4GO0
Crystal structure of the c707s mutant of c-terminal domain of 10'formyltetrahydrofolate dehydrogenase in complex with NADPH
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 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 | 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 | 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 | 27 |
| Details | BINDING SITE FOR RESIDUE NDP A 1001 |
| Chain | Residue |
| A | VAL570 |
| A | SER629 |
| A | GLY630 |
| A | GLY634 |
| A | GLN635 |
| A | PHE648 |
| A | THR649 |
| A | GLY650 |
| A | SER651 |
| A | VAL654 |
| A | ILE658 |
| A | ILE571 |
| A | GLU673 |
| A | LEU674 |
| A | GLY675 |
| A | SER707 |
| A | GLU804 |
| A | PHE806 |
| A | LEU834 |
| A | PHE872 |
| A | PRO572 |
| A | TRP573 |
| A | ASN574 |
| A | MET579 |
| A | LYS597 |
| A | ALA599 |
| A | GLN600 |
| site_id | AC2 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE NDP B 1001 |
| Chain | Residue |
| B | ILE571 |
| B | TRP573 |
| B | ASN574 |
| B | LYS597 |
| B | GLN600 |
| B | SER629 |
| B | GLY630 |
| B | GLY634 |
| B | GLN635 |
| B | PHE648 |
| B | THR649 |
| B | GLY650 |
| B | SER651 |
| B | VAL654 |
| B | ILE658 |
| B | GLU673 |
| B | LEU674 |
| B | GLY675 |
| B | SER707 |
| B | GLU804 |
| B | PHE806 |
| B | LEU834 |
| B | PHE872 |
| site_id | AC3 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE NDP C 1001 |
| Chain | Residue |
| C | VAL570 |
| C | ILE571 |
| C | PRO572 |
| C | TRP573 |
| C | ASN574 |
| C | LYS597 |
| C | ALA599 |
| C | GLN600 |
| C | GLY630 |
| C | GLY634 |
| C | GLN635 |
| C | PHE648 |
| C | THR649 |
| C | GLY650 |
| C | SER651 |
| C | VAL654 |
| C | HIS657 |
| C | ILE658 |
| C | GLU673 |
| C | LEU674 |
| C | GLY675 |
| C | SER707 |
| C | GLU804 |
| C | PHE806 |
| C | LEU834 |
| C | PHE872 |
| site_id | AC4 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE NDP D 1001 |
| Chain | Residue |
| D | LEU834 |
| D | PHE872 |
| D | VAL570 |
| D | ILE571 |
| D | TRP573 |
| D | ASN574 |
| D | LYS597 |
| D | ALA599 |
| D | GLN600 |
| D | SER629 |
| D | GLY630 |
| D | GLY634 |
| D | GLN635 |
| D | PHE648 |
| D | THR649 |
| D | GLY650 |
| D | SER651 |
| D | VAL654 |
| D | ILE658 |
| D | GLU673 |
| D | LEU674 |
| D | GLY675 |
| D | SER707 |
| D | GLU804 |
| D | PHE806 |
Functional Information from PROSITE/UniProt
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGKSP |
| Chain | Residue | Details |
| A | LEU672-PRO679 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:17302434 |
| Chain | Residue | Details |
| A | GLU673 | |
| B | GLU673 | |
| C | GLU673 | |
| D | GLU673 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:17302434, ECO:0000305|PubMed:21540484, ECO:0007744|PDB:2O2Q, ECO:0007744|PDB:3RHO |
| Chain | Residue | Details |
| A | SER707 | |
| B | SER707 | |
| C | SER707 | |
| D | SER707 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17302434, ECO:0000269|PubMed:21540484, ECO:0007744|PDB:2O2Q, ECO:0007744|PDB:2O2R, ECO:0007744|PDB:3RHJ, ECO:0007744|PDB:3RHL, ECO:0007744|PDB:3RHO, ECO:0007744|PDB:3RHQ, ECO:0007744|PDB:3RHR |
| Chain | Residue | Details |
| A | ILE571 | |
| C | LYS597 | |
| C | GLY630 | |
| C | GLY650 | |
| D | ILE571 | |
| D | LYS597 | |
| D | GLY630 | |
| D | GLY650 | |
| A | LYS597 | |
| A | GLY630 | |
| A | GLY650 | |
| B | ILE571 | |
| B | LYS597 | |
| B | GLY630 | |
| B | GLY650 | |
| C | ILE571 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17302434, ECO:0000269|PubMed:21540484, ECO:0007744|PDB:2O2Q, ECO:0007744|PDB:3RHJ, ECO:0007744|PDB:3RHL, ECO:0007744|PDB:3RHO, ECO:0007744|PDB:3RHQ, ECO:0007744|PDB:3RHR |
| Chain | Residue | Details |
| A | GLU673 | |
| A | GLU804 | |
| B | GLU673 | |
| B | GLU804 | |
| C | GLU673 | |
| C | GLU804 | |
| D | GLU673 | |
| D | GLU804 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21540484, ECO:0007744|PDB:3RHO |
| Chain | Residue | Details |
| A | LYS757 | |
| B | LYS757 | |
| C | LYS757 | |
| D | LYS757 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 12 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O75891 |
| Chain | Residue | Details |
| A | SER629 | |
| D | SER629 | |
| D | SER631 | |
| D | SER825 | |
| A | SER631 | |
| A | SER825 | |
| B | SER629 | |
| B | SER631 | |
| B | SER825 | |
| C | SER629 | |
| C | SER631 | |
| C | SER825 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q8K009 |
| Chain | Residue | Details |
| A | LYS660 | |
| B | LYS660 | |
| C | LYS660 | |
| D | LYS660 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q8R0Y6 |
| Chain | Residue | Details |
| A | LYS767 | |
| B | LYS767 | |
| C | LYS767 | |
| D | LYS767 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q3SY69 |
| Chain | Residue | Details |
| A | LYS882 | |
| B | LYS882 | |
| C | LYS882 | |
| D | LYS882 |
Catalytic Information from CSA
