Mutation P11912 at position 5: P → R (P5R)

Overview
Predicted structure (AF):
AF-P11912-F1-model_v4
Uniprot entry:
P11912
Gene:
P11912
Protein length:
226 residues
Mutation:
P → R
Mutation position:
5
D2Deep Prediction:
0.000
Overall confidence:
0.838
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
Original M P G G P G V L Q A
Target M P G G R G V L Q A
Predicted original structure
Differences at amino acid level
Feature Original «P» Target «R»
Name Proline (Pro) Arginine (Arg)
Molecular Formula C5H9NO2 C6H14N4O2
Residue Formula C5H7NO C6H12N4O
Molecular Weight 115.130 174.200 (+59.070)
Residue Weight 97.120 156.190 (+59.070)
Hydrophobicity index at pH 2 Hydrophilic Hydrophilic
Hydrophobicity index at pH 7 Undetermined Hydrophilic
Charge Neutral Positive
Solutibility 1.540 71.800
Structure Image Original Structure Target Structure
Description Proline (Pro) is made from glutamic acid. When it is in a protein it causes sharp bends to occur in the peptide chain, altering the protein’s final structure. Arginine (Arg) is produced when proteins are digested within our bodies, and it is converted into nitric oxide (responsible for relaxing blood vessels).
Predicted structures comparison

About these 3D Structures: The 3D structure representations of both original and target sequences (trimmed to 400 residues, from 1 to 205) 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.