2I5P
Crystal structure of glyceraldehyde-3-phosphate dehydrogenase isoform 1 from K. marxianus
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 | 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 | 0030312 | cellular_component | external encapsulating structure |
| 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 | 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 | 0030312 | cellular_component | external encapsulating structure |
| P | 0050661 | molecular_function | NADP binding |
| P | 0051287 | molecular_function | NAD binding |
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 | ALA147-LEU154 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"UniProtKB","id":"P22513","evidenceCode":"ECO:0000250"},{"source":"PROSITE-ProRule","id":"PRU10009","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P22513","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Site: {"description":"Activates thiol group during catalysis","evidences":[{"source":"UniProtKB","id":"P22513","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P00359","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1szj |
| Chain | Residue | Details |
| O | CYS149 | |
| O | HIS176 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1szj |
| Chain | Residue | Details |
| P | HIS676 | |
| P | CYS649 |






