Structure of PDB 1euq Chain A Binding Site BS01

Receptor Information
>1euq Chain A (length=529) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TNFIRQIIDEDLASGKHTTVHTRFPPEPNGYLHIGHAKSICLNFGIAQDY
KGQCNLRFDDTNPVKEDIEYVESIKNDVEWLGFHWSGNVRYSSDYFDQLH
AYAIELINKGLAYVDELTPEQIREYRGTLTQPGKNSPYRDRSVEENLALF
EKMRAGGFEEGKACLRAKIDMASPFIVMRDPVLYRIKFAEHHQTGNKWCI
YPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNITIPVHPRQYE
FSRLNLEYTVMSKRKLNLLVTDKHVEGWDDPRMPTISGLRRRGYTAASIR
EFCKRIGVTKQDNTIEMASLESCIREDLNENAPRAMAVIDPVKLVIENYQ
GEGEMVTMPNHPNKPEMGSRQVPFSGEIWIDRADFREEANKQYKRLVLGK
EVRLRNAYVIKAERVEKDAEGNITTIFCTYDADTLGVIHWVSAAHALPVE
IRLYDRLFSVPNPGAADDFLSVINPESLVIKQGFAEPSLKDAVAGKAFQF
EREGYFCLDSRHSTAEKPVFNRTVGLRDT
Ligand information
>1euq Chain B (length=72) [Search RNA sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
gggguaucgccaagcgguaaggcaccggauucugauuccggcagcgaggu
ucgaauccucguaccccagcca
<<<<<<..<<<.........>>>.<<<<<.......>>>>>...<<<<<.
......>>>>>>>>>>>.....
Receptor-Ligand Complex Structure
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PDB1euq Influence of transfer RNA tertiary structure on aminoacylation efficiency by glutaminyl and cysteinyl-tRNA synthetases.
Resolution3.1 Å
Binding residue
(original residue number in PDB)		Q13 E34 D66 T68 N69 P126 R130 R133 L136 G168 C171 P181 F182 I183 V189 R192 K194 M210 Y211 F233 I313 T316 K317 Q318 N320 T321 E323 A325 S329 N336 R341 N370 Q399 K401 R410 R412 N413 V455 Q517 E519 R520 L544 R545
Binding residue
(residue number reindexed from 1)		Q6 E27 D59 T61 N62 P119 R123 R126 L129 G161 C164 P174 F175 I176 V182 R185 K187 M203 Y204 F226 I306 T309 K310 Q311 N313 T314 E316 A318 S322 N329 R334 N363 Q392 K394 R403 R405 N406 V437 Q499 E501 R502 L526 R527
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.
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:1euq, PDBe:1euq, PDBj:1euq
PDBsum1euq
PubMed10860750
UniProtP00962|SYQ_ECOLI Glutamine--tRNA ligase (Gene Name=glnS)

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