Mutation P61586 at position 6: K → H (K6H)

Overview
Predicted structure (AF):
AF-P61586-F1-model_v4
Uniprot entry:
P61586
Gene:
RHOA
Protein length:
193 residues
Mutation:
K → H
Mutation position:
6
D2Deep Prediction:
0.017
Overall confidence:
0.778
Pred. interpretation:
Benign based on D2Deep prediction
 
Benign
Pathogenic
Scores that are greater than or equal to 0.5 are considered "Pathogenic", while scores that are less than 0.5 are considered "Benign".
Sequence difference
1 2 3 4 5 6 7 8 9 10 11
Original M A A I R K K L V I V
Target M A A I R H K L V I V
Predicted original structure
Differences at amino acid level
Feature Original «K» Target «H»
Name Lysine (Lys) Histidine (His)
Molecular Formula C6H14N2O2 C6H9N3O2
Residue Formula C6H12N2O C6H7N3O
Molecular Weight 146.190 155.160 (+8.970)
Residue Weight 128.180 137.140 (+8.960)
Hydrophobicity index at pH 2 Hydrophilic Hydrophilic
Hydrophobicity index at pH 7 Hydrophilic Neutral
Charge Positive Positive
Solutibility Undetermined 4.190
Structure Image Original Structure Target Structure
Description Lysine (Lys) is in the binding enzymes to coenzymes. It plays an important role in the way that histones function. Specifically, it binds to histone acetyl transferases which alter the transcription of certain genes. Histidine (His) within proteins acts as both a proton acceptor and donor. Due to this property, histidine can combine into enzymes involved in the metabolism of proteins, carbohydrates, and nucleic acids.
Predicted structures comparison

About these 3D Structures: The 3D structure representations of both original and target sequences (trimmed to 400 residues, from 1 to 193) will be modeled using the ESM Metagenomic Atlas tools. ESM Metagenomic Atlas is a web-based tool for protein structure prediction that uses deep learning methods to predict protein folding and structure from protein sequences.

Below the plots, you will find additional details on how to interpret the biophysical results.

Differences at biophysical features

About these plots: These plots have been generated by using Bio2Byte predictors to plot both the original and target sequences.

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Biophysical features
Interpretation of the biophysical features

The predictions reflect 'emerging' properties, so what the sequence is capable of, not necessarily what it will do in a particular context, for example when it adopts a specific fold.

DynaMine Backbone Dynamics
  • > 1.0 Membrane spanning regions
  • 0.80 - 1.0 Rigid conformations
  • 0.69 - 0.80 Context dependent
  • < 0.69 Flexible regions
DynaMine Side Chain Dynamics

Higher values mean more likely rigid. These values are highly dependent on the amino acid type (e.g. Trp is rigid, Asp is flexible).

DynaMine Conformational Propensities
  • Sheet: Beta sheets consist of β-strands connected laterally by hydrogen bonds, forming a pleated sheet.
  • Helix: Alpha helices are right-handed coiled structures stabilized by hydrogen bonds.
  • Coil: Coil regions lack regular secondary structure and are flexible.
  • ppII: Polyproline II, a left-handed helical structure found in proline-rich regions.

Higher values indicate higher propensities for each structural element.

EFoldMine Early Folding Propensity

Values above 0.169 indicate residues likely to start the protein folding process, based on local interactions.

DisoMine Disorder Prediction

Values above 0.50 indicate likely disordered residues.

Agmata Beta-Sheet Aggregation Propensity

Values are divided by 20 from the original. Peaks indicate residues likely involved in beta-sheet aggregation.