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E680Q

Category 4 — Stable Fold, Function DisruptedLikely pathogenicLumenal · predictedσ-1 candidateEditorial
GlutamateGlutamine at position 680 · C-terminal lumenal domain (653-869) · WFS1 (Wolframin)

Glutamate → Glutamine at position 680 in wolframin's C-terminal lumenal domain. ClinVar Likely pathogenic, optic atrophy. AlphaMissense 0.321 (below threshold) — AM under-call. DynaMut2 ΔΔG +0.12 kcal/mol — essentially neutral. Conservative charge-to-amide swap.

Interactive 3D Structure

Wild-type reference
Wild-type E680 — hydrogen bond to R676
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DynaMut2 mutant · E680Q
Mutant Q680 — energy-minimized; local contact network preserved
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Bond changes · DynaMut2 interaction analysis

0 lost0 gained3 preserved
Interaction typeWild-type partnerMutant partnerStatus
Hydrogen bondR676R676Preserved
Polar contactR676R676Preserved
Van der WaalsR676R676Preserved

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
0.12kcal/mol
Stabilising — mild
AlphaMissense
0.321
LBen
AlphaFold pLDDT
84
model confidence
Schema
Cat 4
Category 4 — Stable Fold, Function Disrupted

Clinical Evidence

ClinVar classificationLikely pathogenic
Review statusno assertion criteria provided
Associated conditionsOptic atrophy
InheritanceOptic atrophy documented.
Population frequency (gnomAD v4)Ultra-rare · AF 0.00034%
cDNA changec.2038G>C
ClinVar accessionVCV003250050
Last evaluated2018/01/01 00:00

Observed at very low frequency in gnomAD.

Structural Context

Position 680 sits in wolframin's C-terminal lumenal domain. The AlphaFold model places E680 within 5 Å of THR681 (2.5 Å), LYS679 (2.5 Å — likely salt-bridge partner), ALA677 (4.0 Å), ARG676 (4.1 Å — second nearby basic), and TRP678 (4.7 Å).

The wild-type glutamate likely forms a salt bridge with K679 and contributes to the local electrostatic surface that includes R676 nearby. Replacing E680 with glutamine eliminates the negative charge while preserving similar volume and H-bonding capacity.

The |ΔΔG| of essentially zero (+0.12) indicates fold accommodates the conservative swap. AlphaMissense's 0.321 is below threshold — AM under-call. ClinVar Pathogenic + optic atrophy confirm clinical relevance.

Amino-acid chemistry
Glutamate (E) → Glutamine (Q) — negatively-charged carboxylate replaced by neutral polar amide. Same side-chain length; charge lost.
Position in the protein
C-terminal lumenal domain · position 680 in the ER lumen (pLDDT 84).

Druggability Assessment

Category 4 — Stable Fold, Function Disrupted (AM under-call). ΔΔG = +0.12 — fold unchanged. AlphaMissense 0.321 below threshold.

Mechanism is loss of E680-K679 salt bridge. Therapeutic strategy: site-directed at the K679 microregion.

Why this matters

E680Q joins the AM-under-call class. Drug discovery for this class requires multi-metric evaluation rather than AM-alone.
Therapeutic Strategy Handoff · prediction

Feed this card to Wolfram Intelligence

Download the E680Q 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 E680Q PDF card ↓Strategies are AI-generated predictions, not validated therapeutics.

UniProt Domain Annotation

Chain1890 · Wolframin
Topological domain653869 · Lumenal
Natural variant680680 · in DFNA6; uncertain significance