1OOE
Structural Genomics of Caenorhabditis elegans : Dihydropteridine reductase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004155 | molecular_function | 6,7-dihydropteridine reductase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0006559 | biological_process | L-phenylalanine catabolic process |
A | 0006729 | biological_process | tetrahydrobiopterin biosynthetic process |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0042558 | biological_process | pteridine-containing compound metabolic process |
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 | 0006559 | biological_process | L-phenylalanine catabolic process |
B | 0006729 | biological_process | tetrahydrobiopterin biosynthetic process |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0042558 | biological_process | pteridine-containing compound metabolic process |
B | 0070402 | molecular_function | NADPH binding |
B | 0070404 | molecular_function | NADH binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE MES A 2001 |
Chain | Residue |
A | SER66 |
A | HIS204 |
A | LYS207 |
A | TRP208 |
A | SER214 |
A | PRO216 |
A | HOH1043 |
A | HOH1516 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE MES B 2002 |
Chain | Residue |
B | HIS204 |
B | LYS207 |
B | TRP208 |
B | SER213 |
B | SER214 |
B | PRO216 |
B | HOH1162 |
B | HOH1522 |
B | HOH1588 |
B | LEU35 |
Functional Information from PROSITE/UniProt
site_id | PS00061 |
Number of Residues | 29 |
Details | ADH_SHORT Short-chain dehydrogenases/reductases family signature. AaaamgptpsMigYGMAKAAVhHLTsSLA |
Chain | Residue | Details |
A | ALA130-ALA158 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1dhr |
Chain | Residue | Details |
A | ASN183 | |
A | TYR143 | |
A | LYS147 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1dhr |
Chain | Residue | Details |
B | ASN183 | |
B | TYR143 | |
B | LYS147 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dhr |
Chain | Residue | Details |
A | MET140 | |
A | LYS147 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dhr |
Chain | Residue | Details |
B | MET140 | |
B | LYS147 |
site_id | CSA5 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dhr |
Chain | Residue | Details |
A | TYR143 | |
A | LYS147 |
site_id | CSA6 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dhr |
Chain | Residue | Details |
B | TYR143 | |
B | LYS147 |