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| Title: | | CRYSTAL STRUCTURE OF GLUTAMINYL-TRNA SYNTHETASE COMPLEXED WITH A TRNA-GLN MUTANT AND AN ACTIVE-SITE INHIBITOR | |
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| Molecular Description: |
GLUTAMINYL-TRNA SYNTHETASE (E.C.6.1.1.18)/GLUTAMINYL TRNA COMPLEX |
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| Structural Features: | T SINGLE STRAND |
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| Nucleic Acid Sequence: |
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| Chain | B: | | G G G G U A U C G C C A A G C G G U A A G G C A C C G G A U U C U G A U U C C G G C A G C G A G G U U C G A A U C C U C G U A C C C C A G C C A |
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| Protein Sequence: |
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| Primary Citation: | Sherlin, L.D., Bullock, T.L., Newberry, K.J., Lipman, R.S., Hou, Y.M., Beijer, B., Sproat, B.S., Perona, J.J.
Influence of transfer RNA tertiary structure on aminoacylation efficiency by glutaminyl and cysteinyl-tRNA synthetases.
J.Mol.Biol.
, 299,
pp. 431 - 446, 2000.
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| Experimental Information: | X-RAY DIFFRACTION |
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| Space Group: |
C
2
2
21
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| Cell Constants: |
| a = 230.910 | b = 93.590 | c = 113.110 | (Ångstroms) |
 = 90.00 |  = 90.00 |  = 90.00 | (degrees) |
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| Refinement: | The structure was refined using the X-PLOR 3.851 program.
The R value is
24.2
for 22694 reflections
in the resolution range 30.0 to
3.1 Ångstroms
with Fobs > 0.0 sigma(Fobs).
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