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G695D

Category 3/4 — Most DruggableLikely pathogenicLumenal · predictedσ-1 candidateEditorial
GlycineAspartate at position 695 · C-terminal lumenal domain (653-869) · WFS1 (Wolframin)

Glycine → Aspartate at position 695 in wolframin's C-terminal lumenal domain. ClinVar Likely pathogenic. AlphaMissense 0.954, DynaMut2 ΔΔG -1.77 kcal/mol (destabilising) — second-largest |ΔΔG| in this batch. A glycine-removal variant with substantial structural cost.

Interactive 3D Structure

Wild-type reference
Wild-type G695 — hydrogen bond to Y660
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DynaMut2 mutant · G695D
Mutant D695 — energy-minimized; 1 new contact formed
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Bond changes · DynaMut2 interaction analysis

0 lost1 gained8 preserved
Interaction typeWild-type partnerMutant partnerStatus
Hydrogen bondV659V659Preserved
Hydrogen bondY660Y660Preserved
Hydrogen bondL829L829Preserved
Polar contactV659V659Preserved
Polar contactY660Y660Preserved
Polar contactL829L829Preserved
Van der WaalsV659V659Preserved
Van der WaalsY660Y660Preserved
Van der WaalsE830Gained

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
-1.77kcal/mol
Destabilising — moderate
AlphaMissense
0.954
LPath
AlphaFold pLDDT
82
model confidence
Schema
Cat 3/4
Category 3/4 — Most Druggable

Clinical Evidence

ClinVar classificationLikely pathogenic
Review statuscriteria provided, single submitter
Associated conditions(no specific conditions catalogued)
InheritanceInheritance not specified.
Population frequency (gnomAD v4)Ultra-rare · AF 0.0021%
cDNA changec.2084G>A
ClinVar accessionVCV002798320
Last evaluated2023/09/10 00:00

Observed at very low frequency in gnomAD.

Structural Context

Position 695 sits in wolframin's C-terminal lumenal domain. The AlphaFold model places G695 within 5 Å of GLU694 (2.5 Å), HIS696 (2.5 Å — same H696 contacted by L829P at 3.9 Å), LEU829 (4.0 Å — partner of L829P!), ILE828 (4.0 Å), and LEU693 (4.5 Å).

The G695-L829 contact at 4.0 Å is structurally significant — G695 sits in spatial contact with the L829P-perturbed microregion (133 sequence positions away). The wild-type glycine at 695 enables the backbone geometry that brings these distant residues into contact.

Replacing glycine with aspartate at 695 introduces both backbone constraint and negative charge. The new D695 carboxylate competes with the existing E694 for local H-bonding. The L829 long-range contact is perturbed.

The |ΔΔG| of 1.77 — the second-largest in this batch and close to the Cat 2 threshold — reflects substantial structural cost. AlphaMissense's 0.954 confirms severe functional consequence.

Amino-acid chemistry
Glycine (G) → Aspartate (D) — smallest amino acid replaced by small negatively-charged carboxylate-bearing residue. Loss of backbone flexibility plus charge introduction.
Position in the protein
C-terminal lumenal domain · position 695 in the ER lumen (pLDDT 82).

Druggability Assessment

Category 3/4 — Most Druggable (near Cat 2 boundary). |ΔΔG| = 1.77 — close to the Cat 2 threshold. AlphaMissense 0.954 confirms severe functional consequence.

Mechanism is glycine-removal at a position with long-range contact to L829 (133 sequence positions apart). Therapeutic strategy: stabilize the G695-L829 long-range geometry.

Why this matters

G695D sits in long-range contact with L829P (Atlas card adjacent). Two Atlas variants 133 sequence positions apart converge on the same therapeutic target region through the folded geometry.
Therapeutic Strategy Handoff · prediction

Feed this card to Wolfram Intelligence

Download the G695D 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 G695D PDF card ↓Strategies are AI-generated predictions, not validated therapeutics.

UniProt Domain Annotation

Chain1890 · Wolframin
Topological domain653869 · Lumenal
Natural variant695695 · in WFS1; dbSNP:rs28937891