Structure of PDB 1n78 Chain B Binding Site BS01

Receptor Information
>1n78 Chain B (length=468) Species: 274 (Thermus thermophilus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MVVTRIAPSPTGDPHVGTAYIALFNYAWARRNGGRFIVRIEDTDRARYVP
GAEERILAALKWLGLSYDEGPDVGGPHGPYRQSERLPLYQKYAEELLKRG
WAYRAFETPEELEQIRKEKGGYDGRARNIPPEEAEERARRGEPHVIRLKV
PRPGTTEVKDELRGVVVYDNQEIPDVVLLKSDGYPTYHLANVVDDHLMGV
TDVIRAEEWLVSTPIHVLLYRAFGWEAPRFYHMPLLRNPDKTKISKRKSH
TSLDWYKAEGFLPEALRNYLCLMGFSMPDGREIFTLEEFIQAFTWERVSL
GGPVFDLEKLRWMNGKYIREVLSLEEVAERVKPFLREAGLSWESEAYLRR
AVELMRPRFDTLKEFPEKARYLFTEDYPVSEKAQRKLEEGLPLLKELYPR
LRAQEEWTEAALEALLRGFAAEKGVKLGQVAQPLRAALTGSLETPGLFEI
LALLGKERALRRLERALA
Ligand information
>1n78 Chain D (length=75) [Search RNA sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
ggccccaucgucuagcgguuaggacgcggcccucucaaggccgaaacggg
gguucgauucccccuggggucacca
<<<<<<<..<<<<........>>>>.<<<<<.......>>>>>....<<<
<<.......>>>>>>>>>>>>....
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1n78 ATP binding by glutamyl-tRNA synthetase is switched to the productive mode by tRNA binding
Resolution2.1 Å
Binding residue
(original residue number in PDB)		S9 T43 R47 V145 R163 V166 Y168 E172 V177 K180 S181 Y187 E207 E208 W209 L210 R237 K241 T242 K243 G274 E282 L300 P303 V304 E308 K309 W312 R319 P357 R358 R417 L427 Q432 R435 L442 E443 T444 G446 L447 F448
Binding residue
(residue number reindexed from 1)		S9 T43 R47 V145 R163 V166 Y168 E172 V177 K180 S181 Y187 E207 E208 W209 L210 R237 K241 T242 K243 G274 E282 L300 P303 V304 E308 K309 W312 R319 P357 R358 R417 L427 Q432 R435 L442 E443 T444 G446 L447 F448
Binding affinityPDBbind-CN: Ki=3uM
Enzymatic activity
Catalytic site (original residue number in PDB) K246
Catalytic site (residue number reindexed from 1) K246
Enzyme Commision number 6.1.1.17: glutamate--tRNA ligase.
Gene Ontology
Molecular Function
GO:0000049 tRNA binding
GO:0000166 nucleotide binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004818 glutamate-tRNA ligase activity
GO:0005524 ATP binding
GO:0008270 zinc ion binding
Biological Process
GO:0006412 translation
GO:0006418 tRNA aminoacylation for protein translation
GO:0006424 glutamyl-tRNA aminoacylation
GO:0043039 tRNA aminoacylation
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1n78, PDBe:1n78, PDBj:1n78
PDBsum1n78
PubMed12554668
UniProtP27000|SYE_THET8 Glutamate--tRNA ligase (Gene Name=gltX)

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