5Y37
Crystal structure of GBS GAPDH
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005737 | cellular_component | cytoplasm |
| 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 | 0005737 | cellular_component | cytoplasm |
| 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 | 0005737 | cellular_component | cytoplasm |
| 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 | 0005737 | cellular_component | cytoplasm |
| 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 | 35 |
| Details | binding site for residue NAD A 401 |
| Chain | Residue |
| A | ASN12 |
| A | ALA100 |
| A | THR101 |
| A | GLY102 |
| A | PHE103 |
| A | PHE104 |
| A | THR125 |
| A | ALA126 |
| A | ASN320 |
| A | TYR324 |
| A | SO4402 |
| A | GLY13 |
| A | HOH509 |
| A | HOH534 |
| A | HOH602 |
| A | HOH612 |
| A | HOH629 |
| A | HOH638 |
| A | HOH659 |
| A | HOH664 |
| A | HOH665 |
| A | HOH670 |
| A | GLY15 |
| A | HOH679 |
| A | HOH706 |
| A | HOH707 |
| A | HOH726 |
| D | PRO195 |
| D | HOH569 |
| A | ARG16 |
| A | ILE17 |
| A | ASN37 |
| A | ASP38 |
| A | LEU39 |
| A | ARG82 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | binding site for residue SO4 A 402 |
| Chain | Residue |
| A | THR186 |
| A | ASP188 |
| A | ARG203 |
| A | ARG239 |
| A | NAD401 |
| A | HOH509 |
| A | HOH530 |
| A | HOH548 |
| A | HOH665 |
| A | HOH683 |
| A | HOH699 |
| site_id | AC3 |
| Number of Residues | 36 |
| Details | binding site for residue NAD B 401 |
| Chain | Residue |
| B | ASN12 |
| B | GLY13 |
| B | GLY15 |
| B | ARG16 |
| B | ILE17 |
| B | ASN37 |
| B | ASP38 |
| B | LEU39 |
| B | ARG82 |
| B | ALA100 |
| B | THR101 |
| B | GLY102 |
| B | PHE103 |
| B | PHE104 |
| B | THR125 |
| B | ALA126 |
| B | CYS156 |
| B | ASN320 |
| B | TYR324 |
| B | SO4402 |
| B | HOH510 |
| B | HOH584 |
| B | HOH599 |
| B | HOH613 |
| B | HOH630 |
| B | HOH632 |
| B | HOH642 |
| B | HOH649 |
| B | HOH654 |
| B | HOH655 |
| B | HOH672 |
| B | HOH673 |
| B | HOH702 |
| B | HOH714 |
| C | PRO195 |
| C | HOH559 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 B 402 |
| Chain | Residue |
| B | THR186 |
| B | ASP188 |
| B | ARG203 |
| B | ARG239 |
| B | NAD401 |
| B | HOH510 |
| B | HOH708 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 C 401 |
| Chain | Residue |
| C | ARG24 |
| C | SER291 |
| C | HOH501 |
| C | HOH660 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 C 402 |
| Chain | Residue |
| C | THR186 |
| C | ASP188 |
| C | ARG203 |
| C | ARG239 |
| C | HOH502 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 C 403 |
| Chain | Residue |
| C | THR157 |
| C | THR216 |
| C | ALA218 |
| C | HOH533 |
| C | HOH655 |
| C | SER155 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 C 404 |
| Chain | Residue |
| A | LYS302 |
| C | LYS220 |
| C | GLY235 |
| C | HOH554 |
| C | HOH605 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | binding site for residue SO4 C 405 |
| Chain | Residue |
| B | HOH629 |
| C | GLY15 |
| C | ARG16 |
| C | HOH519 |
| C | HOH569 |
| C | HOH597 |
| C | HOH637 |
| C | HOH662 |
| C | HOH741 |
| C | HOH797 |
| site_id | AD1 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 D 401 |
| Chain | Residue |
| D | THR186 |
| D | ASP188 |
| D | ARG203 |
| D | ARG239 |
| D | HOH586 |
| D | HOH589 |
| D | HOH620 |
| D | HOH764 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 D 402 |
| Chain | Residue |
| D | SER155 |
| D | THR216 |
| D | GLY217 |
| D | ALA218 |
| D | HOH527 |
| D | HOH541 |
| D | HOH642 |
| site_id | AD3 |
| Number of Residues | 9 |
| Details | binding site for residue SO4 D 403 |
| Chain | Residue |
| D | GLY15 |
| D | ARG16 |
| D | HOH517 |
| D | HOH570 |
| D | HOH593 |
| D | HOH597 |
| D | HOH654 |
| D | HOH695 |
| D | HOH741 |
| site_id | AD4 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 D 404 |
| Chain | Residue |
| B | HOH558 |
| D | ASP273 |
| D | ARG330 |
| D | HOH524 |
| D | HOH568 |
| D | HOH572 |
| D | HOH667 |
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 | ALA154-LEU161 |
