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. 2013 Jul 15;2013:458571. doi: 10.1155/2013/458571

Table 4.

Rabbit cytosolic SHMT structures compared in this study. The table shows the cofactor form and the ligand present in each subunit of the structures.

Enzyme Chain Form Ligand
Unliganded wild type A i.a. PO4 2−
B i.a. PO4 2−
C i.a. MES
D i.a. MES

Unliganded
T254A
A i.a. PO4 2−
B i.a. PO4 2−
C i.a. PO4 2−
D i.a. PO4 2−

T254A + glycine A g.d. Gly.
B g.d. Gly.
C g.d. Gly.
D g.d. Gly.

T254A + L-serine A g.d. L-Ser.
B g.d. L-Ser.
C g.d. L-Ser.
D g.d. L-Ser.

Unliganded
T254C
A i.a. H2O
B i.a. H2O
C i.a. H2O
D i.a. PO4

T254C + glycine A g.d. Gly.
B g.d. Gly.

T254C + L-serine A g.d. L-Ser.
B g.d. L-Ser.
C g.d. L-Ser.
D g.d. L-Ser.

Wild type + glycine + 5-CHO-H4PteGlu3 A g.d. Gly.
B i.a.
C g.d. Gly.
D i.a.

i.a.: internal aldimine.

g.d.: gem-diamine.

MES: 2-(N-morpholino)ethanesulfonate.

5-CHO-H4PteGlu3: triglutamic form of 5-formyltetrahydrofolate.