Structure of PDB 1euy Chain A

Receptor sequence
>1euyA (length=529) Species: 562 (Escherichia coli) [Search protein sequence]
TNFIRQIIDEDLASGKHTTVHTRFPPEPNGYLHIGHAKSICLNFGIAQDY
KGQCNLRFDDTNPVKEDIEYVESIKNDVEWLGFHWSGNVRYSSDYFDQLH
AYAIELINKGLAYVDELTPEQIREYRGTLTQPGKNSPYRDRSVEENLALF
EKMRAGGFEEGKACLRAKIDMASPFIVMRDPVLYRIKFAEHHQTGNKWCI
YPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNITIPVHPRQYE
FSRLNLEYTVMSKRKLNLLVTDKHVEGWDDPRMPTISGLRRRGYTAASIR
EFCKRIGVTKQDNTIEMASLESCIREDLNENAPRAMAVIDPVKLVIENYQ
GEGEMVTMPNHPNKPEMGSRQVPFSGEIWIDRADFREEANKQYKRLVLGK
EVRLRNAYVIKAERVEKDAEGNITTIFCTYDADTLGVIHWVSAAHALPVE
IRLYDRLFSVPNPGAADDFLSVINPESLVIKQGFAEPSLKDAVAGKAFQF
EREGYFCLDSRHSTAEKPVFNRTVGLRDT
3D structure
PDB1euy Influence of transfer RNA tertiary structure on aminoacylation efficiency by glutaminyl and cysteinyl-tRNA synthetases.
ChainA
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E34 R260 K270
Catalytic site (residue number reindexed from 1) E27 R253 K263
Enzyme Commision number 6.1.1.18: glutamine--tRNA ligase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004819 glutamine-tRNA ligase activity
GO:0005524 ATP binding
Biological Process
GO:0006412 translation
GO:0006418 tRNA aminoacylation for protein translation
GO:0006424 glutamyl-tRNA aminoacylation
GO:0006425 glutaminyl-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:1euy, PDBe:1euy, PDBj:1euy
PDBsum1euy
PubMed10860750
UniProtP00962|SYQ_ECOLI Glutamine--tRNA ligase (Gene Name=glnS)

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