Structure of PDB 3e9h Chain D

Receptor sequence
>3e9hD (length=484) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence]
ELNDQLRVRREKLKKIEELGVDPFGKRFERTHKAEELFELYGDLSKEELE
EQQIEVAVAGRIMTKRGMGKAGFAHIQDVTGQIQIYVRQDDVGEQQYELF
KISDLGDIVGVRGTMFKTKVGELSIKVSSYEFLTKALRPLPEKDIEQRYR
QRYLDLIMNPESKKTFITRSLIIQSMRRYLDSHGYLEVETPMMHAVAGGA
AARPFITHHNALDMTLYMRIAIELHLKRLIVGGLEKVYEIGRVFRNEGIS
TRHNPEFTMLELYEAYADFRDIMKLTENLIAHIATEVLGTTKIQYGEHLV
DLTPEWRRLHMVDAIKEYVGVDFWRQMSDEEARELAKEHGVEVAPHMTFG
HIVNEFFEQKVEDKLIQPTFIYGHPVEISPLAKKNPDDPRFTDRFELFIV
GREHANAFTELNDPIDQRQRFEEQLKEREQGNDEAHEMDEDFLEALEYGM
PPTGGLGIGVDRLVMLLTNSPSIRDVLLFPQMRH
3D structure
PDB3e9h Two crystal structures of lysyl-tRNA synthetase from Bacillus stearothermophilus in complex with lysyladenylate-like compounds: insights into the irreversible formation of the enzyme-bound adenylate of L-lysine hydroxamate
ChainD
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R253 E255 R260 H261 E411 N414 R470
Catalytic site (residue number reindexed from 1) R245 E247 R252 H253 E403 N406 R462
Enzyme Commision number 6.1.1.6: lysine--tRNA ligase.
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 MG D E404 E411 N414 E396 E403 N406
BS02 KAA D G207 E231 R253 H261 N262 F265 M267 E269 Y271 E411 H412 N414 F416 E418 G467 R470 G199 E223 R245 H253 N254 F257 M259 E261 Y263 E403 H404 N406 F408 E410 G459 R462
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:0016740 transferase activity
GO:0046872 metal ion binding
Biological Process
GO:0006412 translation
GO:0006418 tRNA aminoacylation for protein translation
GO:0006430 lysyl-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:3e9h, PDBe:3e9h, PDBj:3e9h
PDBsum3e9h
PubMed19174549
UniProtQ9RHV9|SYK_GEOSE Lysine--tRNA ligase (Gene Name=lysS)

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