Table 2 Interaction distances between active site residues and GMP
From: Crystal structure of Leishmania tarentolae hypoxanthine-guanine phosphoribosyltransferase
GMP Atom | Protein Atom | Residue hHGPRTb | Distance (Å) | Protein Atom | Residue L HGPRTc | Distance (Å) |
|---|---|---|---|---|---|---|
Phosphate | ||||||
O1A(O3P)a | OG1 | Thr138B | 2.7 | OG | Ser130B | 2.6 |
N | Thr138B | 3.1 | N | Ser130B | 2.9 | |
O2A(O1P)a | N | Gly139B | 2.7 | N | Ala131B | 2.9 |
N | Asp137B | 3.0 | N | Asp129B | 2.9 | |
O3A(O2P)a | N | Thr141B | 3.3 | N | Thr133B | 3.0 |
OG1 | Thr141B | 2.9 | OG1 | Thr133B | 2.6 | |
N | Lys140B | 3.8 | N | Ile132B | 3.5 | |
Ribose | ||||||
O3* | OE1 | Glu133B | 2.9 | OE1 | Glu125B | 3.7 |
OD1 | Asp134B | 4.7 | OD1 | Asp126B | 2.8 | |
Purine | ||||||
O6 | NZ | Lys165B | 2.3 | NZ | Lys157B | 2.9 |
N | Val187B | 3.1 | N | Val179B | 2.8 | |
N1 | O | Val187B | 2.8 | O | Val179B | 2.8 |
N2 | O | Val187B | 3.3 | O | Val179B | 3.4 |
O | Asp193B | 3.2 | O | Asp185B | 2.8 | |
OD1 | Asp193B | 5.8 | OD1 | Asp185B | 3.4 | |
N7 | OD2 | Asp137B | 3.6 | OD2 | Asp129B | 4.4 |
NZ | Lys165B | 3.4 | NZ | Lys157B | 2.9 |