7YJJ
Human Cytosolic 10-formyltetrahydrofolate dehydrogenase and Gossypol complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 |
| 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 |
Functional Information from PROSITE/UniProt
| site_id | PS00070 |
| Number of Residues | 12 |
| Details | ALDEHYDE_DEHYDR_CYS Aldehyde dehydrogenases cysteine active site. FfNKGENCIAAG |
| Chain | Residue | Details |
| B | PHE700-GLY711 |
| site_id | PS00687 |
| Number of Residues | 8 |
| Details | ALDEHYDE_DEHYDR_GLU Aldehyde dehydrogenases glutamic acid active site. LELGGKSP |
| Chain | Residue | Details |
| B | LEU672-PRO679 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P28037 |
| Chain | Residue | Details |
| B | GLU673 | |
| C | GLU673 | |
| D | GLU673 | |
| E | GLU673 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:P28037 |
| Chain | Residue | Details |
| B | CYS707 | |
| C | CYS707 | |
| D | CYS707 | |
| E | CYS707 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 28 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P28037 |
| Chain | Residue | Details |
| B | ILE571 | |
| C | GLY630 | |
| C | GLY650 | |
| C | GLU673 | |
| C | LYS757 | |
| C | GLU804 | |
| D | ILE571 | |
| D | LYS597 | |
| D | GLY630 | |
| D | GLY650 | |
| D | GLU673 | |
| B | LYS597 | |
| D | LYS757 | |
| D | GLU804 | |
| E | ILE571 | |
| E | LYS597 | |
| E | GLY630 | |
| E | GLY650 | |
| E | GLU673 | |
| E | LYS757 | |
| E | GLU804 | |
| B | GLY630 | |
| B | GLY650 | |
| B | GLU673 | |
| B | LYS757 | |
| B | GLU804 | |
| C | ILE571 | |
| C | LYS597 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
| Chain | Residue | Details |
| B | SER629 | |
| E | SER629 | |
| E | SER631 | |
| E | SER825 | |
| B | SER631 | |
| B | SER825 | |
| C | SER629 | |
| C | SER631 | |
| C | SER825 | |
| D | SER629 | |
| D | SER631 | |
| D | SER825 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q8K009 |
| Chain | Residue | Details |
| B | LYS660 | |
| C | LYS660 | |
| D | LYS660 | |
| E | LYS660 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q8R0Y6 |
| Chain | Residue | Details |
| B | LYS767 | |
| C | LYS767 | |
| D | LYS767 | |
| E | LYS767 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q3SY69 |
| Chain | Residue | Details |
| B | LYS882 | |
| C | LYS882 | |
| D | LYS882 | |
| E | LYS882 |
