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. Author manuscript; available in PMC: 2013 Jul 1.
Published in final edited form as: Hum Mutat. 2012 Apr 30;33(7):1107–1115. doi: 10.1002/humu.22093

Table 2.

Summary of the structural effects of single-point variations deduced from analysis of static GALT structure

Variant Conservation
score§ 		Impact of
variation on
active site of
the enzyme		 Impact of
variation on
intersubunit
interactions		 Impact of
variation on
secondary
structure of
the variant
residue		 Impact of
variation on
solvent
accessibility
of the variant
residue		 Impact of
variation on
H-bond
network of
the variant
residue		 Impact of
variation on
salt bridge
pattern of
the variant
residue		 Impact of
variation on
overall
stability of
the enzyme
Y34N 0.415 NO YES NO YES YES NO YES
H132Q 0.498 YES* NO NO NO NO NO N.D.
V168L 0.513 NO NO NO NO NO NO N.D.
I170T 0.587 NO NO NO NO YES NO YES
P185H 0.510 YES* NO YES NO YES NO YES
R201C 0.446 NO YES NO NO YES YES YES
E220K 0.457 NO NO NO NO YES YES NO
R223S 0.374 NO NO NO NO NO YES YES
L227P 0.458 NO NO YES NO YES NO YES
R259Q 0.340 NO NO NO NO NO YES YES
I278N 0.338 NO NO NO NO NO NO YES
L289F 0.426 NO NO NO NO NO NO N.D.
E291V 0.479 NO NO NO NO YES NO YES
L327P 0.809 NO NO NO YES YES NO N.D.

Analyses were made on the static modelled structures of each homodimeric variant. “YES” and “NO” indicate if the variation is able to perturb each structural feature represented in columns, or not, following the criteria described previously (Facchiano and Marabotti, 2010). N.D indicates that the effect of the variation on protein stability is not determined because the predictors did not reach a consensus.

§

The higher the value, the most conserved the residue (for further information see http://bioinformatica.isa.cnr.it/GALT).

*

These residues are not included into the active site of the enzyme, but may affect the active site indirectly since they interact with active site residues.