Structure of PDB 1e1t Chain A Binding Site BS03

Receptor Information
>1e1t Chain A (length=485) Species: 83333 (Escherichia coli K-12) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AIDFNDELRNRREKLAALRQQGVAFPNDFRRDHTSDQLHEEFDAKDNQEL
ESLNIEVSVAGRMMTRRIMGKASFVTLQDVGGRIQLYVARDSLPEGVYND
QFKKWDLGDIIGARGTLFKTQTGELSIHCTELRLLTKALRPLPDQEVRYR
QRYLDLIANDKSRQTFVVRSKILAAIRQFMVARGFMEVETPMMQVIPGGA
SARPFITHHNALDLDMYLRIAPELYLKRLVVGGFERVFEINRNFRNEGIS
VRHNPEFTMMELYMAYADYHDLIELTESLFRTLAQEVLGTTKVTYGEHVF
DFGKPFEKLTMREAIKKYRPETDMADLDNFDAAKALAESIGITVEKSWGL
GRIVTEIFDEVAEAHLIQPTFITEYPAEVSPLARRNDVNPEITDRFEFFI
GGREIGNGFSELNDAEDQAERFQEQVNAKAAGDDEAMFYDEDYVTALEYG
LPPTAGLGIGIDRMIMLFTNSHTIRDVILFPAMRP
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain1e1t Chain A Residue 603 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1e1t Active Site of Lysyl-tRNA Synthetase: Structural Studies of the Adenylation Reaction
Resolution2.4 Å
Binding residue
(original residue number in PDB)		E414 E421
Binding residue
(residue number reindexed from 1)		E397 E404
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) R262 E264 R269 H270 E421 N424 R480
Catalytic site (residue number reindexed from 1) R245 E247 R252 H253 E404 N407 R463
Enzyme Commision number 6.1.1.6: lysine--tRNA ligase.
Gene Ontology
Molecular Function
GO:0000049 tRNA binding
GO:0000166 nucleotide binding
GO:0000287 magnesium ion binding
GO:0003676 nucleic acid binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004824 lysine-tRNA ligase activity
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
Biological Process
GO:0006412 translation
GO:0006418 tRNA aminoacylation for protein translation
GO:0006430 lysyl-tRNA aminoacylation
GO:0034605 cellular response to heat
GO:0036260 RNA capping
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0016020 membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1e1t, PDBe:1e1t, PDBj:1e1t
PDBsum1e1t
PubMed10913247
UniProtP0A8N5|SYK2_ECOLI Lysine--tRNA ligase, heat inducible (Gene Name=lysU)

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