Structure of PDB 4pg3 Chain D

Receptor sequence
>4pg3D (length=484) Species: 36329 (Plasmodium falciparum 3D7) [Search protein sequence]
PRLYFENRSKFIQDQKDKGINPYPHKFERTISIPEFIEKYKDLGNGEHLE
DTILNITGRIMRVSASGQKLRFFDLVGDGEKIQVLANYSFHNHEKGNFAE
CYDKIRRGDIVGIVGFPGKSKKGELSIFPKETILLSACLHMLPMKYGLTE
IRYRQRYLDLLINESSRHTFVTRTKIINFLRNFLNERGFFEVETPMMNLI
AGGANARPFITHHNDLDLDLYLRIATELPLKMLIVGGIDKVYEIGKVFRN
EGIDNTHNPEFTSCEFYWAYADYNDLIKWSEDFFSQLVYHLFGTYKISYN
KDGPENQPIEIDFTPPYPKVSIVEEIEKVTNTILEQPFDSNETIEKMINI
IKEHKIELPNPPTAAKLLDQLASHFIENKYNDKPFFIVEHPQIMSPLAKY
HRTKPGLTERLEMFICGKEVLNAYTELNDPFKQKECFLDSAFCTSLEYGL
PPTGGLGLGIDRITMFLTNKNSIKDVILFPTMRP
3D structure
PDB4pg3 Structural basis of malaria parasite lysyl-tRNA synthetase inhibition by cladosporin.
ChainD
Resolution2.696 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 E419 N422 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 LYS D E308 E346 Y348 N503 Y505 E507 G552 E227 E265 Y267 N422 Y424 E426 G455
BS02 KRS D R330 E332 H338 N339 F342 V501 G554 G556 R559 R249 E251 H257 N258 F261 V420 G457 G459 R462 BindingDB: IC50=120nM
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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:4pg3, PDBe:4pg3, PDBj:4pg3
PDBsum4pg3
PubMed24935905
UniProtQ8IDJ8

[Back to BioLiP]