3RHD
Crystal structure of glyceraldehyde-3-phosphate dehydrogenase GapN from Methanocaldococcus jannaschii DSM 2661 complexed with NADP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 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 | 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 | 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 | 21 |
| Details | BINDING SITE FOR RESIDUE NAP A 500 |
| Chain | Residue |
| A | ILE137 |
| A | GLY201 |
| A | GLY205 |
| A | ASP206 |
| A | PHE219 |
| A | SER222 |
| A | VAL225 |
| A | HOH550 |
| A | HOH566 |
| A | HOH576 |
| A | HOH598 |
| A | THR138 |
| A | HOH600 |
| A | HOH602 |
| A | PHE140 |
| A | HIS164 |
| A | PRO165 |
| A | SER166 |
| A | SER167 |
| A | LYS168 |
| A | GLY199 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE NAP B 500 |
| Chain | Residue |
| B | ILE137 |
| B | THR138 |
| B | PHE140 |
| B | HIS164 |
| B | PRO165 |
| B | SER166 |
| B | SER167 |
| B | LYS168 |
| B | GLY199 |
| B | GLY201 |
| B | GLY205 |
| B | ASP206 |
| B | PHE219 |
| B | SER222 |
| B | VAL225 |
| B | HOH562 |
| B | HOH586 |
| B | HOH660 |
| B | HOH813 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE NAP C 500 |
| Chain | Residue |
| C | ILE137 |
| C | THR138 |
| C | PHE140 |
| C | HIS164 |
| C | SER166 |
| C | SER167 |
| C | LYS168 |
| C | GLY199 |
| C | GLY201 |
| C | GLY205 |
| C | ASP206 |
| C | PHE219 |
| C | SER222 |
| C | VAL225 |
| C | HOH537 |
| C | HOH588 |
| C | HOH753 |
| site_id | AC4 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE NAP D 500 |
| Chain | Residue |
| D | ILE137 |
| D | THR138 |
| D | PHE140 |
| D | HIS164 |
| D | PRO165 |
| D | SER166 |
| D | SER167 |
| D | LYS168 |
| D | GLY199 |
| D | GLY201 |
| D | GLU202 |
| D | GLY205 |
| D | ASP206 |
| D | PHE219 |
| D | SER222 |
| D | VAL225 |
| D | HOH530 |
| D | HOH537 |
| D | HOH544 |
| D | HOH553 |
| D | HOH794 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Active site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
