. Author manuscript; available in PMC: 2019 Nov 6.

Published in final edited form as: Structure. 2018 Sep 6;26(11):1499–1512.e5. doi: 10.1016/j.str.2018.07.012

Table 1.

Active-Site Amino Acid Comparison between hDHS and TbDHSc:DHSp

NAD 4-Å Shell	TbDHSc:DHSp
hDHS	Dead Site	Catalytic Site
F54hʺ	L40p’	F49c’
T104h	T98c	T71p
S105h	A99c	S72p
N106h^a	N100c^a	N73p^a
L107h	L101c	L74p
S109h	G103c	S76p
T131h	S161c	T98p
A132h	G162c	A99p
G133h^a	G163c^a	G100p^a
E136h	E166c	E103p
E137h^a	H167c^a	E104p^a
A235h	S323c	A210p
D238h	D326c	D213p
G239h	G327c	G214p
S240h^a	D328c^a	S215p^a
G282h	G371c	G260p
G283h	G372c	A261p
I306h	L395c	V280p
N307h	N396c	T281p
T308h	N397c	T282p
A309h	A398c	G283p
S317h	A406c	S291p
A341h	S430c	G315p
D342h	E431c	D316p
A343h	V432c	A317p
G284h’	G262p	G373c
V285h’	L263p	V374c
H288h’^a	H266p^a	H377c^a
D313h’	D287p	D402c
S315h’	C289p	S404c
D316h’	E290p	D405c
S317h’	S291p	A406c

GC7 4-Å Shell	TbDHSc:DHSp
hDHS	Dead Site	Catalytic Site

N106h	N100c	N73p
R165h	H207c	R132p
I166h	F208c	V133p
G167h	G209c	G134p
V171h	Y213c	V138p
S240h	D328c	S215p
D243h	E331c	D218p
H288h’	H266p	H377c
N292h’	R270p	N381c
L295h’	^a	L384c
G314h’	G288p	G403c
S315h’	C289p	S404c
D316h’	E290p	D405c
E323h’	A297p	E412c
W327h’	N301p	W416c
K329h’^b	L303p^a,^b	K418c^b

Residues from the 4-Å shell around NAD⁺ or GC7 within a heterodimer. Numbering is based on the TbDHSc:DHSp structure reported herein or for hDHS, PDB: 1DHS (NAD⁺), or PDB: 1RQD (GC7/NAD⁺). Residues in bold and underlined vary between TbDHSc:DHSp and hDHS.

Each residue is followed by a letter indicating the subunit: c for DHSc, p for DHSc, h or h’ for hDHS; c’, p’, and hʺ indicate contribution from bottom dimer.

Residues contributing to the nicotinamide flip in the dead site.

The catalytic Lys or changed residue to Leu.