Structure of PDB 1n78 Chain A

Receptor sequence
>1n78A (length=468) Species: 274 (Thermus thermophilus) [Search protein sequence]
MVVTRIAPSPTGDPHVGTAYIALFNYAWARRNGGRFIVRIEDTDRARYVP
GAEERILAALKWLGLSYDEGPDVGGPHGPYRQSERLPLYQKYAEELLKRG
WAYRAFETPEELEQIRKEKGGYDGRARNIPPEEAEERARRGEPHVIRLKV
PRPGTTEVKDELRGVVVYDNQEIPDVVLLKSDGYPTYHLANVVDDHLMGV
TDVIRAEEWLVSTPIHVLLYRAFGWEAPRFYHMPLLRNPDKTKISKRKSH
TSLDWYKAEGFLPEALRNYLCLMGFSMPDGREIFTLEEFIQAFTWERVSL
GGPVFDLEKLRWMNGKYIREVLSLEEVAERVKPFLREAGLSWESEAYLRR
AVELMRPRFDTLKEFPEKARYLFTEDYPVSEKAQRKLEEGLPLLKELYPR
LRAQEEWTEAALEALLRGFAAEKGVKLGQVAQPLRAALTGSLETPGLFEI
LALLGKERALRRLERALA
3D structure
PDB1n78 ATP binding by glutamyl-tRNA synthetase is switched to the productive mode by tRNA binding
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
Interaction with ligand
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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