Project name: SH3_Q110G

Status: done

submitted: 2019-03-14 19:07:57, status changed: 2019-03-14 20:56:40
Settings
Chain sequence(s) A: TLFVALYDYEARTEDDLSFHKGEEKFQQILNSSEGDWWEARRSLTTGETGYIPSNYVAPV
Distance of aggregation 10 Å
Dynamic mode No
Mutated residues QA110G
Energy difference between WT (input) and mutated protein (by FoldX) 1.2019 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
1.8513
Average score
-0.8704
Total score value
-49.6136

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 0.7287
86 L A 1.2012
87 F A 1.1705
88 V A 0.5580
89 A A 0.0000
90 L A -0.1100
91 Y A -0.5338
92 D A -2.5196
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 -3.0435
100 D A 0.0000
101 L A 0.0000
102 S A -2.2060
103 F A 0.0000
104 H A -2.6734
105 K A -2.2983
106 G A -1.2321
107 E A -1.1763
108 K A -0.4063
109 F A 0.0000
110 G A 0.2221 mutated: QA110G
111 I A 0.3719
112 L A 0.4549
113 N A -0.7351
114 S A -1.1364
115 S A -1.5776
116 E A -2.5599
117 G A -2.1340
118 D A -2.4444
119 W A -1.1028
120 W A -0.9603
121 E A -1.0194
122 A A 0.0000
123 R A -1.4351
124 S A 0.0000
125 L A 0.4314
126 T A -0.3333
127 T A -0.7576
128 G A -1.2272
129 E A -2.2094
130 T A -1.5841
131 G A -1.4846
132 Y A -0.8500
133 I A 0.0000
134 P A 0.0000
135 S A -0.9168
136 N A -1.1504
137 Y A -0.1366
138 V A 0.0000
139 A A 0.4392
140 P A 0.8629
141 V A 1.8513

 

Laboratory of Theory of Biopolymers 2015