Functional Information from GO Data
Chain | GOid | namespace | contents |
G | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
G | 0005737 | cellular_component | cytoplasm |
G | 0006006 | biological_process | glucose metabolic process |
G | 0006096 | biological_process | glycolytic process |
G | 0016491 | molecular_function | oxidoreductase activity |
G | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
G | 0050661 | molecular_function | NADP binding |
G | 0051287 | molecular_function | NAD binding |
R | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
R | 0005737 | cellular_component | cytoplasm |
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 | ABG |
Number of Residues | 6 |
Details | RESIDUES INTERACTING WITH THE ADENINE BASE OF THE COFACTOR |
Chain | Residue |
G | ASN6 |
G | ASN31 |
G | ASP32 |
G | PHE34 |
G | THR96 |
G | PHE99 |
site_id | ABR |
Number of Residues | 6 |
Details | RESIDUES INTERACTING WITH THE ADENINE BASE OF THE COFACTOR |
Chain | Residue |
R | PHE34 |
R | THR96 |
R | PHE99 |
R | ASN6 |
R | ASN31 |
R | ASP32 |
site_id | AC3 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE NAD G 335 |
Chain | Residue |
G | GLY7 |
G | PHE8 |
G | GLY9 |
G | ARG10 |
G | ILE11 |
G | ASP32 |
G | PHE34 |
G | ILE35 |
G | PHE99 |
G | SER119 |
G | GLU314 |
site_id | AC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE NAD R 339 |
Chain | Residue |
R | PHE8 |
R | ARG10 |
R | ASP32 |
R | THR96 |
R | PHE99 |
R | SER119 |
R | ALA120 |
R | CYS149 |
R | ASN313 |
R | TYR317 |
site_id | AC7 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE PO4 R 337 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PO4 R 338 |
Chain | Residue |
R | THR150 |
R | THR208 |
R | GLY209 |
site_id | APG |
Number of Residues | 2 |
Details | RESIDUES INTERACTING WITH THE PHOSPHATE OF THE ADENOSINE NUCLEOTIDE OF THE NAD COFACTOR |
Chain | Residue |
G | ARG10 |
G | ALA180 |
site_id | APR |
Number of Residues | 2 |
Details | RESIDUES INTERACTING WITH THE PHOSPHATE OF THE ADENOSINE NUCLEOTIDE OF THE NAD COFACTOR |
Chain | Residue |
R | ARG10 |
R | ALA180 |
site_id | ARG |
Number of Residues | 3 |
Details | RESIDUES INTERACTING WITH THE ADENOSINE RIBOSE OF THE NAD COFACTOR |
Chain | Residue |
G | GLY7 |
G | ASP32 |
R | PRO188 |
site_id | ARR |
Number of Residues | 4 |
Details | RESIDUES INTERACTING WITH THE ADENOSINE RIBOSE OF THE NAD COFACTOR |
Chain | Residue |
R | GLY7 |
R | PHE8 |
R | ASP32 |
G | PRO188 |
site_id | NBG |
Number of Residues | 4 |
Details | RESIDUES INTERACTING WITH THE NICOTINAMIDE BASE OF THE NAD COFACTOR |
Chain | Residue |
G | ILE11 |
G | CYS149 |
G | ASN313 |
G | TYR317 |
site_id | NBR |
Number of Residues | 4 |
Details | RESIDUES INTERACTING WITH THE NICOTINAMIDE BASE OF THE NAD COFACTOR |
Chain | Residue |
R | ILE11 |
R | CYS149 |
R | ASN313 |
R | TYR317 |
site_id | NPG |
Number of Residues | 1 |
Details | RESIDUES INTERACTING WITH THE PHOSPHATE OF THE NICOTINAMIDE NUCLEOTIDE OF THE NAD COFACTOR |
site_id | NPR |
Number of Residues | 1 |
Details | RESIDUES INTERACTING WITH THE PHOSPHATE OF THE NICOTINAMIDE NUCLEOTIDE OF THE NAD COFACTOR |
site_id | NRG |
Number of Residues | 4 |
Details | RESIDUES INTERACTING WITH THE RIBOSE OF THE NICOTINAMIDE NUCLEOTIDE OF THE NAD COFACTOR |
Chain | Residue |
G | THR96 |
G | GLY97 |
G | SER119 |
G | ALA120 |
site_id | NRR |
Number of Residues | 4 |
Details | RESIDUES INTERACTING WITH THE RIBOSE OF THE NICOTINAMIDE NUCLEOTIDE OF THE NAD COFACTOR |
Chain | Residue |
R | THR96 |
R | GLY97 |
R | SER119 |
R | ALA120 |
Functional Information from PROSITE/UniProt
site_id | PS00071 |
Number of Residues | 8 |
Details | GAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL |
Chain | Residue | Details |
G | ALA147-LEU154 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile |
Chain | Residue | Details |
G | CYS149 | |
R | CYS149 | |
Chain | Residue | Details |
G | SER119 | |
G | ASN313 | |
R | ARG10 | |
R | ASP32 | |
R | SER119 | |
R | ASN313 | |
G | ARG10 | |
G | ASP32 | |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
R | SER148 | |
R | THR179 | |
R | THR208 | |
R | ARG231 | |
G | ARG231 | |
G | SER148 | |
G | THR179 | |
G | THR208 | |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | SITE: Activates thiol group during catalysis |
Chain | Residue | Details |
G | HIS176 | |
R | HIS176 | |
Chain | Residue | Details |
G | SER1 | |
R | SER1 | |