Structure of PDB 1euq Chain A Binding Site BS02

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
Ligand IDQSI
InChIInChI=1S/C15H22N8O8S/c16-6(1-2-8(17)24)14(27)22-32(28,29)30-3-7-10(25)11(26)15(31-7)23-5-21-9-12(18)19-4-20-13(9)23/h4-7,10-11,15,25-26H,1-3,16H2,(H2,17,24)(H,22,27)(H2,18,19,20)/t6-,7+,10+,11+,15+/m0/s1
InChIKeyKXWKSWRGZLZHEF-WERHYGNASA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)COS(=O)(=O)NC(=O)[C@H](CCC(=O)N)N)O)O)N
CACTVS 3.341N[CH](CCC(N)=O)C(=O)N[S](=O)(=O)OC[CH]1O[CH]([CH](O)[CH]1O)n2cnc3c(N)ncnc23
ACDLabs 10.04O=C(N)CCC(N)C(=O)NS(=O)(=O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
CACTVS 3.341N[C@@H](CCC(N)=O)C(=O)N[S](=O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1O)n2cnc3c(N)ncnc23
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COS(=O)(=O)NC(=O)C(CCC(=O)N)N)O)O)N
FormulaC15 H22 N8 O8 S
Name5'-O-[N-(L-GLUTAMINYL)-SULFAMOYL]ADENOSINE
ChEMBLCHEMBL1163072
DrugBank
ZINCZINC000031976683
PDB chain1euq Chain A Residue 998 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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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)		P33 H40 G42 H43 S46 Y211 H215 C229 F233 R260 K270
Binding residue
(residue number reindexed from 1)		P26 H33 G35 H36 S39 Y204 H208 C222 F226 R253 K263
Annotation score2
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

View graph for
Molecular Function
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Biological Process
View graph for
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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