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DeepMind AlphaFold2

G6PD Structure Analysis

Exploring the 3D structure of Glucose-6-Phosphate Dehydrogenase using AI-predicted protein folding to understand disease mechanisms.

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UniProt: P11413

Very High (pLDDT > 90)
High (70-90)
Low (50-70)
Very Low (< 50)
515
Amino Acids
59.3
kDa Mass
92.4
Avg. pLDDT
2
Domains

Protein Domains

G6PD consists of two functional domains essential for enzymatic activity

N-terminal Domain
27-200

Contains the NADP+ binding site (Rossmann fold). This domain is responsible for coenzyme binding and is highly conserved across species.

Key Residues:
Lys-171 Arg-198 His-201 Ser-188
C-terminal Domain
201-515

Contains the substrate binding site and dimerization interface. Critical for G6P recognition and catalytic activity.

Key Residues:
Asp-258 His-263 Val-282 Arg-459

Structural Insights

Dimer Interface

G6PD functions as a homodimer. The interface involves ~2,400 Ų of buried surface area, with key contacts at residues 393-410.

Catalytic Mechanism

The active site positions G6P and NADP+ for hydride transfer. His-263 acts as the catalytic base in the reaction mechanism.

Structural NADP+

A second "structural" NADP+ binding site stabilizes the dimer. Loss of this site causes protein instability in many variants.

Prediction Confidence

AlphaFold's per-residue confidence scores reveal structural reliability

High Confidence Regions

  • Core β-sheet structures (pLDDT > 95)
  • α-helices in both domains (pLDDT > 90)
  • Active site residues (pLDDT > 92)
  • Dimer interface contacts (pLDDT > 88)

Lower Confidence Regions

  • N-terminal signal peptide (1-26)
  • Surface loops (residues 120-135)
  • C-terminal flexible region (500-515)
  • Disordered linker regions

Methods & Resources

Data Sources

AF
AlphaFold Database

AF-P11413-F1 (Human G6PD)

UP
UniProt

P11413 - G6PD_HUMAN

PDB
Protein Data Bank

6E08, 2BHL (experimental structures)