5JY6
Structures of Streptococcus agalactiae GBS GAPDH in different enzymatic states
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| A | 0006006 | biological_process | glucose metabolic process |
| A | 0006096 | biological_process | glycolytic 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 | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050661 | molecular_function | NADP binding |
| A | 0051287 | molecular_function | NAD binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| B | 0006006 | biological_process | glucose metabolic process |
| B | 0006096 | biological_process | glycolytic 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 | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050661 | molecular_function | NADP binding |
| B | 0051287 | molecular_function | NAD binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| C | 0006006 | biological_process | glucose metabolic process |
| C | 0006096 | biological_process | glycolytic 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 | 0042802 | molecular_function | identical protein binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0050661 | molecular_function | NADP binding |
| C | 0051287 | molecular_function | NAD binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| D | 0006006 | biological_process | glucose metabolic process |
| D | 0006096 | biological_process | glycolytic 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 | 0042802 | molecular_function | identical protein binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0050661 | molecular_function | NADP binding |
| D | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 29 |
| Details | binding site for residue NAD A 401 |
| Chain | Residue |
| A | ASN8 |
| A | THR97 |
| A | GLY98 |
| A | PHE99 |
| A | PHE100 |
| A | THR121 |
| A | ALA122 |
| A | CYS152 |
| A | ASN316 |
| A | TYR320 |
| A | HOH506 |
| A | GLY9 |
| A | HOH546 |
| A | HOH547 |
| A | HOH550 |
| A | HOH552 |
| A | HOH574 |
| A | HOH578 |
| A | HOH593 |
| A | HOH606 |
| C | PRO191 |
| C | HOH512 |
| A | GLY11 |
| A | ARG12 |
| A | ILE13 |
| A | ASP34 |
| A | LEU35 |
| A | ARG78 |
| A | ALA96 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 402 |
| Chain | Residue |
| A | ILE21 |
| A | VAL24 |
| A | VAL27 |
| A | HOH556 |
| A | HOH623 |
| site_id | AC3 |
| Number of Residues | 32 |
| Details | binding site for residue NAD B 401 |
| Chain | Residue |
| B | ASN8 |
| B | GLY9 |
| B | GLY11 |
| B | ARG12 |
| B | ILE13 |
| B | ASP34 |
| B | LEU35 |
| B | ARG78 |
| B | ALA96 |
| B | THR97 |
| B | GLY98 |
| B | PHE99 |
| B | PHE100 |
| B | THR121 |
| B | ALA122 |
| B | CYS152 |
| B | ASN316 |
| B | TYR320 |
| B | HOH526 |
| B | HOH537 |
| B | HOH549 |
| B | HOH553 |
| B | HOH572 |
| B | HOH584 |
| B | HOH591 |
| B | HOH592 |
| B | HOH603 |
| B | HOH612 |
| B | HOH618 |
| B | HOH636 |
| D | PRO191 |
| D | HOH537 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 402 |
| Chain | Residue |
| B | ILE21 |
| B | VAL24 |
| B | VAL27 |
| B | HOH640 |
| site_id | AC5 |
| Number of Residues | 27 |
| Details | binding site for residue NAD C 401 |
| Chain | Residue |
| A | PRO191 |
| A | HOH569 |
| C | ASN8 |
| C | GLY9 |
| C | GLY11 |
| C | ARG12 |
| C | ILE13 |
| C | ASP34 |
| C | LEU35 |
| C | ARG78 |
| C | ALA96 |
| C | THR97 |
| C | GLY98 |
| C | PHE99 |
| C | PHE100 |
| C | THR121 |
| C | ALA122 |
| C | CYS152 |
| C | ASN316 |
| C | TYR320 |
| C | HOH513 |
| C | HOH538 |
| C | HOH556 |
| C | HOH557 |
| C | HOH561 |
| C | HOH564 |
| C | HOH575 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue MG C 402 |
| Chain | Residue |
| C | VAL27 |
| C | HOH579 |
| C | ILE21 |
| C | VAL24 |
| site_id | AC7 |
| Number of Residues | 30 |
| Details | binding site for residue NAD D 401 |
| Chain | Residue |
| B | PRO191 |
| B | HOH532 |
| D | ASN8 |
| D | GLY9 |
| D | GLY11 |
| D | ARG12 |
| D | ILE13 |
| D | ASP34 |
| D | LEU35 |
| D | ARG78 |
| D | ALA96 |
| D | THR97 |
| D | GLY98 |
| D | PHE99 |
| D | PHE100 |
| D | THR121 |
| D | ALA122 |
| D | CYS152 |
| D | ASN316 |
| D | TYR320 |
| D | HOH503 |
| D | HOH559 |
| D | HOH567 |
| D | HOH583 |
| D | HOH589 |
| D | HOH606 |
| D | HOH616 |
| D | HOH620 |
| D | HOH623 |
| D | HOH627 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue MG D 402 |
| Chain | Residue |
| D | ILE21 |
| D | VAL24 |
| D | VAL27 |
| D | HOH648 |
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 |
