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Table 4 Residues involved with HETA binding to the three MTAPs

From: Leishmania infantum 5’-Methylthioadenosine Phosphorylase presents relevant structural divergence to constitute a potential drug target

huMTAP

T18

H65

P69

A94

C95

G96

F177

I194

N195

M196

T197

T219

D220

D222

V231

V236

Li MTAP

G16

G17

R60

H61

H65

N68

P69

I92

N93

A94

F181

G199

M200

T201

M221

M243

Tb MTAP

G18

H62

H66

V93

N94

A95

V96

F185

M204

A225

T227

M247

N250

V251

V254

MEME motifs

5

5

2

2

2

2

2

3

3

3

3

3

1

1

1

1

1

1

1

1

1

1

4

4

4

4

  1. The table illustrates interacting residues with HETA at a distance lower than or equal to a cutoff of 4Ǻ. Residues listed in the same column are structurally aligned IRs. Residues were observed that interact in the three MTAPs with both MTA and HETA. Residues specifically involved with HETA binding (vs. MTA) are shown in bold