3V1Y
Crystal structures of glyceraldehyde-3-phosphate dehydrogenase complexes with NAD
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| A | 0005737 | cellular_component | cytoplasm |
| 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 | 0032991 | cellular_component | protein-containing complex |
| A | 0042301 | molecular_function | phosphate ion binding |
| A | 0050661 | molecular_function | NADP binding |
| A | 0051287 | molecular_function | NAD binding |
| A | 0070403 | molecular_function | NAD+ binding |
| B | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| B | 0005737 | cellular_component | cytoplasm |
| 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 | 0032991 | cellular_component | protein-containing complex |
| B | 0042301 | molecular_function | phosphate ion binding |
| B | 0050661 | molecular_function | NADP binding |
| B | 0051287 | molecular_function | NAD binding |
| B | 0070403 | molecular_function | NAD+ binding |
| C | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| C | 0005737 | cellular_component | cytoplasm |
| 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 | 0032991 | cellular_component | protein-containing complex |
| C | 0042301 | molecular_function | phosphate ion binding |
| C | 0050661 | molecular_function | NADP binding |
| C | 0051287 | molecular_function | NAD binding |
| C | 0070403 | molecular_function | NAD+ 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 | 0032991 | cellular_component | protein-containing complex |
| O | 0042301 | molecular_function | phosphate ion binding |
| O | 0050661 | molecular_function | NADP binding |
| O | 0051287 | molecular_function | NAD binding |
| O | 0070403 | molecular_function | NAD+ binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NAD O 401 |
| Chain | Residue |
| O | ASN9 |
| O | PHE37 |
| O | ARG82 |
| O | SER100 |
| O | THR101 |
| O | GLY102 |
| O | PHE104 |
| O | SER124 |
| O | ALA125 |
| O | CYS154 |
| O | ALA185 |
| O | GLY10 |
| O | ASN318 |
| O | TYR322 |
| O | HOH503 |
| O | HOH511 |
| O | HOH526 |
| O | HOH537 |
| O | HOH567 |
| O | HOH574 |
| O | HOH579 |
| O | HOH584 |
| O | PHE11 |
| O | GLY12 |
| O | ARG13 |
| O | ILE14 |
| O | ASN34 |
| O | ASP35 |
| O | PRO36 |
| site_id | AC2 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NAD A 401 |
| Chain | Residue |
| A | ASN9 |
| A | GLY10 |
| A | PHE11 |
| A | GLY12 |
| A | ARG13 |
| A | ILE14 |
| A | ASN34 |
| A | ASP35 |
| A | PRO36 |
| A | PHE37 |
| A | ARG82 |
| A | SER100 |
| A | THR101 |
| A | GLY102 |
| A | PHE104 |
| A | SER124 |
| A | ALA125 |
| A | CYS154 |
| A | ALA185 |
| A | ASN318 |
| A | TYR322 |
| A | HOH509 |
| A | HOH525 |
| A | HOH538 |
| A | HOH553 |
| A | HOH561 |
| A | HOH570 |
| site_id | AC3 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAD B 401 |
| Chain | Residue |
| B | ASN9 |
| B | GLY10 |
| B | PHE11 |
| B | GLY12 |
| B | ARG13 |
| B | ILE14 |
| B | ASN34 |
| B | ASP35 |
| B | PRO36 |
| B | PHE37 |
| B | ARG82 |
| B | SER100 |
| B | THR101 |
| B | GLY102 |
| B | PHE104 |
| B | SER124 |
| B | ALA125 |
| B | CYS154 |
| B | ALA185 |
| B | ASN318 |
| B | TYR322 |
| B | HOH501 |
| B | HOH515 |
| B | HOH529 |
| B | HOH542 |
| B | HOH543 |
| B | HOH569 |
| B | HOH570 |
| B | HOH571 |
| B | HOH575 |
| B | HOH577 |
| O | HOH538 |
| site_id | AC4 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NAD C 401 |
| Chain | Residue |
| C | SER100 |
| C | THR101 |
| C | GLY102 |
| C | PHE104 |
| C | SER124 |
| C | ALA125 |
| C | CYS154 |
| C | ALA185 |
| C | ASN318 |
| C | TYR322 |
| C | HOH507 |
| C | HOH516 |
| C | HOH521 |
| C | HOH536 |
| C | HOH551 |
| C | HOH564 |
| C | HOH574 |
| C | HOH576 |
| A | HOH527 |
| C | ASN9 |
| C | GLY10 |
| C | PHE11 |
| C | GLY12 |
| C | ARG13 |
| C | ILE14 |
| C | ASP35 |
| C | PRO36 |
| C | PHE37 |
| C | ARG82 |
Functional Information from PROSITE/UniProt
| site_id | PS00071 |
| Number of Residues | 8 |
| Details | GAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL |
| Chain | Residue | Details |
| O | ALA152-LEU159 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10009","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22903596","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Site: {"description":"Activates thiol group during catalysis","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |






