Table 2.

Summary of Non-Synonymous SNP-Induced Changes in NAT2 Function & Structure

SNP/Amino Acid Change (rs identifier)	Domain	Secondary Structure	Side-Chain Location	Type of Change(s)	Functional Effect(s)	Structural Effect(s)
G191A R64Q (rs1801279)	I	Coil	Core	↑Hydrophobicity ↓H-bond Capacity (+) Charge Lost ↓Size	↓Stability	Loss of Electrostatic Interactions
C190T R64W (rs1805158)	I	Coil	Core	↓Flexibility ↓H-bond Capacity ↑Hydrophobicity ↑Aromaticity	↓Stability	Loss of Electrostatic Interactions
T341C I114T (rs1801280)	II	β-Barrel	Hydrophobic Core	↑H-bond Capacity ↓Hydrophobicity ↑Polarity ↓Size	↑Protein Degradation	Conformational Change
G364A D122N (rs4986996)	II	Active Site Loop	Core	Conservative	↓Protein	Catalytic Triad Disruption
A411T L137F (rs4986997)	II	β-Barrel	6.1% Surface Exposed	↑Aromaticity ↑Size	↓Protein	Conformational Change
A434C Q145P	II	β-Barrel	11.1% Surface Exposed	↓Flexibility H-bond Capacity Lost Polarity Lost	↓Protein	Conformational Change
G499A E167K	II	Coil	Domain II Loop	↓H-bond Capacity ↓Hydrophobicity Different Charge ↑Size	↓Protein	Conformational Change
G590A R197Q (rs1799930)	II	Coil	16.6% Surface Exposed	↑Hydrophobicity ↓H-bond Capacity (+) Charge Lost ↓Size	↓Stability	Loss of Electrostatic Interactions
A803G K268R (rs1208)	III	α-Helix	Surface	Conservative	None Detected	None Expected
A845C K282T	III	Coil	C-Terminal Tail	↓Flexibility ↑ Hydrophobicity (+) Charge Lost ↓Size	Slight ↓Stability	Loss of Electrostatic Interactions
G857A G286E (rs1799931)	III	Coil	C-Terminal Tail	↑H-bond Capacity (−) Charge ↓Hydrophobicity ↑Size	↓Protein	Altered Active Site Size/Shape