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1jh3

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1jh3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JH3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JH3 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1jh3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JH3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JH3 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ts1|2ts1]]</td></tr>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ts1|2ts1]]</td></tr>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tyrS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1422 Geobacillus stearothermophilus])</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tyrS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1422 Geobacillus stearothermophilus])</td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tyrosine--tRNA_ligase Tyrosine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.1 6.1.1.1] </span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tyrosine--tRNA_ligase Tyrosine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.1 6.1.1.1] </span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jh3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jh3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1jh3 RCSB], [http://www.ebi.ac.uk/pdbsum/1jh3 PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jh3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jh3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1jh3 RCSB], [http://www.ebi.ac.uk/pdbsum/1jh3 PDBsum]</span></td></tr>
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<table>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/SYY_BACST SYY_BACST]] Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).[HAMAP-Rule:MF_02006]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Geobacillus stearothermophilus]]
[[Category: Geobacillus stearothermophilus]]
[[Category: Tyrosine--tRNA ligase]]
[[Category: Tyrosine--tRNA ligase]]
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[[Category: Bedouelle, H.]]
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[[Category: Bedouelle, H]]
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[[Category: Delepierre, M.]]
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[[Category: Delepierre, M]]
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[[Category: Gilquin, B.]]
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[[Category: Gilquin, B]]
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[[Category: Guez, V.]]
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[[Category: Guez, V]]
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[[Category: Guijarro, J I.]]
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[[Category: Guijarro, J I]]
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[[Category: Pintar, A.]]
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[[Category: Pintar, A]]
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[[Category: Prochnicka-Chalufour, A.]]
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[[Category: Prochnicka-Chalufour, A]]
[[Category: Aminoacyl-trna synthetase]]
[[Category: Aminoacyl-trna synthetase]]
[[Category: Anticodon-arm binding domain]]
[[Category: Anticodon-arm binding domain]]
[[Category: Ligase]]
[[Category: Ligase]]

Revision as of 19:38, 25 December 2014

Solution structure of tyrosyl-tRNA synthetase C-terminal domain.

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