EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.17.1.4 | reduced enzyme in complex with oxipurinol at 2.0 A resolution. Electron density is observed between the N2 nitrogen atom of oxipurinol and the molybdenum atom of the molybdopterin cofactor. Oxipurinol forms hydrogen bonds with residues E802, R880, and E1261 | Bos taurus |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
1.17.1.4 | Oxipurinol | crystal structure of reduced enzyme in complex with oxipurinol at 2.0 A resolution. Electron density is observed between the N2 nitrogen atom of oxipurinol and the molybdenum atom of the molybdopterin cofactor. Oxipurinol forms hydrogen bonds with residues E802, R880, and E1261 | Bos taurus |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.17.1.4 | Bos taurus | - |
- |
- |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
1.17.1.4 | milk | - |
Bos taurus | - |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.17.1.4 | molybdopterin | in the crystal structure of reduced enzyme in complex with oxipurinol at 2.0 A resolution, electron density is observed between the N2 nitrogen atom of oxipurinol and the molybdenum atom of the molybdopterin cofactor | Bos taurus |