Project name: SH3_K108G

Status: done

submitted: 2019-03-14 19:07:19, status changed: 2019-03-14 20:50:22
Settings
Chain sequence(s) A: TLFVALYDYEARTEDDLSFHKGEEKFQQILNSSEGDWWEARRSLTTGETGYIPSNYVAPV
Distance of aggregation 10 Å
Dynamic mode No
Mutated residues KA108G
Energy difference between WT (input) and mutated protein (by FoldX) 3.15199 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
1.9638
Average score
-0.8717
Total score value
-49.6845

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 0.5647
86 L A 1.1062
87 F A 1.2552
88 V A 0.8636
89 A A 0.0000
90 L A -0.0581
91 Y A -0.5658
92 D A -2.5599
93 Y A -1.9315
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 -2.6330
105 K A -2.2932
106 G A -1.2522
107 E A -0.8766
108 G A 0.2171 mutated: KA108G
109 F A 0.0000
110 Q A -0.2755
111 I A 0.0284
112 L A 0.1369
113 N A -0.8907
114 S A -1.1794
115 S A -1.5962
116 E A -2.5599
117 G A -2.1340
118 D A -2.4444
119 W A -1.1028
120 W A -1.0581
121 E A -1.1563
122 A A 0.0000
123 R A -1.5319
124 S A 0.0000
125 L A 0.6052
126 T A -0.1657
127 T A -0.6604
128 G A -1.2681
129 E A -2.1917
130 T A -1.6623
131 G A -1.4992
132 Y A -0.8673
133 I A 0.0000
134 P A 0.0000
135 S A -0.9206
136 N A -1.1504
137 Y A -0.1131
138 V A 0.0000
139 A A 0.5362
140 P A 0.9057
141 V A 1.9638

 

Laboratory of Theory of Biopolymers 2015