Structure of PDB 3vgj Chain B

Receptor sequence
>3vgjB (length=356) Species: 36329 (Plasmodium falciparum 3D7) [Search protein sequence]
AQEESKIEDVDKILNDILSISSECIQPDELRVKLLLKRKLICYDGFEPSG
RMHIAQGLLKSIIVNKLTSNGCTFIFWIADWFAHLNNKMSGDLKKIKKVG
SYFIEVWKSCGMNMENVQFLWASEEINKKPNEYWSLVLDISRSFNINRMK
RCLKIMGRSEGEENYCSQILYPCMQCADIFFLNVDICQLGIDQRKVNMLA
REYCDIKKIKKKPVILSHGMLPGLLEGQEKMSKSDENSAIFMDDSESDVN
RKIKKAYCPPNVIENNPIYAYAKSIIFPSYNEFNLVRKEKNGGDKTYYTL
QELEHDYVNGFIHPLDLKDNVAMYINKLLQPVRDHFQNNIEAKNLLNEIK
KYKVTK
3D structure
PDB3vgj Malaria parasite tyrosyl-tRNA synthetase secretion triggers pro-inflammatory responses.
ChainB
Resolution2.212 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 6.1.1.1: tyrosine--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 TYR B Y60 G62 E64 W94 F99 I172 Y188 Q192 D195 L206 Q210 Y43 G45 E47 W77 F82 I155 Y171 Q175 D178 L189 Q193
BS02 AMP B D61 G62 F63 E64 A72 L206 G207 D209 H235 M237 L238 K247 M248 D44 G45 F46 E47 A55 L189 G190 D192 H218 M220 L221 K230 M231
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004831 tyrosine-tRNA ligase activity
GO:0005524 ATP binding
GO:0046789 host cell surface receptor binding
GO:0046872 metal ion binding
Biological Process
GO:0006412 translation
GO:0006418 tRNA aminoacylation for protein translation
GO:0006437 tyrosyl-tRNA aminoacylation
GO:0044650 adhesion of symbiont to host cell
Cellular Component
GO:0005737 cytoplasm
GO:0044164 host cell cytosol

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:3vgj, PDBe:3vgj, PDBj:3vgj
PDBsum3vgj
PubMed22068597
UniProtQ8IAR7

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