1IR8: Im Mutant Of Lysozyme

X-ray structure determination of proteins by using the multiple-wavelength anomalous dispersion method targeting selenomethionine is now widely employed. Isoleucine was examined for the second choice of the substitution of methionine next to leucine. We performed a systematic mutational study of the substitutions of methionine for isoleucine. All mutated lysozymes were less stable than the wild-type by about 1 kcal/mol and it is suggested that this instability was caused by the change in residual hydrophobicity from isoleucine to methionine. The X-ray structures of all mutant lysozymes were very similar to that of the wild-type. In addition, both the accessible surface areas and the conformation of the side chain of methionine in all mutant lysozymes were similar to those of the side chain at the respective isoleucine in the wild-type. Therefore, it is suggested that the mutation from isoleucine to methionine in a protein can be considered as a "safe" substitution.
PDB ID: 1IR8Download
MMDB ID: 17218
PDB Deposition Date: 2001/9/19
Updated in MMDB: 2017/10
Experimental Method:
x-ray diffraction
Resolution: 1.63  Å
Source Organism:
Similar Structures:
Biological Unit for 1IR8: monomeric; determined by author
Molecular Components in 1IR8
Label Count Molecule
Protein (1 molecule)
Lysozyme(Gene symbol: LYZ)
Molecule annotation
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Citing MMDB