Structure of PDB 4jyz Chain A Binding Site BS01

Receptor Information
>4jyz Chain A (length=542) Species: 83333 (Escherichia coli K-12) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PTNFIRQIIDEDLASGKHTTVHTRFPPEPNGYLHIGHAKSICLNFGIAQD
YKGQCNLRFDDTNPVKEDIEYVESIKNDVEWLGFHWSGNVRYSSDYFDQL
HAYAIELINKGLAYVDELTPEQIREYRGTLTQPGKNSPYRDRSVEENLAL
FEKMRAGGFEEGKACLRAKIDMASPFIVMRDPVLYRIKFAEHHQTGNKWC
IYPMYDFTHCISDALEGITHSLCTLEFQDNRRLYDWVLDNITIPVHPRQY
EFSRLNLEYTVMSKRKLNLLVTDKHVEGWDDPRMPTISGLRRRGYTAASI
REFCKRIGVTKQDNTIEMASLESCIREDLNENAPRAMAVIDPVKLVIENY
QGEGEMVTMPNHPNKPEMGSRQVPFSGEIWIDRADFREEANKQYKRLVLG
KEVRLRNAYVIKAERVEKDAEGNITTIFCTYDADTLSKDPADGRKVKGVI
HWVSAAHALPVEIRLYDRLFSVPNPGAADDFLSVINPESLVIKQGFAEPS
LKDAVAGKAFQFEREGYFCLDSRHSTAEKPVFNRTVGLRDTW
Ligand information
>4jyz Chain B (length=72) [Search RNA sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
gggguaucgccaagcgguaaggcaccgguuuuugauaccggcacgcaggu
ucgaauccugcuaccccagcca
<<<<<<..<<<.........>>>.<<<<<.......>>>>>...<<<<<.
......>>>>>>>>>>>.....
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB4jyz Structural and Mechanistic Basis for Enhanced Translational Efficiency by 2-Thiouridine at the tRNA Anticodon Wobble Position.
Resolution2.5 Å
Binding residue
(original residue number in PDB)		Q13 E34 T68 N69 P126 R130 R133 T135 L136 G168 C171 P181 F182 I183 V189 R192 K194 M210 Y211 F233 Q234 D235 R238 I313 T316 K317 Q318 D319 N320 T321 E323 A325 S326 S329 N336 R341 N370 Q399 K401 R402 R410 R412 S443 K444 V455 Q517 E519 R520 L544 R545 T547 W548
Binding residue
(residue number reindexed from 1)		Q7 E28 T62 N63 P120 R124 R127 T129 L130 G162 C165 P175 F176 I177 V183 R186 K188 M204 Y205 F227 Q228 D229 R232 I307 T310 K311 Q312 D313 N314 T315 E317 A319 S320 S323 N330 R335 N364 Q393 K395 R396 R404 R406 S437 K438 V449 Q511 E513 R514 L538 R539 T541 W542
Binding affinityPDBbind-CN: Kd=0.47uM
Enzymatic activity
Catalytic site (original residue number in PDB) E34 R260 K270
Catalytic site (residue number reindexed from 1) E28 R254 K264
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
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4jyz, PDBe:4jyz, PDBj:4jyz
PDBsum4jyz
PubMed23727144
UniProtP00962|SYQ_ECOLI Glutamine--tRNA ligase (Gene Name=glnS)

[Back to BioLiP]