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K705E

Category 3/4 — Most DruggableConflictingLumenal · predictedσ-1 candidateEditorial
LysineGlutamate at position 705 · C-terminal lumenal domain (653-869) · WFS1 (Wolframin)

Lysine → Glutamate at position 705 in wolframin's C-terminal lumenal domain. ClinVar Conflicting classifications including Cataract 41. AlphaMissense 0.975, DynaMut2 ΔΔG -0.17 kcal/mol (mild destabilising). Charge-flip variant at the SAME position as K705N (Atlas card adjacent).

Interactive 3D Structure

Wild-type reference
Wild-type K705 — ionic bond to D801
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DynaMut2 mutant · K705E
Mutant E705 — ionic bond to D801 lost (5 contacts lost)
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Bond changes · DynaMut2 interaction analysis

5 lost2 gained4 preserved
Interaction typeWild-type partnerMutant partnerStatus
Ionic bondD801Lost
Hydrogen bondT778T778Preserved
Hydrogen bondD801Lost
Hydrogen bondQ819Gained
Polar contactR703R703Preserved
Polar contactT778T778Preserved
Polar contactD801Lost
Polar contactQ819Q819Preserved
Van der WaalsD801Lost
Van der WaalsQ819Gained
HydrophobicT778Lost

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
-0.17kcal/mol
Destabilising — mild
AlphaMissense
0.975
LPath
AlphaFold pLDDT
90
model confidence
Schema
Cat 3/4
Category 3/4 — Most Druggable

Clinical Evidence

ClinVar classificationConflicting classifications of pathogenicity
Review statuscriteria provided, conflicting classifications
Associated conditionsCataract 41
InheritanceCataract 41 documented.
Population frequency (gnomAD v4)Absent from gnomAD v4
cDNA changec.2113A>G
ClinVar accessionVCV001685475
Last evaluated2024/02/26 00:00

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

Structural Context

Position 705 same neighbor environment as K705N: TYR706 (2.4 Å), PHE704 (2.5 Å), THR778 (3.6 Å), GLN819 (4.4 Å), ARG703 (4.5 Å).

K705E is the charge-flip variant complementing K705N (charge-neutral) at this position. Where the wild-type K705 made a long-range contact (likely cation-π or salt bridge) with residues across the fold, the variant E705 makes opposite-sign electrostatic contacts. The R703 neighbor at 4.5 Å — previously experiencing K705's same-sign positive charge — now experiences an opposite-sign attractive contact.

The |ΔΔG| of 0.17 is mild — fold accommodates the charge flip easily. AlphaMissense's 0.975 + Cataract 41 clinical evidence confirm severe functional consequence. The mechanism is charge-reversal at the long-range contact position that K705 supplied positive charge to.

Amino-acid chemistry
Lysine (K) → Glutamate (E) — large positively-charged amine replaced by small negatively-charged carboxylate. Complete charge sign reversal.
Position in the protein
C-terminal lumenal domain · position 705 in the ER lumen (pLDDT 90). Same position as K705N.

Druggability Assessment

Category 3/4 — Most Druggable. |ΔΔG| = 0.17 — fold survives. AlphaMissense 0.975 + Cataract 41 confirm severe functional consequence.

Mechanism is charge-flip at K705 disrupting long-range contacts (THR778, GLN819). Therapeutic strategy: same microregion as K705N.

Why this matters

K705E + K705N at the same position with different chemistry — both pathogenic. The K705 position is structurally critical regardless of which residue substitutes.
Therapeutic Strategy Handoff · prediction

Feed this card to Wolfram Intelligence

Download the K705E 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 K705E PDF card ↓Strategies are AI-generated predictions, not validated therapeutics.

UniProt Domain Annotation

Chain1890 · Wolframin
Topological domain653869 · Lumenal