4K9D
X-ray crystal structure of a Glyceraldehyde 3-phosphate dehydrogenase from Brugia malayi bound to the co-factor NAD
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006006 | biological_process | glucose metabolic process |
| A | 0006096 | biological_process | glycolytic process |
| A | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| A | 0019682 | biological_process | glyceraldehyde-3-phosphate metabolic process |
| A | 0050661 | molecular_function | NADP binding |
| A | 0051287 | molecular_function | NAD binding |
| B | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006006 | biological_process | glucose metabolic process |
| B | 0006096 | biological_process | glycolytic process |
| B | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| B | 0019682 | biological_process | glyceraldehyde-3-phosphate metabolic process |
| B | 0050661 | molecular_function | NADP binding |
| B | 0051287 | molecular_function | NAD binding |
| C | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0006006 | biological_process | glucose metabolic process |
| C | 0006096 | biological_process | glycolytic process |
| C | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| C | 0019682 | biological_process | glyceraldehyde-3-phosphate metabolic process |
| C | 0050661 | molecular_function | NADP binding |
| C | 0051287 | molecular_function | NAD binding |
| D | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0006006 | biological_process | glucose metabolic process |
| D | 0006096 | biological_process | glycolytic process |
| D | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| D | 0019682 | biological_process | glyceraldehyde-3-phosphate metabolic process |
| D | 0050661 | molecular_function | NADP binding |
| D | 0051287 | molecular_function | NAD binding |
| E | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0005829 | cellular_component | cytosol |
| E | 0006006 | biological_process | glucose metabolic process |
| E | 0006096 | biological_process | glycolytic process |
| E | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| E | 0019682 | biological_process | glyceraldehyde-3-phosphate metabolic process |
| E | 0050661 | molecular_function | NADP binding |
| E | 0051287 | molecular_function | NAD binding |
| F | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0005829 | cellular_component | cytosol |
| F | 0006006 | biological_process | glucose metabolic process |
| F | 0006096 | biological_process | glycolytic process |
| F | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| F | 0019682 | biological_process | glyceraldehyde-3-phosphate metabolic process |
| F | 0050661 | molecular_function | NADP binding |
| F | 0051287 | molecular_function | NAD binding |
| G | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| G | 0005737 | cellular_component | cytoplasm |
| G | 0005829 | cellular_component | cytosol |
| G | 0006006 | biological_process | glucose metabolic process |
| G | 0006096 | biological_process | glycolytic process |
| G | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| G | 0019682 | biological_process | glyceraldehyde-3-phosphate metabolic process |
| G | 0050661 | molecular_function | NADP binding |
| G | 0051287 | molecular_function | NAD binding |
| H | 0004365 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity |
| H | 0005737 | cellular_component | cytoplasm |
| H | 0005829 | cellular_component | cytosol |
| H | 0006006 | biological_process | glucose metabolic process |
| H | 0006096 | biological_process | glycolytic process |
| H | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| H | 0019682 | biological_process | glyceraldehyde-3-phosphate metabolic process |
| H | 0050661 | molecular_function | NADP binding |
| H | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NAD A 401 |
| Chain | Residue |
| A | ASN9 |
| A | PHE37 |
| A | ILE38 |
| A | SER83 |
| A | LYS84 |
| A | SER102 |
| A | THR103 |
| A | GLY104 |
| A | SER126 |
| A | ALA127 |
| A | CYS157 |
| A | GLY10 |
| A | ALA188 |
| A | ASN321 |
| A | TYR325 |
| A | HOH502 |
| A | HOH504 |
| A | HOH510 |
| A | HOH511 |
| A | HOH574 |
| A | HOH586 |
| A | HOH594 |
| A | PHE11 |
| A | HOH628 |
| A | GLY12 |
| A | ARG13 |
| A | ILE14 |
| A | ASN34 |
| A | ASP35 |
| A | PRO36 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 402 |
| Chain | Residue |
| A | PRO133 |
| A | MET134 |
| A | LYS224 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 403 |
| Chain | Residue |
| A | ARG20 |
| A | HIS53 |
| A | GLY293 |
| A | TYR323 |
| site_id | AC4 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE NAD B 401 |
| Chain | Residue |
| B | ASN9 |
| B | GLY10 |
| B | GLY12 |
| B | ARG13 |
| B | ILE14 |
| B | ASP35 |
| B | PRO36 |
| B | PHE37 |
| B | SER83 |
| B | LYS84 |
| B | SER102 |
| B | THR103 |
| B | GLY104 |
| B | SER126 |
| B | ALA127 |
| B | CYS157 |
| B | ALA188 |
| B | ASN321 |
| B | TYR325 |
| B | HOH501 |
| B | HOH502 |
| B | HOH520 |
| B | HOH521 |
| B | HOH522 |
| B | HOH523 |
| B | HOH528 |
| B | HOH550 |
| B | HOH617 |
| B | HOH618 |
| B | HOH626 |
| B | HOH642 |
| B | HOH643 |
| B | HOH660 |
| B | HOH670 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 402 |
| Chain | Residue |
| B | ARG20 |
| B | HIS53 |
| B | GLY293 |
| B | TYR323 |
| site_id | AC6 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAD C 401 |
| Chain | Residue |
| C | HOH573 |
| C | HOH587 |
| C | HOH626 |
| F | HOH617 |
| C | ASN9 |
| C | GLY10 |
| C | GLY12 |
| C | ARG13 |
| C | ILE14 |
| C | ASN34 |
| C | ASP35 |
| C | PRO36 |
| C | PHE37 |
| C | SER83 |
| C | LYS84 |
| C | SER102 |
| C | THR103 |
| C | GLY104 |
| C | PHE106 |
| C | SER126 |
| C | ALA127 |
| C | ALA188 |
| C | ASN321 |
| C | TYR325 |
| C | HOH502 |
| C | HOH521 |
| C | HOH538 |
| C | HOH540 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO C 402 |
| Chain | Residue |
| C | ARG20 |
| C | HIS53 |
| C | TYR323 |
| C | HOH543 |
| site_id | AC8 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAD D 500 |
| Chain | Residue |
| D | ASN9 |
| D | GLY10 |
| D | PHE11 |
| D | GLY12 |
| D | ARG13 |
| D | ILE14 |
| D | ASN34 |
| D | ASP35 |
| D | PRO36 |
| D | PHE37 |
| D | ILE38 |
| D | LYS84 |
| D | SER102 |
| D | THR103 |
| D | GLY104 |
| D | PHE106 |
| D | SER126 |
| D | ALA127 |
| D | ALA188 |
| D | ASN321 |
| D | TYR325 |
| D | HOH601 |
| D | HOH602 |
| D | HOH604 |
| D | HOH605 |
| D | HOH628 |
| D | HOH661 |
| D | HOH668 |
| D | HOH669 |
| D | HOH686 |
| D | HOH687 |
| site_id | AC9 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE NAD E 500 |
| Chain | Residue |
| E | ASN9 |
| E | GLY10 |
| E | GLY12 |
| E | ARG13 |
| E | ILE14 |
| E | ASP35 |
| E | PRO36 |
| E | PHE37 |
| E | LYS84 |
| E | SER102 |
| E | THR103 |
| E | GLY104 |
| E | SER126 |
| E | CYS157 |
| E | ALA188 |
| E | ASN321 |
| E | HOH622 |
| E | HOH642 |
| E | HOH658 |
| H | PRO196 |
| site_id | BC1 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAD F 401 |
| Chain | Residue |
| F | ASN9 |
| F | GLY10 |
| F | GLY12 |
| F | ARG13 |
| F | ILE14 |
| F | ASP35 |
| F | PRO36 |
| F | PHE37 |
| F | SER83 |
| F | LYS84 |
| F | SER102 |
| F | THR103 |
| F | GLY104 |
| F | SER126 |
| F | ALA127 |
| F | ALA188 |
| F | ASN321 |
| F | TYR325 |
| F | HOH519 |
| F | HOH521 |
| F | HOH531 |
| F | HOH532 |
| F | HOH533 |
| F | HOH547 |
| F | HOH612 |
| F | HOH616 |
| F | HOH630 |
| F | HOH642 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO F 402 |
| Chain | Residue |
| F | ARG20 |
| F | HIS53 |
| F | GLY293 |
| site_id | BC3 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NAD G 401 |
| Chain | Residue |
| G | ASN9 |
| G | GLY10 |
| G | PHE11 |
| G | GLY12 |
| G | ARG13 |
| G | ILE14 |
| G | ASN34 |
| G | ASP35 |
| G | PRO36 |
| G | PHE37 |
| G | LYS84 |
| G | SER102 |
| G | THR103 |
| G | GLY104 |
| G | PHE106 |
| G | SER126 |
| G | ALA127 |
| G | ALA188 |
| G | ASN321 |
| G | TYR325 |
| G | HOH522 |
| G | HOH523 |
| G | HOH537 |
| G | HOH562 |
| G | HOH564 |
| G | HOH567 |
| G | HOH611 |
| G | HOH666 |
| G | HOH668 |
| G | HOH670 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO G 402 |
| Chain | Residue |
| G | PRO133 |
| G | MET134 |
| G | LYS224 |
| G | HOH648 |
| site_id | BC5 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE NAD H 500 |
| Chain | Residue |
| E | PRO196 |
| H | ASN9 |
| H | GLY12 |
| H | ARG13 |
| H | ILE14 |
| H | ASP35 |
| H | PRO36 |
| H | PHE37 |
| H | ILE38 |
| H | LYS84 |
| H | SER102 |
| H | GLY104 |
| H | SER126 |
| H | ALA127 |
| H | ALA188 |
| H | ASN321 |
| H | TYR325 |
| H | HOH614 |
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 | ALA155-LEU162 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10009","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 72 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Site: {"description":"Activates thiol group during catalysis","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |






