Structure of PDB 4dpg Chain G

Receptor sequence
>4dpgG (length=501) Species: 9606 (Homo sapiens) [Search protein sequence]
DPNQYYKIRSQAIHQLKVNGEDPYPHKFHVDISLTDFIQKYSHLQPGDHL
TDITLKVAGRIHAKRASGGKLIFYDLRGEGVKLQVMANSRNYKSEEEFIH
INNKLRRGDIIGVQGNPGKTKKGELSIIPYEITLLSPCLHMLPHGLKDKE
TRYRQRYLDLILNDFVRQKFIIRSKIITYIRSFLDELGFLEIETPMMNII
PGGAVAKPFITYHNELDMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRN
EGIDLTHNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKHITGSYKVTYH
PDGPEGQAYDVDFTPPFRRINMVEELEKALGMKLPETNLFETEETRKILD
DICVAKAVECPPPRTTARLLDKLVGEFLEVTCINPTFICDHPQIMSPLAK
WHRSKEGLTERFELFVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDD
EAMFIDENFCTALEYGLPPTAGWGMGIDRVAMFLTDSNNIKEVLLFPAMK
P
3D structure
PDB4dpg Structural Switch of Lysyl-tRNA Synthetase between Translation and Transcription.
ChainG
Resolution2.844 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R323 E325 T330 H331 E494 N497 R553
Catalytic site (residue number reindexed from 1) R249 E251 T256 H257 E420 N423 R479
Enzyme Commision number 2.7.7.-
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 LYS G E301 E339 Y341 N497 Y499 E501 G546 E227 E265 Y267 N423 Y425 E427 G472
BS02 APC G R323 T330 H331 N332 F335 R553 R249 T256 H257 N258 F261 R479
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003676 nucleic acid binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004824 lysine-tRNA ligase activity
GO:0005524 ATP binding
Biological Process
GO:0006418 tRNA aminoacylation for protein translation
GO:0006430 lysyl-tRNA aminoacylation
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4dpg, PDBe:4dpg, PDBj:4dpg
PDBsum4dpg
PubMed23159739
UniProtQ15046|SYK_HUMAN Lysine--tRNA ligase (Gene Name=KARS1)

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