Project name: SH3_K108T

Status: done

submitted: 2019-03-14 19:07:40, status changed: 2019-03-14 20:52:06
Settings
Chain sequence(s) A: TLFVALYDYEARTEDDLSFHKGEEKFQQILNSSEGDWWEARRSLTTGETGYIPSNYVAPV
Distance of aggregation 10 Å
Dynamic mode No
Mutated residues KA108T
Energy difference between WT (input) and mutated protein (by FoldX) 1.26747 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
1.9585
Average score
-0.8818
Total score value
-50.2634

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 0.5587
86 L A 1.0820
87 F A 1.2341
88 V A 0.8304
89 A A 0.0000
90 L A -0.0589
91 Y A -0.5694
92 D A -2.5594
93 Y A -1.9312
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 -2.6294
105 K A -2.2910
106 G A -1.2475
107 E A -0.8993
108 T A 0.2009 mutated: KA108T
109 F A 0.0000
110 Q A -0.2898
111 I A 0.0441
112 L A 0.1430
113 N A -0.8879
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 -1.0557
121 E A -1.1529
122 A A 0.0000
123 R A -1.5660
124 S A 0.0000
125 L A 0.4260
126 T A -0.2506
127 T A -0.7114
128 G A -1.3257
129 E A -2.2234
130 T A -1.6811
131 G A -1.4991
132 Y A -0.8673
133 I A 0.0000
134 P A 0.0000
135 S A -0.9206
136 N A -1.1501
137 Y A -0.1183
138 V A 0.0000
139 A A 0.5293
140 P A 0.9015
141 V A 1.9585

 

Laboratory of Theory of Biopolymers 2015