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G494C

Category 4 — Stable Fold, Function DisruptedUncertain significanceTransmembrane · predictedSource card
GlycineCysteine at position 494 · Lumenal loop 3 · WFS1 (Wolframin)

Interactive 3D Structure

Wild-type reference
Wild-type G494 — hydrogen bond to P492
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DynaMut2 mutant · G494C
Mutant C494 — energy-minimized; local contact network preserved
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Bond changes · DynaMut2 interaction analysis

0 lost0 gained2 preserved
Interaction typeWild-type partnerMutant partnerStatus
Hydrogen bondP492P492Preserved
Polar contactP492P492Preserved

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
-0.37kcal/mol
Destabilising — mild
AlphaMissense
0.371
ambiguous
AlphaFold pLDDT
80
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)Absent from gnomAD v4
cDNA changec.1480G>T
ClinVar accessionVCV002181636
Last evaluated2022/06/07 00:00

Not observed in ~730k individuals — consistent with a rare allele (ACMG PM2_supporting).

Full Variant Card

WFS1 Wolframin — G494C Variant Card

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

Glycine → Cysteine at position 494. Lumenal loop 3. ClinVar Uncertain significance, AlphaMissense 0.371, DynaMut2 ΔΔG -0.37 kcal/mol (destabilising).


Identity

FieldValue
VariantG494C (p.Glycine494Cysteine)
DNA changec.1480G>T
Gene · ProteinWFS1 · Wolframin (890 aa)
UniProtO76024 · WFS1_HUMAN
ClinVar accessionVCV002181636
Amino acid changeGlycine (G) → Cysteine (C)

Structural Context

FieldValue
AlphaFold modelAF-O76024-F1, v6
pLDDT at residue 49479.62 — well-folded
DomainLumenal loop 3
Position contextC-terminal lumenal domain · position 494 projects into the ER lumen
IDR flagNo — pLDDT above 50 threshold

UniProt features at this position:

(none catalogued)

Position 494 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 small/flexible (glycine — backbone flexibility, no sidechain); the mutant is thiol (cysteine — disulfide-capable, free -SH). The chemistry shift implies altered local packing, hydrogen-bonding, and/or electrostatics at this site.


Computational Predictions

AlphaMissense

FieldValue
am_pathogenicity0.3711
am_classambiguous
InterpretationLikely benign (threshold 0.564)

DynaMut2

FieldValue
ΔΔG (kcal/mol)-0.37 (Destabilising)
Job ID178094715226
Result URLhttps://biosig.lab.uq.edu.au/dynamut2/results_prediction/178094715226

Clinical Evidence

FieldValue
ClassificationUncertain significance
Review statuscriteria provided, single submitter
Last evaluated2022/06/07 00:00
InheritanceInheritance pattern not specified in ClinVar entry; WFS1 has both AD and AR presentations.
WFS1 variant landscapeG494C 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|=0.37 negligible. Likely site-specific functional disruption — docking strategy.

Why this card matters. Wolframin's fold survives this substitution (|ΔΔG|=0.37 kcal/mol). The pathogenic signal is real — AlphaMissense places it at 0.371. 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
  • G494C_molstar_viewer.html — interactive 3D viewer (auto-highlights position 494 with ball-and-stick + neighbors within 5Å)
  • G494C_variant_card.md — this card (source of truth)
  • G494C_variant_card.html — styled printable card
  • G494C_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)
  • G494C_wildtype_interactions.pse / G494C_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 G494C 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 G494C PDF card ↓Strategies are AI-generated predictions, not validated therapeutics.