Project name: SH3_G106D

Status: done

submitted: 2019-03-14 19:05:50, status changed: 2019-03-14 20:35:52
Settings
Chain sequence(s) A: TLFVALYDYEARTEDDLSFHKGEEKFQQILNSSEGDWWEARRSLTTGETGYIPSNYVAPV
Distance of aggregation 10 Å
Dynamic mode No
Mutated residues GA106D
Energy difference between WT (input) and mutated protein (by FoldX) 3.3704 kcal/mol

CAUTION: Your mutation/s can destabilize the protein structure

Changes in protein stability upon mutation are calculated using the FoldX forcefield. Computational prediction of protein stability is used with the intention of preventing the experimental characterization of proteins bearing mutations that significantly destabilize their structure. Mutations resulting in a predicted reduction in protein stability ≥ 1 kcal/mol are considered disruptive.

Show buried residues

Minimal score value
-3.1028
Maximal score value
1.6494
Average score
-1.0231
Total score value
-58.3187

The table below lists A3D score for protein residues. Residues with A3D score > 0.0000 are marked by yellow rows.

residue index residue name chain Aggrescan3D score mutation
residue index residue name chain Aggrescan3D score
mutation
85 T A 0.5118
86 L A 0.7834
87 F A 0.7409
88 V A 0.0495
89 A A 0.0000
90 L A -0.3587
91 Y A -0.6599
92 D A -2.6043
93 Y A -1.8617
94 E A -2.6452
95 A A -2.6259
96 R A -2.9852
97 T A -2.6608
98 E A -3.1028
99 D A -3.0434
100 D A 0.0000
101 L A 0.0000
102 S A -2.2059
103 F A 0.0000
104 H A -2.8867
105 K A -2.6619
106 D A -2.5969 mutated: GA106D
107 E A -1.8328
108 K A -0.9398
109 F A 0.0000
110 Q A -0.5132
111 I A -0.0560
112 L A 0.1429
113 N A -0.8877
114 S A -1.1790
115 S A -1.5957
116 E A -2.5591
117 G A -2.1323
118 D A -2.4437
119 W A -1.1023
120 W A -1.0554
121 E A -1.1528
122 A A 0.0000
123 R A -1.7128
124 S A 0.0000
125 L A 0.0619
126 T A -0.6049
127 T A -0.8180
128 G A -1.3554
129 E A -2.2392
130 T A -1.6920
131 G A -1.4992
132 Y A -0.8674
133 I A 0.0000
134 P A 0.0000
135 S A -0.9205
136 N A -1.1505
137 Y A -0.0789
138 V A 0.0000
139 A A 0.2670
140 P A 0.7624
141 V A 1.6494

 

Laboratory of Theory of Biopolymers 2015