR99 |
| P | GLY100 |
| P | SER122 |
| P | ALA123 |
| P | CYS153 |
| P | ALA184 |
| P | ASN319 |
| P | TYR323 |
| P | AES602 |
| P | HOH707 |
| P | HOH711 |
| P | HOH720 |
| P | HOH727 |
| P | HOH732 |
| P | HOH740 |
| P | HOH754 |
| site_id | AC3 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NAD O 801 |
| Chain | Residue |
| O | ASN9 |
| O | GLY10 |
| O | PHE11 |
| O | GLY12 |
| O | ARG13 |
| O | ILE14 |
| O | ASN34 |
| O | ASP35 |
| O | PRO36 |
| O | PHE37 |
| O | MET38 |
| O | GLU79 |
| O | LYS80 |
| O | SER98 |
| O | THR99 |
| O | GLY100 |
| O | SER122 |
| O | ALA123 |
| O | CYS153 |
| O | ALA184 |
| O | ASN319 |
| O | TYR323 |
| O | AES601 |
| O | HOH812 |
| O | HOH829 |
| O | HOH842 |
| O | HOH847 |
| O | HOH853 |
| R | HOH963 |
| site_id | AC4 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NAD R 901 |
| Chain | Residue |
| R | ASN319 |
| R | TYR323 |
| R | AES603 |
| R | HOH904 |
| R | HOH907 |
| R | HOH910 |
| R | HOH918 |
| R | HOH923 |
| R | HOH939 |
| R | HOH941 |
| R | HOH942 |
| R | ASN9 |
| R | GLY10 |
| R | GLY12 |
| R | ARG13 |
| R | ILE14 |
| R | ASN34 |
| R | ASP35 |
| R | PRO36 |
| R | PHE37 |
| R | GLU79 |
| R | LYS80 |
| R | SER98 |
| R | THR99 |
| R | GLY100 |
| R | PHE102 |
| R | SER122 |
| R | ALA123 |
| R | ALA184 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE AES O 601 |
| Chain | Residue |
| O | THR183 |
| O | ASN185 |
| O | NAD801 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE AES P 602 |
| Chain | Residue |
| P | THR183 |
| P | ASN185 |
| P | ARG237 |
| P | NAD701 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE AES R 603 |
| Chain | Residue |
| R | THR183 |
| R | ASN185 |
| R | NAD901 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL R 503 |
| Chain | Residue |
| Q | GLY196 |
| Q | LYS197 |
| Q | ASP198 |
| Q | TRP199 |
| R | GLU283 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL P 703 |
| Chain | Residue |
| O | GLU283 |
| P | GLY196 |
| P | ASP198 |
| P | TRP199 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL O 804 |
| Chain | Residue |
| O | ASP292 |
| O | ASN293 |
| O | ARG294 |
| R | GLU71 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL R 903 |
| Chain | Residue |
| Q | GLU283 |
| R | ASP198 |
| R | TRP199 |
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 |






