Structure of PDB 4jxz Chain A Binding Site BS01

Receptor Information
>4jxz Chain A (length=538) 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
KEVRLRNAYVIKAERVEKDAEGNITTIFCTYDADTLSKGRKVKGVIHWVS
AAHALPVEIRLYDRLFSVPNPGAADDFLSVINPESLVIKQGFAEPSLKDA
VAGKAFQFEREGYFCLDSRHSTAEKPVFNRTVGLRDTW
Ligand information
>4jxz Chain B (length=71) [Search RNA sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
gggguaucgccaagcgguaaggcaccgguuuuugauaccggccgcagguu
cgaauccugcuaccccagcca
<<<<<<..<<<.........>>>.<<<<<.......>>>>>..<<<<<..
.....>>>>>>>>>>>.....
Receptor-Ligand Complex Structure
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PDB4jxz Structural and Mechanistic Basis for Enhanced Translational Efficiency by 2-Thiouridine at the tRNA Anticodon Wobble Position.
Resolution2.4 Å
Binding residue
(original residue number in PDB)		Q13 E34 T68 N69 P126 R130 R133 T135 L136 G168 P181 F182 I183 R192 K194 M210 Y211 F233 Q234 D235 R238 I313 T316 K317 Q318 D319 N320 T321 E323 S326 S329 N336 R341 N370 Q399 R402 R410 R412 L442 S443 V455 Q517 E519 R520 R545 T547 W548
Binding residue
(residue number reindexed from 1)		Q7 E28 T62 N63 P120 R124 R127 T129 L130 G162 P175 F176 I177 R186 K188 M204 Y205 F227 Q228 D229 R232 I307 T310 K311 Q312 D313 N314 T315 E317 S320 S323 N330 R335 N364 Q393 R396 R404 R406 L436 S437 V445 Q507 E509 R510 R535 T537 W538
Binding affinityPDBbind-CN: Kd=1.84uM
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4jxz, PDBe:4jxz, PDBj:4jxz
PDBsum4jxz
PubMed23727144
UniProtP00962|SYQ_ECOLI Glutamine--tRNA ligase (Gene Name=glnS)

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