Structure of PDB 3bju Chain B

Receptor sequence

>3bjuB (length=495) Species: 9606 (Homo sapiens)

DPNQYYKIRSQAIHQLKVNGEDPYPHKFHVDISLTDFIQKYSHLQPGDHL
TDITLKVAGRIHAKRASGGKLIFYDLRGEGVKLQVMANSRNYKSEEEFIH
INNKLRRGDIIGVQGNPGKTKKGELSIIPYEITLLSPCLHMLPKETRYRQ
RYLDLILNDFVRQKFIIRSKIITYIRSFLDELGFLEIETPMMNIIPGGAV
AKPFITYHNELDMNLYMRIAPELYHKMLVVGGIDRVYEIGRQFRNEGIDL
THNPEFTTCEFYMAYADYHDLMEITEKMVSGMVKHITGSYKVTYHPDGPE
GQAYDVDFTPPFRRINMVEELEKALGMKLPETNLFETEETRKILDDICVA
KAVECPPPRTTARLLDKLVGEFLEVTCINPTFICDHPQIMSPLAKWHRSK
EGLTERFELFVMKKEICNAYTELNDPMRQRQLFEEQAKAKAAGDDEAMFI
DENFCTALEYGLPPTAGWGMGIDRVAMFLTDSNNIKEVLLFPAMK

3D structure

• PDB: 3bju Crystal structure of tetrameric form of human lysyl-tRNA synthetase: Implications for multisynthetase complex formation
• Chain: B
• Resolution: 2.31 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R323 E325 T330 H331 E494 N497 R553
• Catalytic site (residue number reindexed from 1): R244 E246 T251 H252 E415 N418 R474
• 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	CA	B	E487 E494 N497	E408 E415 N418
BS02	LYS	B	E301 E339 Y341 N497 Y499 E501 G546	E222 E260 Y262 N418 Y420 E422 G467
BS03	ATP	B	R323 H331 N332 F335 E494 I495 R553	R244 H252 N253 F256 E415 I416 R474

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

External links

• PDB: RCSB:3bju, PDBe:3bju, PDBj:3bju
• PDBsum: 3bju
• PubMed: 18272479
• UniProt: Q15046|SYK_HUMAN Lysine--tRNA ligase (Gene Name=KARS1)