. 2021 Jul 29;16(7):e0255098. doi: 10.1371/journal.pone.0255098

Table 2. The amino acid content of SSPs and structural parts of the active site of TaTT, BCAT from E. coli and R-TA from Aspergillus fumigatus.

Parts of the active site:	BCAT from E. coli, (PDB ID: 1IYE)	R-TA from A. fumigatus, (PDB ID: 4CHI)	TaTT (PDB ID: 6GKR)
P-pocket:
SSP	G39	V60	G41
	R40	-	R43
	G256	-	G259
	A259	G276	A262
Structural parts:
αCOOH binding sites	R40 + ²⁵⁶GTAA²⁵⁹		R43 + ²⁵⁹GTHA²⁶²
	Y99 + R97		Y101
β-turn	²⁵⁶GTAA²⁵⁹	²⁷³TTAG²⁷⁶	²⁵⁹GTHA²⁶²
Interdomain loop	¹²⁵PWGAYLGAEALE¹³⁶	¹⁴⁴PYIWVMAPENQL¹⁵⁵	¹³⁰PAVSRLEEDFS¹⁴⁰
O-pocket:
SSP	Y31*	H53*	S34*
	F36	Y58	F39
	R97	-	M103
	-	R126	S115*
	Y164	W183	Y166
Structural parts:
α-COOH binding sites	-	R126*	-
left side/bottom	H27, H30, F36, R97, M107, L109, G161, Tyr164	F51, M52, H53*, Y58, E115, I117, L181, W183	W31, W32, F39, M103, L105, L163, Y166**
O-pocket loop* (from the adjacent subunit)	¹⁰³GDVGMGVNPPAGYS¹¹⁶	¹²¹GLTGVRGSKPEDLYNN¹³⁶	¹¹⁰GNKAFSVVGDR¹²⁰
PLP coordination:
of phenyl group	Y164 F36	W183 Y58	Y166 F39
of N1-atom	E193	E212	E195
of phosphate group	R59 I220 T221 T257	R77 I237 T238 T274	R64 I222 T223 T260

Sites in TaTT sequence chosen for mutagenesis are shown in Bold. Residues from the adjacent subunit of the dimer are marked with an asterisk.