1.5.3.1	-	392379, 392397	
1.5.3.1	alpha subunit contains NAD+ and putative folate binding site. The FAD binding site is in the beta subunit, FMN is bound at the interface of the alpha and beta subunit. A zinc ion, coordinated by three cysteine and one histidine side-chains, is bound to the delta subunit	675389	
1.5.3.1	complexed with methylthioacetate, pyrrole 2-carboxylate and sulfite, and sarcosine-reduced enzyme. Sarcosine oxidase comprises alpha-, beta-, gamma- and delta-subunits, FAD and FMN cofactors, and a large internal cavity. Methylthioacetate and pyrrole 2-carboxylate are sandwiched between the re-face of the FAD isoalloxazine ring and the beta-subunit C-terminal residues. Reduction of flavin cofactors shifts the beta-subunit A1 residue towards the alpha-subunit M55, forming a surface cavity at the oxygen-channel vestibule and rendering the beta-subunit C-terminal residues mobile. Three channels connect the cavity and the enzyme surface. Two of them exist in the inter-subunit space between alpha- and beta-subunits, and the substrate sarcosine seems to enter the active site through either of these channels and reaches the reside of the FAD isoalloxazine ring by traversing the mobile beta-subunit C-terminal residues. The third channel goes through the alpha-subunit and has a folinic acid-binding site	712321	
1.5.3.1	enzyme in complex with dimethylglycine and folinic acid, vapor diffusion method, using 0.1 M Tris-HCl (pH 8.5), 1.9 M ammonium sulfate, and 10 mM CuSO4	764062	
1.5.3.1	enzyme inhibitor complexes, discussion of active site bindung determinants	392407	
1.5.3.1	in complex with dimethylglycine and folinic acid. The alpha subunit consists of two domains, contains NAD+ and binds folinic acid. The beta subunit contains dimethylglycine, FAD and FMN. The gamma subunit is in contact with two domains of alpha subunit and has possibly a folate-binding structure. The delta subunit contains a single atom of and has a Cys3His zinc finger structure	671702	
1.5.3.1	mutants K265M, K265Q, K265A, K265R, to 1.6-2.1 A resolution. The overall structure of MSOX and residue conformation in the sarcosine binding cavity are unaffected by replacement of K265 with Met or Arg. The side chain of K265M exhibits the same configuration in each molecule of K265M crystals and is nearly congruent with K265 in wild-type MSOX. The side chain of K265R is dramatically shifted compared with K265, points in the opposite direction, and exhibits significant conformational variability between molecules of the same crystal. The major species in solutions of K265R is likely to contain a flipped-out R265 and exhibit negligible oxygen activation, similar to K265M. The 400fold higher oxygen reactivity observed with K265R is attributed to a minor flipped-in R265 conformer whose oxygen reactivity is similar to that of wild-type MSOX. Structural water molecule 1 is strikingly absent in K265M and K265R	711236	
1.5.3.1	R49K mutant after reconstitution with FAD, sitting drop vapor diffusion method, high salt or high PEG conditions	685219	
1.5.3.1	recombinant protein	392396	
1.5.3.1	unliganded enzyme, high flexibility of the active site loop is important for enzyme activity	676764