Structure of PDB 6kcn Chain B

Receptor sequence
>6kcnB (length=500) Species: 5843 (Plasmodium falciparum NF54) [Search protein sequence]
DPRLYFENRSKFIQDQKDKGINPYPHKFERTISIPEFIEKYKDLGNGEHL
EDTILNITGRIMRVSASGQKLRFFDLVGDGEKIQVLANYSFHNHEKGNFA
ECYDKIRRGDIVGIVGFPGKSKKGELSIFPKETILLSACLHMLPMKKDTE
IRYRQRYLDLLINESSRHTFVTRTKIINFLRNFLNERGFFEVETPMMNLI
AGGANARPFITHHNDLDLDLYLRIATELPLKMLIVGGIDKVYEIGKVFRN
EGIDNTHNPEFTSCEFYWAYADYNDLIKWSEDFFSQLVYHLFGTYKISYN
KDGPENQPIEIDFTPPYPKVSIVEEIEKVTNTILEQPFDSNETIEKMINI
IKEHKIELPPPTAAKLLDQLASHFIENKYNDKPFFIVEHPQIMSPLAKYH
RTKPGLTERLEMFICGKEVLNAYTELNDPFKQKECFKLQQKDREKGDTEA
AQLDSAFCTSLEYGLPPTGGLGLGIDRITMFLTNKNSIKDVILFPTMRPA
3D structure
PDB6kcn Atomic Resolution Analyses of Isocoumarin Derivatives for Inhibition of Lysyl-tRNA Synthetase.
ChainB
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R330 E332 T337 H338 E500 N503 R559
Catalytic site (residue number reindexed from 1) R249 E251 T256 H257 E418 N421 R477
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 D5F B R330 E332 H338 N339 F342 E500 L502 G554 R559 R249 E251 H257 N258 F261 E418 L420 G472 R477 MOAD: ic50=276nM
BS02 LYS B E308 E346 Y348 N503 Y505 E507 G552 G554 E227 E265 Y267 N421 Y423 E425 G470 G472
Gene Ontology
Molecular Function
GO:0000049 tRNA binding
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
GO:0016874 ligase activity
Biological Process
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:6kcn, PDBe:6kcn, PDBj:6kcn
PDBsum6kcn
PubMed32195573
UniProtW7JP72

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