3RHH
Crystal structure of NADP-dependent glyceraldehyde-3-phosphate dehydrogenase from Bacillus halodurans C-125 complexed with NADP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0008886 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NADP+) (non-phosphorylating) activity |
| A | 0008911 | molecular_function | lactaldehyde dehydrogenase (NAD+) activity |
| 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 |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0008886 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NADP+) (non-phosphorylating) activity |
| B | 0008911 | molecular_function | lactaldehyde dehydrogenase (NAD+) activity |
| 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 |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0008886 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NADP+) (non-phosphorylating) activity |
| C | 0008911 | molecular_function | lactaldehyde dehydrogenase (NAD+) activity |
| 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 |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0008886 | molecular_function | glyceraldehyde-3-phosphate dehydrogenase (NADP+) (non-phosphorylating) activity |
| D | 0008911 | molecular_function | lactaldehyde dehydrogenase (NAD+) activity |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE NAP A 506 |
| Chain | Residue |
| A | ILE159 |
| A | PHE237 |
| A | GLY240 |
| A | THR243 |
| A | HOH557 |
| A | SER160 |
| A | LYS186 |
| A | PRO187 |
| A | ALA188 |
| A | THR189 |
| A | GLY219 |
| A | GLY223 |
| A | ASP224 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 507 |
| Chain | Residue |
| A | ARG112 |
| A | ARG292 |
| A | GLU445 |
| A | ARG446 |
| A | GLY447 |
| A | HOH556 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE NAP B 506 |
| Chain | Residue |
| B | ILE159 |
| B | SER160 |
| B | PRO161 |
| B | PHE162 |
| B | LYS186 |
| B | PRO187 |
| B | ALA188 |
| B | THR189 |
| B | GLY217 |
| B | GLY219 |
| B | GLY223 |
| B | ASP224 |
| B | PHE237 |
| B | GLY239 |
| B | GLY240 |
| B | THR243 |
| B | HOH512 |
| B | HOH560 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 507 |
| Chain | Residue |
| B | ARG112 |
| B | TYR164 |
| B | ARG446 |
| B | GLY447 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE NAP C 506 |
| Chain | Residue |
| C | ILE159 |
| C | SER160 |
| C | PHE162 |
| C | LYS186 |
| C | PRO187 |
| C | ALA188 |
| C | THR189 |
| C | ARG218 |
| C | GLY219 |
| C | GLY223 |
| C | ASP224 |
| C | PHE237 |
| C | GLY240 |
| C | THR243 |
| C | ARG246 |
| C | HOH532 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 C 507 |
| Chain | Residue |
| C | ARG112 |
| C | TYR164 |
| C | ARG292 |
| C | GLU445 |
| C | ARG446 |
| C | GLY447 |
| site_id | AC7 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE NAP D 506 |
| Chain | Residue |
| D | ILE159 |
| D | SER160 |
| D | PRO161 |
| D | PHE162 |
| D | LYS186 |
| D | PRO187 |
| D | ALA188 |
| D | THR189 |
| D | ARG218 |
| D | GLY219 |
| D | GLY223 |
| D | ASP224 |
| D | PHE237 |
| D | GLY239 |
| D | GLY240 |
| D | THR243 |
| D | ARG246 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 D 507 |
| Chain | Residue |
| D | ARG112 |
| D | TYR164 |
| D | ARG292 |
| D | GLU445 |
| D | ARG446 |
| D | GLY447 |
Functional Information from PROSITE/UniProt
| site_id | PS00070 |
| Number of Residues | 12 |
| Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FsYSGQRCTAIK |
| Chain | Residue | Details |
| A | PHE286-LYS297 |
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGKDP |
| Chain | Residue | Details |
| A | LEU258-PRO265 |
