4GPD
THE STRUCTURE OF LOBSTER APO-D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE AT 3.0 ANGSTROMS RESOLUTION
Replaces: 2GPDFunctional Information from GO Data
| Chain | GOid | namespace | contents |
| 1 | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| 1 | 0005737 | cellular_component | cytoplasm |
| 1 | 0006006 | biological_process | glucose metabolic process |
| 1 | 0006096 | biological_process | glycolytic process |
| 1 | 0016491 | molecular_function | oxidoreductase activity |
| 1 | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| 1 | 0050661 | molecular_function | NADP binding |
| 1 | 0051287 | molecular_function | NAD binding |
| 2 | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| 2 | 0005737 | cellular_component | cytoplasm |
| 2 | 0006006 | biological_process | glucose metabolic process |
| 2 | 0006096 | biological_process | glycolytic process |
| 2 | 0016491 | molecular_function | oxidoreductase activity |
| 2 | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| 2 | 0050661 | molecular_function | NADP binding |
| 2 | 0051287 | molecular_function | NAD binding |
| 3 | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| 3 | 0005737 | cellular_component | cytoplasm |
| 3 | 0006006 | biological_process | glucose metabolic process |
| 3 | 0006096 | biological_process | glycolytic process |
| 3 | 0016491 | molecular_function | oxidoreductase activity |
| 3 | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| 3 | 0050661 | molecular_function | NADP binding |
| 3 | 0051287 | molecular_function | NAD binding |
| 4 | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| 4 | 0005737 | cellular_component | cytoplasm |
| 4 | 0006006 | biological_process | glucose metabolic process |
| 4 | 0006096 | biological_process | glycolytic process |
| 4 | 0016491 | molecular_function | oxidoreductase activity |
| 4 | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| 4 | 0050661 | molecular_function | NADP binding |
| 4 | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AB1 |
| Number of Residues | 6 |
| Details | RESIDUES INTERACTING WITH THE ADENINE BASE OF THE COFACTOR |
| Chain | Residue |
| 1 | ASN6 |
| 1 | ASN30 |
| 1 | ASP31 |
| 1 | PHE33 |
| 1 | THR95 |
| 1 | PHE98 |
| site_id | AB2 |
| Number of Residues | 6 |
| Details | RESIDUES INTERACTING WITH THE ADENINE BASE OF THE COFACTOR |
| Chain | Residue |
| 2 | ASN6 |
| 2 | ASN30 |
| 2 | ASP31 |
| 2 | PHE33 |
| 2 | THR95 |
| 2 | PHE98 |
| site_id | AB3 |
| Number of Residues | 6 |
| Details | RESIDUES INTERACTING WITH THE ADENINE BASE OF THE COFACTOR |
| Chain | Residue |
| 3 | ASN6 |
| 3 | ASN30 |
| 3 | ASP31 |
| 3 | PHE33 |
| 3 | THR95 |
| 3 | PHE98 |
| site_id | AB4 |
| Number of Residues | 6 |
| Details | RESIDUES INTERACTING WITH THE ADENINE BASE OF THE COFACTOR |
| Chain | Residue |
| 4 | ASN6 |
| 4 | ASN30 |
| 4 | ASP31 |
| 4 | PHE33 |
| 4 | THR95 |
| 4 | PHE98 |
| site_id | AP1 |
| Number of Residues | 2 |
| Details | RESIDUES INTERACTING WITH THE PHOSPHATE OF THE ADENOSINE NUCLEOTIDE OF THE NAD COFACTOR. |
| Chain | Residue |
| 1 | ALA179 |
| 1 | ARG10 |
| site_id | AP2 |
| Number of Residues | 2 |
| Details | RESIDUES INTERACTING WITH THE PHOSPHATE OF THE ADENOSINE NUCLEOTIDE OF THE NAD COFACTOR. |
| Chain | Residue |
| 2 | ARG10 |
| 2 | ALA179 |
| site_id | AP3 |
| Number of Residues | 2 |
| Details | RESIDUES INTERACTING WITH THE PHOSPHATE OF THE ADENOSINE NUCLEOTIDE OF THE NAD COFACTOR. |
| Chain | Residue |
| 3 | ARG10 |
| 3 | ALA179 |
| site_id | AP4 |
| Number of Residues | 2 |
| Details | RESIDUES INTERACTING WITH THE PHOSPHATE OF THE ADENOSINE NUCLEOTIDE OF THE NAD COFACTOR. |
| Chain | Residue |
| 4 | ARG10 |
| 4 | ALA179 |
| site_id | AR1 |
| Number of Residues | 2 |
| Details | RESIDUES INTERACTING WITH THE ADENOSINE RIBOSE OF THE NAD COFACTOR |
| Chain | Residue |
| 1 | GLY7 |
| 1 | ASP31 |
| site_id | AR2 |
| Number of Residues | 2 |
| Details | RESIDUES INTERACTING WITH THE ADENOSINE RIBOSE OF THE NAD COFACTOR |
| Chain | Residue |
| 2 | GLY7 |
| 2 | ASP31 |
| site_id | AR3 |
| Number of Residues | 2 |
| Details | RESIDUES INTERACTING WITH THE ADENOSINE RIBOSE OF THE NAD COFACTOR |
| Chain | Residue |
| 3 | GLY7 |
| 3 | ASP31 |
| site_id | AR4 |
| Number of Residues | 2 |
| Details | RESIDUES INTERACTING WITH THE ADENOSINE RIBOSE OF THE NAD COFACTOR |
| Chain | Residue |
| 4 | GLY7 |
| 4 | ASP31 |
| site_id | NB1 |
| Number of Residues | 4 |
| Details |
| Chain | Residue |
| 1 | ILE11 |
| 1 | CYS148 |
| 1 | ASN312 |
| 1 | TYR316 |
| site_id | NB2 |
| Number of Residues | 4 |
| Details |
| Chain | Residue |
| 2 | ILE11 |
| 2 | CYS148 |
| 2 | ASN312 |
| 2 | TYR316 |
| site_id | NB3 |
| Number of Residues | 4 |
| Details |
| Chain | Residue |
| 3 | ILE11 |
| 3 | CYS148 |
| 3 | ASN312 |
| 3 | TYR316 |
| site_id | NB4 |
| Number of Residues | 4 |
| Details |
| Chain | Residue |
| 4 | ILE11 |
| 4 | CYS148 |
| 4 | ASN312 |
| 4 | TYR316 |
| site_id | NP1 |
| Number of Residues | 1 |
| Details | RESIDUES INTERACTING WITH THE PHOSPHATE OF THE NICOTINAMIDE NUCLEOTIDE OF THE NAD COFACTOR |
| Chain | Residue |
| 1 | ILE11 |
| site_id | NP2 |
| Number of Residues | 1 |
| Details | RESIDUES INTERACTING WITH THE PHOSPHATE OF THE NICOTINAMIDE NUCLEOTIDE OF THE NAD COFACTOR |
| Chain | Residue |
| 2 | ILE11 |
| site_id | NP3 |
| Number of Residues | 1 |
| Details | RESIDUES INTERACTING WITH THE PHOSPHATE OF THE NICOTINAMIDE NUCLEOTIDE OF THE NAD COFACTOR |
| Chain | Residue |
| 3 | ILE11 |
| site_id | NP4 |
| Number of Residues | 1 |
| Details | RESIDUES INTERACTING WITH THE PHOSPHATE OF THE NICOTINAMIDE NUCLEOTIDE OF THE NAD COFACTOR |
| Chain | Residue |
| 4 | ILE11 |
| site_id | NR1 |
| Number of Residues | 4 |
| Details | RESIDUES INTERACTING WITH THE RIBOSE OF THE NICOTINAMIDE NUCLEOTIDE OF THE NAD COFACTOR |
| Chain | Residue |
| 1 | THR95 |
| 1 | GLY96 |
| 1 | SER118 |
| 1 | ALA119 |
| site_id | NR2 |
| Number of Residues | 4 |
| Details | RESIDUES INTERACTING WITH THE RIBOSE OF THE NICOTINAMIDE NUCLEOTIDE OF THE NAD COFACTOR |
| Chain | Residue |
| 2 | THR95 |
| 2 | GLY96 |
| 2 | SER118 |
| 2 | ALA119 |
| site_id | NR3 |
| Number of Residues | 4 |
| Details | RESIDUES INTERACTING WITH THE RIBOSE OF THE NICOTINAMIDE NUCLEOTIDE OF THE NAD COFACTOR |
| Chain | Residue |
| 3 | THR95 |
| 3 | GLY96 |
| 3 | SER118 |
| 3 | ALA119 |
| site_id | NR4 |
| Number of Residues | 4 |
| Details | RESIDUES INTERACTING WITH THE RIBOSE OF THE NICOTINAMIDE NUCLEOTIDE OF THE NAD COFACTOR |
| Chain | Residue |
| 4 | THR95 |
| 4 | GLY96 |
| 4 | SER118 |
| 4 | ALA119 |
Functional Information from PROSITE/UniProt
| site_id | PS00071 |
| Number of Residues | 8 |
| Details | GAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL |
| Chain | Residue | Details |
| 1 | ALA146-LEU153 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Nucleophile |
| Chain | Residue | Details |
| 1 | CYS148 | |
| 2 | CYS148 | |
| 3 | CYS148 | |
| 4 | CYS148 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:127793 |
| Chain | Residue | Details |
| 1 | ARG10 | |
| 3 | ASP31 | |
| 3 | SER118 | |
| 3 | ASN312 | |
| 4 | ARG10 | |
| 4 | ASP31 | |
| 4 | SER118 | |
| 4 | ASN312 | |
| 1 | ASP31 | |
| 1 | SER118 | |
| 1 | ASN312 | |
| 2 | ARG10 | |
| 2 | ASP31 | |
| 2 | SER118 | |
| 2 | ASN312 | |
| 3 | ARG10 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| 1 | SER147 | |
| 3 | THR178 | |
| 3 | THR207 | |
| 3 | ARG230 | |
| 4 | SER147 | |
| 4 | THR178 | |
| 4 | THR207 | |
| 4 | ARG230 | |
| 1 | THR178 | |
| 1 | THR207 | |
| 1 | ARG230 | |
| 2 | SER147 | |
| 2 | THR178 | |
| 2 | THR207 | |
| 2 | ARG230 | |
| 3 | SER147 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | SITE: Activates thiol group during catalysis |
| Chain | Residue | Details |
| 1 | HIS175 | |
| 2 | HIS175 | |
| 3 | HIS175 | |
| 4 | HIS175 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | MOD_RES: N-acetylserine => ECO:0000269|PubMed:4294736 |
| Chain | Residue | Details |
| 1 | SER1 | |
| 2 | SER1 | |
| 3 | SER1 | |
| 4 | SER1 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1szj |
| Chain | Residue | Details |
| 1 | HIS175 | |
| 1 | CYS148 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1szj |
| Chain | Residue | Details |
| 2 | HIS175 | |
| 2 | CYS148 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1szj |
| Chain | Residue | Details |
| 3 | HIS175 | |
| 3 | CYS148 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1szj |
| Chain | Residue | Details |
| 4 | HIS175 | |
| 4 | CYS148 |
