4QX6
CRYSTAL STRUCTURE OF GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE FROM STREPTOCOCCUS AGALACTIAE NEM316 at 2.46 ANGSTROM RESOLUTION
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0006006 | biological_process | glucose metabolic 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 | 0050661 | molecular_function | NADP binding |
| A | 0051287 | molecular_function | NAD binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0006006 | biological_process | glucose metabolic 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 | 0050661 | molecular_function | NADP binding |
| B | 0051287 | molecular_function | NAD binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0006006 | biological_process | glucose metabolic 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 | 0050661 | molecular_function | NADP binding |
| C | 0051287 | molecular_function | NAD binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0006006 | biological_process | glucose metabolic process |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| D | 0050661 | molecular_function | NADP binding |
| D | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE NAD A 401 |
| Chain | Residue |
| A | GLY9 |
| A | THR97 |
| A | GLY98 |
| A | THR121 |
| A | ALA122 |
| A | CYS152 |
| A | ASN316 |
| A | HOH510 |
| A | HOH516 |
| A | HOH517 |
| A | HOH532 |
| A | GLY11 |
| B | PRO191 |
| A | ARG12 |
| A | ILE13 |
| A | ASP34 |
| A | LEU35 |
| A | GLU77 |
| A | ARG78 |
| A | ALA96 |
| site_id | AC2 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE NAD B 401 |
| Chain | Residue |
| A | PRO191 |
| A | HOH504 |
| B | GLY9 |
| B | GLY11 |
| B | ARG12 |
| B | ILE13 |
| B | ASN33 |
| B | ASP34 |
| B | LEU35 |
| B | GLU77 |
| B | ARG78 |
| B | ALA96 |
| B | THR97 |
| B | GLY98 |
| B | PHE99 |
| B | PHE100 |
| B | THR121 |
| B | ALA122 |
| B | CYS152 |
| B | ASN316 |
| B | TYR320 |
| B | HOH503 |
| B | HOH510 |
| B | HOH523 |
| site_id | AC3 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE NAD C 401 |
| Chain | Residue |
| C | ASN8 |
| C | GLY9 |
| C | GLY11 |
| C | ARG12 |
| C | ILE13 |
| C | ASN33 |
| C | ASP34 |
| C | LEU35 |
| C | GLU77 |
| C | ARG78 |
| C | ALA96 |
| C | THR97 |
| C | GLY98 |
| C | PHE99 |
| C | PHE100 |
| C | THR121 |
| C | ALA122 |
| C | CYS152 |
| C | THR182 |
| C | ASN316 |
| C | TYR320 |
| C | EDO402 |
| C | HOH508 |
| D | PRO191 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO C 402 |
| Chain | Residue |
| C | GLU95 |
| C | THR97 |
| C | GLY98 |
| C | PHE99 |
| C | PHE100 |
| C | ALA101 |
| C | THR121 |
| C | ALA122 |
| C | NAD401 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO C 403 |
| Chain | Residue |
| C | GLN185 |
| C | MET186 |
| C | ILE187 |
| D | MET186 |
| D | ILE187 |
| site_id | AC6 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE NAD D 401 |
| Chain | Residue |
| D | CYS152 |
| D | ASN316 |
| D | TYR320 |
| D | HOH506 |
| D | HOH519 |
| C | PRO191 |
| C | HOH503 |
| D | GLY9 |
| D | GLY11 |
| D | ARG12 |
| D | ILE13 |
| D | ASN33 |
| D | ASP34 |
| D | LEU35 |
| D | GLU77 |
| D | ARG78 |
| D | ALA96 |
| D | THR97 |
| D | GLY98 |
| D | PHE100 |
| D | THR121 |
| D | ALA122 |
Functional Information from PROSITE/UniProt
| site_id | PS00071 |
| Number of Residues | 8 |
| Details | GAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL |
| Chain | Residue | Details |
| A | ALA150-LEU157 |
