6NLX
Crystal Structure of Glyceraldehyde-3-phosphate Dehydrogenase from Naegleria fowleri with bound NAD
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 | 0005829 | cellular_component | cytosol |
| 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 | 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 | 0005829 | cellular_component | cytosol |
| 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 | 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 | 0005829 | cellular_component | cytosol |
| 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 | 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 | 0005829 | cellular_component | cytosol |
| 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 | 0050661 | molecular_function | NADP binding |
| D | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 401 |
| Chain | Residue |
| A | PRO126 |
| A | THR127 |
| A | ASN133 |
| A | MET141 |
| A | HOH639 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 402 |
| Chain | Residue |
| A | HOH624 |
| C | EDO1604 |
| C | HOH1898 |
| A | ILE285 |
| A | HOH517 |
| A | HOH548 |
| A | HOH555 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 403 |
| Chain | Residue |
| A | ARG11 |
| A | ILE12 |
| site_id | AC4 |
| Number of Residues | 30 |
| Details | binding site for residue NAD B 401 |
| Chain | Residue |
| B | GLY8 |
| B | GLY10 |
| B | ARG11 |
| B | ILE12 |
| B | ASN32 |
| B | ASP33 |
| B | ILE34 |
| B | MET35 |
| B | ARG78 |
| B | SER96 |
| B | THR97 |
| B | GLY98 |
| B | PHE100 |
| B | SER120 |
| B | ALA121 |
| B | ALA180 |
| B | ASN314 |
| B | TYR318 |
| B | HOH516 |
| B | HOH538 |
| B | HOH547 |
| B | HOH557 |
| B | HOH563 |
| B | HOH564 |
| B | HOH583 |
| B | HOH614 |
| B | HOH618 |
| B | HOH660 |
| B | HOH674 |
| B | HOH685 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 402 |
| Chain | Residue |
| B | PRO126 |
| B | THR127 |
| B | PHE128 |
| B | MET141 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 403 |
| Chain | Residue |
| B | ASP283 |
| B | ASP287 |
| D | TYR47 |
| D | LYS53 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue EDO C 1601 |
| Chain | Residue |
| A | ASP283 |
| A | HOH541 |
| A | HOH557 |
| C | TYR47 |
| C | LYS53 |
| C | HOH1739 |
| site_id | AC8 |
| Number of Residues | 33 |
| Details | binding site for residue NAD C 1602 |
| Chain | Residue |
| C | GLY8 |
| C | GLY10 |
| C | ARG11 |
| C | ILE12 |
| C | ASN32 |
| C | ASP33 |
| C | ILE34 |
| C | MET35 |
| C | ARG78 |
| C | SER96 |
| C | THR97 |
| C | GLY98 |
| C | PHE100 |
| C | SER120 |
| C | ALA121 |
| C | ALA180 |
| C | ASN314 |
| C | TYR318 |
| C | HOH1710 |
| C | HOH1719 |
| C | HOH1727 |
| C | HOH1763 |
| C | HOH1765 |
| C | HOH1780 |
| C | HOH1786 |
| C | HOH1793 |
| C | HOH1814 |
| C | HOH1822 |
| C | HOH1827 |
| C | HOH1851 |
| C | HOH1858 |
| C | HOH1861 |
| C | HOH1895 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue EDO C 1603 |
| Chain | Residue |
| C | PRO126 |
| C | THR127 |
| C | PHE128 |
| C | MET141 |
| C | HOH1735 |
| C | HOH1894 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue EDO C 1604 |
| Chain | Residue |
| A | HOH610 |
| C | ILE285 |
| C | EDO1605 |
| C | HOH1703 |
| A | EDO402 |
| A | HOH548 |
| site_id | AD2 |
| Number of Residues | 2 |
| Details | binding site for residue EDO C 1605 |
| Chain | Residue |
| A | HOH548 |
| C | EDO1604 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue EDO C 1606 |
| Chain | Residue |
| C | GLU91 |
| C | LYS115 |
| C | ARG116 |
| C | GLN333 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue EDO D 1501 |
| Chain | Residue |
| B | HOH510 |
| C | TRP193 |
| D | GLU278 |
| D | LYS296 |
| D | HOH1653 |
| site_id | AD5 |
| Number of Residues | 23 |
| Details | binding site for residue NAD D 1502 |
| Chain | Residue |
| A | PRO188 |
| D | GLY10 |
| D | ARG11 |
| D | ILE12 |
| D | ASP33 |
| D | ILE34 |
| D | MET35 |
| D | ARG78 |
| D | SER96 |
| D | THR97 |
| D | GLY98 |
| D | SER120 |
| D | ALA121 |
| D | CYS149 |
| D | ALA180 |
| D | ASN314 |
| D | HOH1611 |
| D | HOH1616 |
| D | HOH1642 |
| D | HOH1650 |
| D | HOH1669 |
| D | HOH1700 |
| D | HOH1713 |
| site_id | AD6 |
| Number of Residues | 3 |
| Details | binding site for residue EDO D 1503 |
| Chain | Residue |
| D | THR127 |
| D | LEU216 |
| D | HOH1668 |
| site_id | AD7 |
| Number of Residues | 3 |
| Details | binding site for residue EDO D 1504 |
| Chain | Residue |
| D | ASP124 |
| D | THR125 |
| D | PRO126 |
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 | ALA147-LEU154 |
