1VSV
Crystal Structure of holo-glyceraldehyde 3-phosphate dehydrogenase from Cryptosporidium parvum
Replaces: 3CIEFunctional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006006 | biological_process | glucose metabolic process |
| A | 0006096 | biological_process | glycolytic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0050661 | molecular_function | NADP binding |
| A | 0051287 | molecular_function | NAD binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006006 | biological_process | glucose metabolic process |
| B | 0006096 | biological_process | glycolytic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0050661 | molecular_function | NADP binding |
| B | 0051287 | molecular_function | NAD binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| C | 0005829 | cellular_component | cytosol |
| C | 0006006 | biological_process | glucose metabolic process |
| C | 0006096 | biological_process | glycolytic process |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0050661 | molecular_function | NADP binding |
| C | 0051287 | molecular_function | NAD binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| D | 0005829 | cellular_component | cytosol |
| D | 0006006 | biological_process | glucose metabolic process |
| D | 0006096 | biological_process | glycolytic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0050661 | molecular_function | NADP binding |
| D | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NAD A 340 |
| Chain | Residue |
| A | ASN8 |
| A | PHE36 |
| A | MET37 |
| A | LYS79 |
| A | SER97 |
| A | THR98 |
| A | GLY99 |
| A | PHE101 |
| A | SER121 |
| A | ALA122 |
| A | CYS153 |
| A | GLY9 |
| A | ALA184 |
| A | ASN319 |
| A | TYR323 |
| A | HOH351 |
| A | HOH373 |
| A | HOH425 |
| A | HOH459 |
| A | HOH494 |
| A | HOH517 |
| A | HOH601 |
| A | PHE10 |
| D | HOH464 |
| A | GLY11 |
| A | ARG12 |
| A | ILE13 |
| A | ASN33 |
| A | ASP34 |
| A | PRO35 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE NAD B 340 |
| Chain | Residue |
| B | ASN8 |
| B | GLY9 |
| B | GLY11 |
| B | ARG12 |
| B | ILE13 |
| B | ASN33 |
| B | ASP34 |
| B | PRO35 |
| B | PHE36 |
| B | MET37 |
| B | LYS79 |
| B | SER97 |
| B | THR98 |
| B | GLY99 |
| B | PHE101 |
| B | SER121 |
| B | ALA122 |
| B | CYS153 |
| B | ASN319 |
| B | TYR323 |
| B | HOH461 |
| B | HOH626 |
| site_id | AC3 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE NAD C 340 |
| Chain | Residue |
| C | ASN8 |
| C | GLY9 |
| C | PHE10 |
| C | GLY11 |
| C | ARG12 |
| C | ILE13 |
| C | ASN33 |
| C | ASP34 |
| C | PRO35 |
| C | PHE36 |
| C | MET37 |
| C | LYS79 |
| C | SER97 |
| C | THR98 |
| C | GLY99 |
| C | PHE101 |
| C | SER121 |
| C | ALA122 |
| C | CYS153 |
| C | ALA184 |
| C | ASN319 |
| C | TYR323 |
| C | HOH717 |
| site_id | AC4 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE NAD D 340 |
| Chain | Residue |
| D | HOH345 |
| D | HOH358 |
| D | HOH364 |
| D | HOH379 |
| D | HOH385 |
| D | HOH457 |
| D | HOH474 |
| D | HOH510 |
| D | HOH602 |
| D | HOH638 |
| A | HOH415 |
| D | ASN8 |
| D | GLY9 |
| D | PHE10 |
| D | GLY11 |
| D | ARG12 |
| D | ILE13 |
| D | ASN33 |
| D | ASP34 |
| D | PRO35 |
| D | PHE36 |
| D | MET37 |
| D | ALA78 |
| D | LYS79 |
| D | SER97 |
| D | THR98 |
| D | GLY99 |
| D | PHE101 |
| D | SER121 |
| D | ALA122 |
| D | CYS153 |
| D | ALA184 |
| D | ASN319 |
| D | TYR323 |
Functional Information from PROSITE/UniProt
| site_id | PS00071 |
| Number of Residues | 8 |
| Details | GAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL |
| Chain | Residue | Details |
| A | ALA151-LEU158 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1szj |
| Chain | Residue | Details |
| A | HIS180 | |
| A | CYS153 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1szj |
| Chain | Residue | Details |
| B | HIS180 | |
| B | CYS153 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1szj |
| Chain | Residue | Details |
| C | HIS180 | |
| C | CYS153 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1szj |
| Chain | Residue | Details |
| D | HIS180 | |
| D | CYS153 |
