3ORF
Crystal Structure of Dihydropteridine Reductase from Dictyostelium discoideum
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004155 | molecular_function | 6,7-dihydropteridine reductase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006729 | biological_process | tetrahydrobiopterin biosynthetic process |
| A | 0006979 | biological_process | response to oxidative stress |
| A | 0042558 | biological_process | pteridine-containing compound metabolic process |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0045335 | cellular_component | phagocytic vesicle |
| A | 0051287 | molecular_function | NAD binding |
| A | 0070402 | molecular_function | NADPH binding |
| A | 0070404 | molecular_function | NADH binding |
| B | 0004155 | molecular_function | 6,7-dihydropteridine reductase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006729 | biological_process | tetrahydrobiopterin biosynthetic process |
| B | 0006979 | biological_process | response to oxidative stress |
| B | 0042558 | biological_process | pteridine-containing compound metabolic process |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0045335 | cellular_component | phagocytic vesicle |
| B | 0051287 | molecular_function | NAD binding |
| B | 0070402 | molecular_function | NADPH binding |
| B | 0070404 | molecular_function | NADH binding |
| C | 0004155 | molecular_function | 6,7-dihydropteridine reductase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006729 | biological_process | tetrahydrobiopterin biosynthetic process |
| C | 0006979 | biological_process | response to oxidative stress |
| C | 0042558 | biological_process | pteridine-containing compound metabolic process |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0045335 | cellular_component | phagocytic vesicle |
| C | 0051287 | molecular_function | NAD binding |
| C | 0070402 | molecular_function | NADPH binding |
| C | 0070404 | molecular_function | NADH binding |
| D | 0004155 | molecular_function | 6,7-dihydropteridine reductase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006729 | biological_process | tetrahydrobiopterin biosynthetic process |
| D | 0006979 | biological_process | response to oxidative stress |
| D | 0042558 | biological_process | pteridine-containing compound metabolic process |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0045335 | cellular_component | phagocytic vesicle |
| D | 0051287 | molecular_function | NAD binding |
| D | 0070402 | molecular_function | NADPH binding |
| D | 0070404 | molecular_function | NADH binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAD A 901 |
| Chain | Residue |
| A | LEU8 |
| A | ALA75 |
| A | GLY76 |
| A | GLY77 |
| A | ASP97 |
| A | MET98 |
| A | ASN99 |
| A | SER102 |
| A | GLY124 |
| A | ALA125 |
| A | TYR138 |
| A | GLY12 |
| A | LYS142 |
| A | PRO170 |
| A | VAL171 |
| A | THR172 |
| A | LEU173 |
| A | THR175 |
| A | ASN178 |
| A | HOH253 |
| A | HOH269 |
| A | ALA13 |
| A | LEU14 |
| A | ASP33 |
| A | PHE34 |
| A | ARG35 |
| A | SER49 |
| A | ALA74 |
| site_id | AC2 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE NAD B 902 |
| Chain | Residue |
| B | GLY12 |
| B | ALA13 |
| B | LEU14 |
| B | ASP33 |
| B | PHE34 |
| B | ARG35 |
| B | SER49 |
| B | ALA74 |
| B | ALA75 |
| B | GLY76 |
| B | GLY77 |
| B | ASP97 |
| B | MET98 |
| B | THR123 |
| B | GLY124 |
| B | TYR138 |
| B | LYS142 |
| B | PRO170 |
| B | LEU173 |
| B | THR175 |
| B | ASN178 |
| B | HOH236 |
| B | HOH239 |
| B | HOH242 |
| site_id | AC3 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NAD C 903 |
| Chain | Residue |
| C | LEU8 |
| C | GLY12 |
| C | ALA13 |
| C | LEU14 |
| C | ASP33 |
| C | PHE34 |
| C | ARG35 |
| C | SER49 |
| C | ALA74 |
| C | ALA75 |
| C | GLY76 |
| C | GLY77 |
| C | ASP97 |
| C | MET98 |
| C | THR123 |
| C | GLY124 |
| C | TYR138 |
| C | LYS142 |
| C | PRO170 |
| C | VAL171 |
| C | THR172 |
| C | LEU173 |
| C | THR175 |
| C | HOH232 |
| C | HOH262 |
| D | SER183 |
| D | ASP184 |
| site_id | AC4 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE NAD D 904 |
| Chain | Residue |
| D | LYS142 |
| D | PRO170 |
| D | THR172 |
| D | LEU173 |
| D | ASN178 |
| D | HOH236 |
| D | HOH255 |
| C | SER183 |
| C | ASP184 |
| D | LEU8 |
| D | GLY12 |
| D | ALA13 |
| D | LEU14 |
| D | ASP33 |
| D | PHE34 |
| D | ARG35 |
| D | SER49 |
| D | ALA74 |
| D | ALA75 |
| D | GLY76 |
| D | GLY77 |
| D | ASP97 |
| D | MET98 |
| D | SER102 |
| D | THR123 |
| D | GLY124 |
| D | TYR138 |
Functional Information from PROSITE/UniProt
| site_id | PS00061 |
| Number of Residues | 29 |
| Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. AsaalnrtsgMiaYGATKAAThHIIkDLA |
| Chain | Residue | Details |
| A | ALA125-ALA153 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10001","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 96 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
