Structure of PDB 3a5y Chain A

Receptor sequence
>3a5yA (length=297) Species: 562 (Escherichia coli) [Search protein sequence]
ASWQPSASIPNLLKRAAIMAEIRRFFADRGVLEVETPCMSQATVTDIHLV
PFETRFVGPGHSQGMNLWLMTSPEYHMKRLLVAGCGPVFQLCRSFRNEEM
GRYHNPEFTMLEWYRPHYDMYRLMNEVDDLLQQVLDCPAAESLSYQQAFL
RYLEIDPLSADTLLQLLFTFGVEPNIGKEKPTFVYHFPASQASLAQISTE
DHRVAERFEVYYKGIELANGFHELTDAREQQQRFEQDNRKRAARGLPQHP
IDQNLIEALKVGMPDCSGVALGVDRLVMLALGAETLAEVIAFSVDRA
3D structure
PDB3a5y A paralog of lysyl-tRNA synthetase aminoacylates a conserved lysine residue in translation elongation factor P.
ChainA
Resolution1.9 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 6.3.1.-
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 KAA A S76 E78 R100 H108 N109 F112 M114 Y118 E244 L245 N247 F249 E251 G296 A298 G300 R303 S72 E74 R96 H104 N105 F108 M110 Y114 E216 L217 N219 F221 E223 G268 A270 G272 R275 MOAD: Kd=11nM
PDBbind-CN: -logKd/Ki=7.96,Kd=11nM
Gene Ontology
Molecular Function
GO:0000049 tRNA binding
GO:0000166 nucleotide binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004824 lysine-tRNA ligase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0016880 acid-ammonia (or amide) ligase activity
GO:0042803 protein homodimerization activity
GO:0052868 protein-lysine lysyltransferase activity
Biological Process
GO:0006418 tRNA aminoacylation for protein translation
GO:0006430 lysyl-tRNA aminoacylation
GO:0043687 post-translational protein modification
GO:0071468 cellular response to acidic pH
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:3a5y, PDBe:3a5y, PDBj:3a5y
PDBsum3a5y
PubMed20729861
UniProtP0A8N7|EPMA_ECOLI Elongation factor P--(R)-beta-lysine ligase (Gene Name=epmA)

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