Project name: SH3_G106Y

Status: done

submitted: 2019-03-14 19:06:24, status changed: 2019-03-14 20:42:48
Settings
Chain sequence(s) A: TLFVALYDYEARTEDDLSFHKGEEKFQQILNSSEGDWWEARRSLTTGETGYIPSNYVAPV
Distance of aggregation 10 Å
Dynamic mode No
Mutated residues GA106Y
Energy difference between WT (input) and mutated protein (by FoldX) 2.90744 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
1.9539
Average score
-0.7882
Total score value
-44.9254

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 0.5092
86 L A 0.7776
87 F A 1.1020
88 V A 1.0561
89 A A 0.0000
90 L A 0.5522
91 Y A 0.1107
92 D A -1.9741
93 Y A -1.7926
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 -1.8687
105 K A -0.7397
106 Y A 0.6966 mutated: GA106Y
107 E A -0.2142
108 K A -0.0971
109 F A 0.0000
110 Q A -0.5164
111 I A -0.0560
112 L A 0.1429
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 -1.1530
122 A A 0.0000
123 R A -1.7128
124 S A 0.0000
125 L A 0.0592
126 T A -0.2837
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 -0.8673
133 I A 0.0000
134 P A 0.0000
135 S A -0.9206
136 N A -1.1508
137 Y A -0.0299
138 V A 0.0000
139 A A 0.5685
140 P A 0.7559
141 V A 1.9539

 

Laboratory of Theory of Biopolymers 2015