A
B
H228
E227
K526, A527
E525, P526
P510, V511
A509, K510
Q360
H359
R165, P166
L164, T165
T493
I492
Q533, S532
M532, K531
Supplementary Figure 1. A) Sequence alignment of GalNacT1 and T3. Non identical residues
are presented with black characters in white background. Non conservative substitutions are
indicated with red arrows. The linker region connecting the catalytic and lectin domains is
indicated with a red rectangle. The catalityc diad is shown with red letters. B) Cartoon
representation of the X-ray structure of GalNacT1 (PDB id:1XHB). The catalytic domain is
shown in gray, while the a, b and g regions within the lectin domains are shown in blue, orange
and green, respectively. Amino acids indicated with red arrows in A are shown with sticks. The
identity of the residues in the T1 and T13 isoforms is shown on the top and bottom lines,
respectively. The position of the active site is indicated with a red oval for reference.