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| Title: | | THE ACTIVE SITE OF YEAST ASPARTYL-TRNA SYNTHETASE: STRUCTURAL AND FUNCTIONAL ASPECTS OF THE AMINOACYLATION REACTION | |
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| Molecular Description: |
ASPARTYL TRNA SYNTHETASE (ASPRS) (E.C.6.1.1.12) COMPLEXED WITH TRANSFER RIBONUCLEIC ACID (TRNA ASP) AND ATP |
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| Nucleic Acid Sequence: |
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| Chains | R,S: | | U C C G U G A U A G U U (PSU) A A (H2U) G G (H2U) C A G A A U G G G C G C (PSU) U G U C (1MG) C G U G C C A G A U (5MC) G G G G (5MU) (PSU) C A A U U C C C C G U C G C G G A G C C A |
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| Protein Sequence: |
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| Primary Citation: | Cavarelli, J., Eriani, G., Rees, B., Ruff, M., Boeglin, M., Mitschler, A., Martin, F., Gangloff, J., Thierry, J.C., Moras, D.
The active site of yeast aspartyl-tRNA synthetase: structural and functional aspects of the aminoacylation reaction.
EMBO J.
, 13,
pp. 327 - 337, 1994.
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| Experimental Information: | X-RAY DIFFRACTION |
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| Space Group: |
P
21
21
2
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| Cell Constants: |
| a = 211.270 | b = 145.350 | c = 86.190 | (Ångstroms) |
 = 90.00 |  = 90.00 |  = 90.00 | (degrees) |
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| Refinement: | The structure was refined using the X-PLOR program.
The R value is
20.3
for 42994 reflections
in the resolution range 7. to
3.0 Ångstroms
with Fobs > 3.0 sigma(Fobs).
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