EC Number   |
|---|
   1.6.5.5 | - |
| 1.6.5.5 | crystal structures of zeta-crystallin-like quinone oxidoreductase and its complexes with NADPH determined at 2.4 and 2.01 A resolution |
| 1.6.5.5 | crystallographic structure of human zeta-crystallin is reported. Enzyme shows a tetrameric structure |
| 1.6.5.5 | native enzyme and its complex with NADPH at 2.3 A and 2.8 A resolution. QOR forms a homodimer in the crystal by interaction of the betaF-strands in domain II, forming a large beta-sheet that crosses the dimer interface. NADPH is located between the two domains in the QOR-NADPH complex. The disordered segment involved in the coenzyme binding of apo-QOR becomes ordered upon NADPH binding. The segment covers an NADPH-binding cleft and may serve as a lid. The 2'-phosphate group of the adenine of NADPH is surrounded by polar and positively charged residues in QOR, suggesting that QOR binds NADPH more readily than NADH. The putative substrate-binding site of QOR, is largely blocked by nearby residues |
| 1.6.5.5 | structure in the free state at 2.3 A resolution. VAT-1 forms a dimer with the conserved NADPH-binding cleft on each protomer. The structure of VAT-1 in the NADP-bound state at 2.6 A resolution shows that NADP binds the binding cleft to create a putative active site with the nicotine ring |
