Table 6.
E. coli | T. thermophilus | S. cerevisiae | Region |
---|---|---|---|
R26 | R27 | N117 | Anti-codon binding |
R28 | R29 | R119 | |
L30 | L31 | Q121 | |
L33 | L34 | L125 | |
G31 | - | - | |
F35 | F36 | F127 | |
N84 | N82 | I179 | |
S32 | G33 | T124 | |
D86 | R84 | K180 | |
E93 | E91 | E188 | |
Q46 | Q47 | Q138 | |
- | - | L223 | |
R64 | R64 | N161 | |
R78 | R78 | V175 | |
- | - | P224 | |
V107 | - | V226 | |
T117 | - | N227 | Hinge region |
- | - | L228 | |
- | R115 | - | |
A120 | L126 | T230 | |
R217 | - | R325 | Catalytic domain |
R222 | A229 | T331 | |
D224 | - | R333 | |
R225 | R231 | H334 | |
F229 | F235 | F338 | |
I343 | R343 | - | Insertion domain |
- | - | T424 | Catalytic domain |
- | - | K428 | |
T558 | K552 | - | |
R537 | R531 | R531 | |
R549 | R543 | R544 | |
A560 | G554 | K553 | |
T557 | N551 | D551 | |
A561 | K555 | R554 |
Bold face indicates the set of residues strongly interacting with tRNAAsp. The equivalent residues from other sources, which are not interacting with tRNAAsp are italics"-" indicates gap or no equivalent residues.