Structure of PDB 4pg3 Chain B

Receptor sequence
>4pg3B (length=486) Species: 36329 (Plasmodium falciparum 3D7) [Search protein sequence]
PRLYFENRSKFIQDQKDKGINPYPHKFERTISIPEFIEKYKDLGNGEHLE
DTILNITGRIMRVSASGQKLRFFDLVGDGEKIQVLANYSFHNHEKGNFAE
CYDKIRRGDIVGIVGFPGKSKKGELSIFPKETILLSACLHMLPMKYGLKD
TEIRYRQRYLDLLINESSRHTFVTRTKIINFLRNFLNERGFFEVETPMMN
LIAGGANARPFITHHNDLDLDLYLRIATELPLKMLIVGGIDKVYEIGKVF
RNEGIDNTHNPEFTSCEFYWAYADYNDLIKWSEDFFSQLVYHLFGTYKIS
YNKDGPENQPIEIDFTPPYPKVSIVEEIEKVTNTILEQPFDSNETIEKMI
NIIKEHKIELPNPPTAAKLLDQLASHFIENKYNDKPFFIVEHPQIMSPLA
KYHRTKPGLTERLEMFICGKEVLNAYTELNDPFKQKECFLDSAFCTSLEY
GLPPTGGLGLGIDRITMFLTNKNSIKDVILFPTMRP
3D structure
PDB4pg3 Structural basis of malaria parasite lysyl-tRNA synthetase inhibition by cladosporin.
ChainB
Resolution2.696 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) R251 E253 T258 H259 E421 N424 R464
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 B E308 E346 Y348 N503 Y505 E507 G552 E229 E267 Y269 N424 Y426 E428 G457
BS02 KRS B R330 E332 H338 N339 F342 E500 V501 G554 G556 R559 R251 E253 H259 N260 F263 E421 V422 G459 G461 R464 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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4pg3, PDBe:4pg3, PDBj:4pg3
PDBsum4pg3
PubMed24935905
UniProtQ8IDJ8

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