Functional Information from GO Data
| Chain | GOid | namespace | contents |
| O | 0006006 | biological_process | glucose metabolic process |
| 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 | 0006006 | biological_process | glucose metabolic process |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAD O 2 |
| Chain | Residue |
| O | HOH27 |
| O | GLY84 |
| O | ARG85 |
| O | ILE86 |
| O | ASP106 |
| O | PRO107 |
| O | PHE108 |
| O | ILE109 |
| O | LYS151 |
| O | SER169 |
| O | THR170 |
| O | HOH30 |
| O | GLY171 |
| O | TYR173 |
| O | SER193 |
| O | ALA194 |
| O | ALA255 |
| O | ASN388 |
| O | TYR392 |
| O | GOL416 |
| O | HOH423 |
| O | HOH444 |
| O | HOH31 |
| O | HOH457 |
| O | HOH459 |
| O | HOH491 |
| O | HOH38 |
| O | HOH47 |
| O | HOH55 |
| O | ASN81 |
| O | GLY82 |
| O | PHE83 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL O 1 |
| Chain | Residue |
| O | GLY205 |
| O | VAL206 |
| O | GLU208 |
| O | ASN209 |
| O | LYS234 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL O 415 |
| Chain | Residue |
| O | SER223 |
| O | THR225 |
| O | HIS251 |
| O | THR283 |
| O | ALA304 |
| O | ARG306 |
| O | HOH499 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL O 416 |
| Chain | Residue |
| O | NAD2 |
| O | THR254 |
| O | THR256 |
| O | ARG306 |
| O | HOH459 |
| site_id | AC5 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NAD P 1 |
| Chain | Residue |
| P | ASN81 |
| P | GLY82 |
| P | PHE83 |
| P | GLY84 |
| P | ARG85 |
| P | ILE86 |
| P | ASP106 |
| P | PRO107 |
| P | PHE108 |
| P | LYS151 |
| P | SER169 |
| P | THR170 |
| P | GLY171 |
| P | TYR173 |
| P | SER193 |
| P | ALA194 |
| P | CYS224 |
| P | ALA255 |
| P | PRO263 |
| P | ASN388 |
| P | TYR392 |
| P | GOL416 |
| P | HOH440 |
| P | HOH448 |
| P | HOH451 |
| P | HOH474 |
| P | HOH489 |
| P | HOH517 |
| P | HOH525 |
| P | HOH555 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL P 415 |
| Chain | Residue |
| P | SER223 |
| P | CYS224 |
| P | THR225 |
| P | HIS251 |
| P | THR283 |
| P | ALA304 |
| P | ARG306 |
| P | HOH492 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL P 416 |
| Chain | Residue |
| P | NAD1 |
| P | THR254 |
| P | THR256 |
| P | ARG306 |
| P | HOH451 |
| P | HOH517 |
| P | HOH531 |
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 | ALA222-LEU229 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10009","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21269272","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21269272","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Site: {"description":"Activates thiol group during catalysis"} |