Residue | Fabry mutation | Importance in α-Gal A | Residue/side-chain accessible surface (Ǻ2) | Solvent exposure of residue |
---|---|---|---|---|
N34 | K | Disrupts hydrogen bonding | 42.83/18.23 | Buried |
T41 | I | Buried, lines active site | 8.87/2.18 | Buried |
D93 | V | Active site; prevents substrate binding | 2.38/2.38 | Buried |
R112 | S | Misfolding | 19.69/15.48 | Buried |
L166 | G | Active site; prevents substrate binding | 4.19/4.19 | Buried |
G171 | D | Active site; prevents substrate binding | 3.04/0.00 | Buried |
M187 | T | Misfolding | 0.05/0.05 | Buried |
S201 | Y | Active site, prevents substrate binding | 7.71/7.71 | Buried |
F | Active site; prevents substrate binding | |||
D234 | E | Dimer interface; disrupts dimer association | 1.44/0.84 | Buried |
W236 | R | Dimer interface; buries acharge | 20.31/18.66 | Buried |
D264 | Y | Active site; prevents substrate binding | 12.79/11.00 | Buried |
M267 | R | Misfolding; buries charge | 4.87/3.78 | Buried |
V269 | M | Misfolding | 1.76/0.00 | Buried |
G271 | V | Misfolding; phi/psi constraints | 15.13/0.00 | Intermediate |
S | Misfolding; phi/psi constraints | |||
S276 | G | Misfolding; loss of hydrogen bonding | 5.32/3.27 | Buried |
Q283 | P | Misfolding | 0.00/0.00 | Buried |
A285 | P | Misfolding | 0.01/0.01 | Buried |
D | Misfolding, buries charge | |||
M290 | I | Misfolding | 3.29/3.10 | Buried |
P293 | T | Misfolding | 1.71/0.01 | Buried |
Q312 | H | Unknown | 40.14/28.62 | Intermediate |
Q321 | R | Misfolding, disrupts hydrogen bonding | 39.66/33.15 | Intermediate |
G328 | V | Misfolding | 0.83/0.00 | Buried |
E338 | K | Unknown | 5.92/5.42 | Buried |
A348 | P | Misfolding | 7.98/7.45 | Buried |
E358 | A | Misfolding; loss of charge | 33.13/28.70 | Intermediate |
Q386 | P | Misfolding | 12.93/12.93 | Buried |