EC Number | Cloned (Comment) | Organism |
---|---|---|
1.1.1.263 | expression in Escherichia coli | Sinorhizobium meliloti |
1.1.1.292 | expresssion in Escherichia coli | Sinorhizobium meliloti |
EC Number | Crystallization (Comment) | Organism |
---|---|---|
1.1.1.263 | to 1.93 A resolution. The structure displays an empty substrate-binding site in an open conformation reflecting the enzyme state shortly after the release of product, presumably with bound oxidized cofactor NADP+. Amino-acid residues Lys94, His151, Trp162, Arg163, Asp176 and His180 are involved in substrate binding, catalysis or product release. The side chain of Lys94 seems to function as a molecular switch | Sinorhizobium meliloti |
1.1.1.292 | in complex with NADP(H), to 1.93 A resolution. The structure displays an empty substrate-binding, showing an open conformation of the enzyme state shortly after the release of product, presumably with bound oxidized cofactor NADP+. Amino-acid residues Lys94, His151, Trp162, Arg163, Asp176 and His180 are involved in substrate binding, catalysis or product release. The side chain of Lys94 may function as a molecular switch | Sinorhizobium meliloti |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.1.1.263 | Sinorhizobium meliloti | Q92KZ3 | - |
- |
1.1.1.292 | Sinorhizobium meliloti | Q92KZ3 | - |
- |