Fig. 1 | Scientific Reports

Fig. 1

From: The role of Gln269Leu mutation on the thermostability and structure of uricase from Aspergillus flavus

Fig. 1Fig. 1

(a) Topology of Aspergillus flavus uricase as a homotetramer (PDB: 1r56) was obtained using UCSF Chimera software. (b) The dimer structure of the UOX enzyme, active site residues (1 and 2), and the S7-S8 loop (260–277) are drawn in red and blue, respectively. (c) The monomer structure of Aspergillus flavus uricase enzyme (Chain A) at residue position 269. Glutamine residue 269 (in red) is in contact with the other indicated residues. By substituting glutamine with leucine at position 269, asparagine 274 contacts leucine 269. The yellow line indicates contact between residues.

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