Project name: SH3_Q110P

Status: done

submitted: 2019-03-14 19:08:12, status changed: 2019-03-14 20:57:12
Settings
Chain sequence(s) A: TLFVALYDYEARTEDDLSFHKGEEKFQQILNSSEGDWWEARRSLTTGETGYIPSNYVAPV
Distance of aggregation 10 Å
Dynamic mode No
Mutated residues QA110P
Energy difference between WT (input) and mutated protein (by FoldX) 2.15575 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
1.8374
Average score
-0.8825
Total score value
-50.3048

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 0.7083
86 L A 1.1361
87 F A 1.1604
88 V A 0.5607
89 A A 0.0000
90 L A -0.1096
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 -3.0434
100 D A 0.0000
101 L A 0.0000
102 S A -2.2059
103 F A 0.0000
104 H A -2.6729
105 K A -2.2977
106 G A -1.2309
107 E A -1.1573
108 K A -0.4346
109 F A 0.0000
110 P A 0.1681 mutated: QA110P
111 I A 0.3578
112 L A 0.5476
113 N A -0.6576
114 S A -1.1025
115 S A -1.5585
116 E A -2.5599
117 G A -2.1340
118 D A -2.4444
119 W A -1.1028
120 W A -0.9644
121 E A -1.0359
122 A A 0.0000
123 R A -1.7205
124 S A 0.0000
125 L A 0.4282
126 T A -0.3389
127 T A -0.7857
128 G A -1.3004
129 E A -2.3018
130 T A -1.7012
131 G A -1.5436
132 Y A -0.8801
133 I A 0.0000
134 P A 0.0000
135 S A -0.9179
136 N A -1.1504
137 Y A -0.1366
138 V A 0.0000
139 A A 0.4327
140 P A 0.8521
141 V A 1.8374

 

Laboratory of Theory of Biopolymers 2015