Protein translation is a remarkably complex and crucial process of life. Translation speed varies along mRNA to coordinate the co-translational protein folding, and such variations may have drastic effects on the final conformation of the protein encoded. In this paper, we choose HisA protein with TIM beta-alpha barrel fold from two different species to investigate the factors that may be involved in modulating translation process for the fomation of structure symmetry. The association between symmetry in protein structure and several intragenic features is explored, including local codon usage bias along codon sequence, local charge distribution of the encoded protein sequence, local GC content distribution along the nucleotide sequence. Our results show that for HisA proteins from two different species, symmetry in structure is correlated with codon usage bias, charge of the residues and GC content.