Structure of PDB 3vgj Chain A

Receptor sequence
>3vgjA (length=353) Species: 36329 (Plasmodium falciparum 3D7) [Search protein sequence]
EESKIEDVDKILNDILSISSECIQPDELRVKLLLKRKLICYDGFEPSGRM
HIAQGLLKSIIVNKLTSNGCTFIFWIADWFAHLNNKMSGDLKKIKKVGSY
FIEVWKSCGMNMENVQFLWASEEINKKPNEYWSLVLDISRSFNINRMKRC
LKIMGRSEGEENYCSQILYPCMQCADIFFLNVDICQLGIDQRKVNMLARE
YCDIKKIKKKPVILSHGMLPGLLEGQEKMSKSDENSAIFMDDSESDVNRK
IKKAYCPPNVIENNPIYAYAKSIIFPSYNEFNLVRKEKNGGDKTYYTLQE
LEHDYVNGFIHPLDLKDNVAMYINKLLQPVRDHFQNNIEAKNLLNEIKKY
KVT
3D structure
PDB3vgj Malaria parasite tyrosyl-tRNA synthetase secretion triggers pro-inflammatory responses.
ChainA
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 A Y60 G62 E64 W94 F99 I172 Y188 Q192 D195 Q210 Y41 G43 E45 W75 F80 I153 Y169 Q173 D176 Q191
BS02 AMP A D61 G62 F63 E64 H70 A72 Q73 G207 D209 H235 M237 L238 K247 M248 D42 G43 F44 E45 H51 A53 Q54 G188 D190 H216 M218 L219 K228 M229
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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