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D713H

Category 4 — Stable Fold, Function DisruptedUncertain significanceLumenal · predictedσ-1 candidateSource card
Aspartic acidHistidine at position 713 · C-terminal ER-lumenal (calcium binding, calmodulin, chaperone) · WFS1 (Wolframin)

Interactive 3D Structure

Wild-type reference
Wild-type D713 — ionic bond to K774
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DynaMut2 mutant · D713H
Mutant H713 — ionic bond to K774 lost (4 contacts lost)
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Bond changes · DynaMut2 interaction analysis

4 lost0 gained2 preserved
Interaction typeWild-type partnerMutant partnerStatus
Ionic bondK774Lost
Hydrogen bondR772R772Preserved
Hydrogen bondK774Lost
Polar contactR772R772Preserved
Polar contactK774Lost
HydrophobicR772Lost

Lost / gained / preserved interatomic contacts at the variant residue, from the DynaMut2 (Arpeggio) interaction analysis of the wild-type and energy-minimized mutant structures.

Computational Predictions

DynaMut2 ΔΔG
-0.34kcal/mol
Destabilising — mild
AlphaMissense
0.445
ambiguous
AlphaFold pLDDT
85
model confidence
Schema
Cat 4
Category 4 — Stable Fold, Function Disrupted

Clinical Evidence

ClinVar classificationUncertain significance
Review statuscriteria provided, single submitter
Associated conditions
Population frequency (gnomAD v4)Ultra-rare · AF 0.00019%
cDNA changec.2137G>C
ClinVar accessionVCV001398188
Last evaluated2024/09/19 00:00

Observed at very low frequency in gnomAD.

Full Variant Card

WFS1 Wolframin — D713H Variant Card

Molecular Atlas Pilot · RareResearch.AI · Generated by wolfram-variant-card skill

Aspartic acid → Histidine at position 713. C-terminal ER-lumenal (calcium binding. ClinVar Uncertain significance, AlphaMissense 0.445, DynaMut2 ΔΔG -0.34 kcal/mol (destabilising).


Identity

FieldValue
VariantD713H (p.Aspartic acid713Histidine)
DNA changec.2137G>C
Gene · ProteinWFS1 · Wolframin (890 aa)
UniProtO76024 · WFS1_HUMAN
ClinVar accessionVCV001398188
Amino acid changeAspartic acid (D) → Histidine (H)

Structural Context

FieldValue
AlphaFold modelAF-O76024-F1, v6
pLDDT at residue 71385.31 — well-folded
DomainC-terminal ER-lumenal (calcium binding, calmodulin, chaperone)
Position contextC-terminal lumenal domain · position 713 projects into the ER lumen
IDR flagNo — pLDDT above 50 threshold

UniProt features at this position:

(none catalogued)

Position 713 sits in the C-terminal lumenal domain (residues 653–869), wolframin's largest soluble region. This domain projects into the ER lumen and is implicated in calcium handling, ER stress sensing, and protein–protein interactions with ATF6 and Na+/K+ ATPase β1. The wild-type residue is negatively charged (aspartate — carboxylate); the mutant is titratable basic (histidine — imidazole). The chemistry shift implies altered local packing, hydrogen-bonding, and/or electrostatics at this site.


Computational Predictions

AlphaMissense

FieldValue
am_pathogenicity0.4445
am_classambiguous
InterpretationLikely benign (threshold 0.564)

DynaMut2

FieldValue
ΔΔG (kcal/mol)-0.34 (Destabilising)
Job ID178094702947
Result URLhttps://biosig.lab.uq.edu.au/dynamut2/results_prediction/178094702947

Clinical Evidence

FieldValue
ClassificationUncertain significance
Review statuscriteria provided, single submitter
Last evaluated2024/09/19 00:00
InheritanceInheritance pattern not specified in ClinVar entry; WFS1 has both AD and AR presentations.
WFS1 variant landscapeD713H is 1 of ~326 pathogenic-spectrum variants in WFS1 (out of 2,243 catalogued in ClinVar)

(no conditions catalogued)


Research Path Decision Tree

ΔΔG < 2  + binding site affected   →  CATEGORY 3 — docking experiments
ΔΔG 2–4                            →  CATEGORY 2 — pharmacological chaperones
ΔΔG > 4                            →  CATEGORY 1 — gene therapy
pLDDT < 50                         →  CATEGORY 5 — IDR, experimental only
Stable fold + functional site hit  →  CATEGORY 4 — site-specific docking

Final Schema Categorization

Category 4 — Stable Fold, Function Disrupted

<strong>Category 4 — Stable Fold, Function Disrupted</strong><br/><br/>|ΔΔG|=0.34 negligible. Likely site-specific functional disruption — docking strategy.

Why this card matters. Wolframin's fold survives this substitution (|ΔΔG|=0.34 kcal/mol). The pathogenic signal is real — AlphaMissense places it at 0.445. Protein still folds, but a specific local site is broken. Pharmacological chaperones and small-molecule binders are the rational therapeutic vector.


Files in this folder

  • AF-O76024-F1-model_v6.pdb — AlphaFold structure
  • D713H_molstar_viewer.html — interactive 3D viewer (auto-highlights position 713 with ball-and-stick + neighbors within 5Å)
  • D713H_variant_card.md — this card (source of truth)
  • D713H_variant_card.html — styled printable card
  • D713H_dynamut2_summary.html — clean offline DynaMut2 result card
  • dynamut2_result.json — structured result data
  • dynamut2_result_page.html — local snapshot of the Biosig result page (asset URLs absolutized)
  • D713H_wildtype_interactions.pse / D713H_mutant_interactions.pse — PyMOL sessions

Generated by wolfram-variant-card skill · RareResearch.AI Molecular Atlas Every assumption documented. Every score sourced.

Therapeutic Strategy Handoff · prediction

Feed this card to Wolfram Intelligence

Download the D713H PDF below and upload it to Wolfram Intelligence to generate therapeutic-strategy proposals — guanidinium mimetics, sigma-1 agonist docking, NAC thiol-capping. NAC is already on the bench-testing list.

Download D713H PDF card ↓Strategies are AI-generated predictions, not validated therapeutics.