3GNQ
Crystal structure of glyceraldehyde-3-phosphate dehydrogenase, type I from Burkholderia pseudomallei
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 | 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 | 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 | 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 |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0006006 | biological_process | glucose metabolic process |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| E | 0050661 | molecular_function | NADP binding |
| E | 0051287 | molecular_function | NAD binding |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0006006 | biological_process | glucose metabolic process |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| F | 0050661 | molecular_function | NADP binding |
| F | 0051287 | molecular_function | NAD binding |
| G | 0000166 | molecular_function | nucleotide binding |
| G | 0006006 | biological_process | glucose metabolic process |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| G | 0050661 | molecular_function | NADP binding |
| G | 0051287 | molecular_function | NAD binding |
| H | 0000166 | molecular_function | nucleotide binding |
| H | 0006006 | biological_process | glucose metabolic process |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0016620 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor |
| H | 0050661 | molecular_function | NADP binding |
| H | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE NAD B 901 |
| Chain | Residue |
| B | GLY8 |
| B | THR99 |
| B | GLY100 |
| B | PHE101 |
| B | SER122 |
| B | ALA123 |
| B | CYS154 |
| B | ASN185 |
| B | ASN316 |
| B | PHE320 |
| B | HOH348 |
| B | GLY10 |
| B | HOH350 |
| B | HOH360 |
| B | HOH381 |
| B | HOH517 |
| B | HOH530 |
| B | ARG11 |
| B | ILE12 |
| B | ASN35 |
| B | ASP36 |
| B | LEU37 |
| B | ARG80 |
| B | CYS98 |
| site_id | AC2 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NAD C 901 |
| Chain | Residue |
| C | GLY8 |
| C | TYR9 |
| C | GLY10 |
| C | ARG11 |
| C | ILE12 |
| C | ASN35 |
| C | ASP36 |
| C | ARG80 |
| C | CYS98 |
| C | THR99 |
| C | GLY100 |
| C | SER122 |
| C | ALA123 |
| C | CYS154 |
| C | ASN185 |
| C | ASN316 |
| C | PHE320 |
| C | HOH337 |
| C | HOH341 |
| C | HOH343 |
| C | HOH364 |
| C | HOH365 |
| C | HOH369 |
| C | HOH372 |
| C | HOH383 |
| C | HOH384 |
| C | HOH395 |
| D | VAL192 |
| D | TYR193 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE NAD D 901 |
| Chain | Residue |
| C | VAL192 |
| D | GLY10 |
| D | ARG11 |
| D | ILE12 |
| D | ASP36 |
| D | CYS98 |
| D | THR99 |
| D | SER122 |
| D | CYS154 |
| D | ASN185 |
| D | ASN316 |
| D | HOH344 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE NAD E 901 |
| Chain | Residue |
| E | GLY8 |
| E | GLY10 |
| E | ARG11 |
| E | ILE12 |
| E | ASP36 |
| E | CYS98 |
| E | PHE101 |
| E | SER122 |
| E | CYS154 |
| E | ASN185 |
| E | ASN316 |
| E | PHE320 |
| E | HOH352 |
| F | VAL192 |
| site_id | AC5 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE NAD F 901 |
| Chain | Residue |
| F | HOH344 |
| F | HOH349 |
| F | HOH350 |
| F | HOH473 |
| F | GLY8 |
| F | GLY10 |
| F | ARG11 |
| F | ILE12 |
| F | ASN35 |
| F | ASP36 |
| F | LEU37 |
| F | ARG80 |
| F | CYS98 |
| F | THR99 |
| F | GLY100 |
| F | SER122 |
| F | ALA123 |
| F | CYS154 |
| F | ASN185 |
| F | ASN316 |
| F | PHE320 |
| F | HOH338 |
| F | HOH339 |
| F | HOH341 |
| site_id | AC6 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE NAD G 901 |
| Chain | Residue |
| G | ASN7 |
| G | GLY8 |
| G | GLY10 |
| G | ARG11 |
| G | ILE12 |
| G | ASP36 |
| G | ARG80 |
| G | CYS98 |
| G | THR99 |
| G | GLY100 |
| G | SER122 |
| G | ALA123 |
| G | THR184 |
| G | ASN185 |
| G | ASN316 |
| G | HOH343 |
| G | HOH344 |
| G | HOH355 |
| G | HOH487 |
| site_id | AC7 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAD H 901 |
| Chain | Residue |
| G | VAL192 |
| H | GLY8 |
| H | TYR9 |
| H | GLY10 |
| H | ARG11 |
| H | ILE12 |
| H | ASN35 |
| H | ASP36 |
| H | LEU37 |
| H | ARG80 |
| H | CYS98 |
| H | THR99 |
| H | GLY100 |
| H | SER122 |
| H | ALA123 |
| H | CYS154 |
| H | THR184 |
| H | ASN185 |
| H | ASN316 |
| H | PHE320 |
| H | HOH341 |
| H | HOH353 |
| H | HOH355 |
| H | HOH356 |
| H | HOH360 |
| H | HOH380 |
| H | HOH499 |
| H | HOH527 |
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 | ALA152-LEU159 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1szj |
| Chain | Residue | Details |
| A | HIS181 | |
| A | CYS154 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1szj |
| Chain | Residue | Details |
| B | HIS181 | |
| B | CYS154 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1szj |
| Chain | Residue | Details |
| C | HIS181 | |
| C | CYS154 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1szj |
| Chain | Residue | Details |
| D | HIS181 | |
| D | CYS154 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1szj |
| Chain | Residue | Details |
| E | HIS181 | |
| E | CYS154 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1szj |
| Chain | Residue | Details |
| F | HIS181 | |
| F | CYS154 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1szj |
| Chain | Residue | Details |
| G | HIS181 | |
| G | CYS154 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1szj |
| Chain | Residue | Details |
| H | HIS181 | |
| H | CYS154 |
