EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
3.1.4.17 | Mg2+ | is coordinated to Asp564, two phosphate oxygen atoms, and three water molecules | Homo sapiens | |
3.1.4.17 | Zn2+ | is coordinated to His529, His563, Asp564, Asp674, and two phosphate oxygen atoms | Homo sapiens |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.4.17 | additional information | Homo sapiens | structure analysis of phosphodiesterase 10 binding with cAMP and cGMP by hybrid quantum mechanical/molecular mechanical calculations using cyrstal structures of the substrate-bound enzyme, detailed overview | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.1.4.17 | Homo sapiens | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.4.17 | adenosine 3',5'-cyclic phosphate + H2O | - |
Homo sapiens | adenosine 5'-phosphate | - |
? | |
3.1.4.17 | guanosine 3',5'-cyclic phosphate + H2O | - |
Homo sapiens | guanosine 5'-phosphate | - |
? | |
3.1.4.17 | additional information | structure analysis of phosphodiesterase 10 binding with cAMP and cGMP by hybrid quantum mechanical/molecular mechanical calculations using cyrstal structures of the substrate-bound enzyme, detailed overview | Homo sapiens | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.1.4.17 | PDE10 | - |
Homo sapiens |
3.1.4.17 | phosphodiesterase 10 | - |
Homo sapiens |