3STH
Crystal structure of glyceraldehyde-3-phosphate dehydrogenase from Toxoplasma gondii
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 | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 501 |
| Chain | Residue |
| A | ALA21 |
| A | MET22 |
| A | ARG24 |
| A | VAL27 |
| A | HOH402 |
| A | HOH434 |
| site_id | AC2 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE NAD A 380 |
| Chain | Residue |
| A | GLY11 |
| A | ARG12 |
| A | ILE13 |
| A | ASN33 |
| A | ASP34 |
| A | PRO35 |
| A | PHE36 |
| A | MET37 |
| A | GLU78 |
| A | LYS79 |
| A | SER97 |
| A | THR98 |
| A | GLY99 |
| A | SER121 |
| A | ALA122 |
| A | ALA183 |
| A | ASN319 |
| A | TYR323 |
| A | HOH350 |
| A | HOH354 |
| A | HOH382 |
| A | HOH411 |
| A | HOH438 |
| A | HOH456 |
| A | HOH506 |
| A | HOH536 |
| B | HOH389 |
| A | ASN8 |
| A | GLY9 |
| A | PHE10 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 701 |
| Chain | Residue |
| A | PRO129 |
| A | MET130 |
| A | ASN136 |
| A | LYS221 |
| A | HOH533 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 702 |
| Chain | Residue |
| A | ASP49 |
| A | SER50 |
| A | VAL51 |
| A | GLY53 |
| A | HOH447 |
| C | HOH430 |
| C | HOH436 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 703 |
| Chain | Residue |
| A | ARG199 |
| A | PRO210 |
| A | ALA211 |
| A | SER212 |
| D | GLU283 |
| D | ASN301 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA B 501 |
| Chain | Residue |
| B | ALA21 |
| B | ARG24 |
| B | VAL27 |
| B | HOH421 |
| B | HOH615 |
| site_id | AC7 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAD B 380 |
| Chain | Residue |
| B | ASN8 |
| B | GLY9 |
| B | PHE10 |
| B | GLY11 |
| B | ARG12 |
| B | ILE13 |
| B | ASN33 |
| B | ASP34 |
| B | PRO35 |
| B | PHE36 |
| B | MET37 |
| B | GLU78 |
| B | LYS79 |
| B | SER97 |
| B | THR98 |
| B | GLY99 |
| B | SER121 |
| B | ALA122 |
| B | CYS152 |
| B | ALA183 |
| B | ASN319 |
| B | TYR323 |
| B | HOH355 |
| B | HOH356 |
| B | HOH361 |
| B | HOH362 |
| B | HOH379 |
| B | HOH398 |
| B | HOH428 |
| B | HOH442 |
| B | HOH643 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 701 |
| Chain | Residue |
| B | PRO129 |
| B | MET130 |
| B | LYS221 |
| B | HOH509 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO B 702 |
| Chain | Residue |
| B | HOH464 |
| D | SER287 |
| D | HOH440 |
| D | HOH464 |
| B | ASP49 |
| B | SER50 |
| B | VAL51 |
| B | HIS52 |
| B | GLY53 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 703 |
| Chain | Residue |
| B | ARG199 |
| B | HOH563 |
| C | GLU283 |
| C | ASN301 |
| C | HOH440 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA C 501 |
| Chain | Residue |
| C | ALA21 |
| C | MET22 |
| C | ARG24 |
| C | VAL27 |
| C | HOH429 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO C 703 |
| Chain | Residue |
| B | GLU283 |
| B | ASN301 |
| C | ARG199 |
| C | SER212 |
| C | HOH432 |
| site_id | BC4 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAD C 380 |
| Chain | Residue |
| C | ASN8 |
| C | GLY9 |
| C | GLY11 |
| C | ARG12 |
| C | ILE13 |
| C | ASP34 |
| C | PRO35 |
| C | PHE36 |
| C | MET37 |
| C | GLU78 |
| C | LYS79 |
| C | SER97 |
| C | THR98 |
| C | GLY99 |
| C | SER121 |
| C | ALA122 |
| C | CYS152 |
| C | ALA183 |
| C | ASN319 |
| C | HOH350 |
| C | HOH392 |
| C | HOH405 |
| C | HOH410 |
| C | HOH427 |
| C | HOH437 |
| C | HOH514 |
| C | HOH527 |
| C | HOH636 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO C 701 |
| Chain | Residue |
| C | PRO129 |
| C | MET130 |
| C | LYS221 |
| C | HOH667 |
| site_id | BC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO C 702 |
| Chain | Residue |
| A | VAL290 |
| A | HOH447 |
| A | HOH485 |
| C | ASP49 |
| C | SER50 |
| C | VAL51 |
| C | GLY53 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO C 704 |
| Chain | Residue |
| C | VAL135 |
| C | ASN136 |
| C | ASN137 |
| C | ASP138 |
| C | PRO272 |
| site_id | BC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA D 501 |
| Chain | Residue |
| D | ALA21 |
| D | MET22 |
| D | ARG24 |
| D | VAL27 |
| D | HOH377 |
| D | HOH544 |
| site_id | BC9 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NAD D 380 |
| Chain | Residue |
| D | ASN8 |
| D | GLY9 |
| D | PHE10 |
| D | GLY11 |
| D | ARG12 |
| D | ILE13 |
| D | ASP34 |
| D | PRO35 |
| D | PHE36 |
| D | MET37 |
| D | GLU78 |
| D | LYS79 |
| D | SER97 |
| D | THR98 |
| D | GLY99 |
| D | SER121 |
| D | ALA122 |
| D | CYS152 |
| D | ALA183 |
| D | ASN319 |
| D | TYR323 |
| D | HOH357 |
| D | HOH371 |
| D | HOH373 |
| D | HOH374 |
| D | HOH376 |
| D | HOH406 |
| D | HOH647 |
| D | HOH671 |
| site_id | CC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO D 701 |
| Chain | Residue |
| D | PRO129 |
| D | MET130 |
| D | LYS221 |
| D | HOH353 |
| site_id | CC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO D 702 |
| Chain | Residue |
| B | VAL290 |
| B | HOH447 |
| B | HOH464 |
| D | ASP49 |
| D | SER50 |
| D | VAL51 |
| D | GLY53 |
| D | HOH464 |
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 |
