Sandbox Reserved 1477: Difference between revisions

Each chain of the enzyme contains a <scene name='80/800656/Fad/1'>FAD cofactor</scene> and the molecules are tightly but non-covalently bonded to the enzyme <ref>PMID: 19374943</ref>. The residues of the active sites, Tyr-73, Phe-418, Trp-430, Arg-516, Asn-518, His-520 and His-563, locate around the cofactor. The cofactors locate at the interface between two chains of the enzyme, covered by an “irregular two-stranded antiparallel-sheet structure formed by residues 75-98”, which prevents the cofactors being released <ref>PMID:10216293</ref>. Generally speaking, the FAD molecules are tightly “covered” or “surrounded” by the enzyme. The binding sites with FAD of both enzymes (GOX’s from Aspergillus niger and Penicillium Amagasakiense) are almost identical with several exceptions of hydrogen-bonds-forming residues His-78 and Thr-110. These two residues are Gln-78 and Ser-100 in the GOX from Penicillium Amagasakiense. Flavin O4’s of the FAD cofactors in both enzymes are connected to the 110th residue (either Thr or Ser) and the Gly-108 residue <ref>PMID:10216293</ref>.

Fig. 2 Relative position of two FAD molecules of the penicillium amagasakiense (PDB code: 1gpe) with transparent surface, which will hopefully give a rough image about how the two chains of the enzyme are arranged. Since the 1cf3 file (GOX from aspergillus niger) only have one chain given, the 1gpe (GOX from penicillium amagasakiense) was used instead.