Structure of PDB 1f7v Chain A

Receptor sequence
>1f7vA (length=606) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
ASTANMISQLKKLSIAEPAVAKDSHPDVNIVDLMRNYISQELSKISGVDS
SLIFPALEWTNTMERGDLLIPIPRLRIKGANPKDLAVQWAEKFPCGDFLE
KVEANGPFIQFFFNPQFLAKLVIPDILTRKEDYGSCKLVENKKVIIEFSS
PNIAKPFHAGHLRSTIIGGFLANLYEKLGWEVIRMNYLGDWGKQFGLLAV
GFERYGNEEALVKDPIHHLFDVYVRINKDIEEEGDSIPLEQSTNGKAREY
FKRMEDGDEEALKIWKRFREFSIEKYIDTYARLNIKYDVYSGESQVSKES
MLKAIDLFKEKGLTHEDKGAVLIDLTKFNKKLGKAIVQKSDGTTLYLTRD
VGAAMDRYEKYHFDKMIYVIASQQDLHAAQFFEILKQMGFEWAKDLQHVN
FGMVQGMSTRKGTVVFLDNILEETKEKMHEVMKKNENKYAQIEHPEEVAD
LVGISAVMIQDMQGKRINNYEFKWERMLSFEGDTGPYLQYAHSRLRSVER
NASGITQEKWINADFSLLKEPAAKLLIRLLGQYPDVLRNAIKTHEPTTVV
TYLFKLTHQVSSCYDVLWVAGQTEELATARLALYGAARQVLYNGMRLLGL
TPVERM
3D structure
PDB1f7v tRNA aminoacylation by arginyl-tRNA synthetase: induced conformations during substrates binding
ChainA
Resolution2.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K156 H159 H162
Catalytic site (residue number reindexed from 1) K155 H158 H161
Enzyme Commision number 6.1.1.19: arginine--tRNA ligase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004814 arginine-tRNA ligase activity
GO:0005524 ATP binding
GO:1990825 sequence-specific mRNA binding
Biological Process
GO:0006412 translation
GO:0006418 tRNA aminoacylation for protein translation
GO:0006420 arginyl-tRNA aminoacylation
GO:0032543 mitochondrial translation
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion
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:1f7v, PDBe:1f7v, PDBj:1f7v
PDBsum1f7v
PubMed11060012
UniProtQ05506|SYRC_YEAST Arginine--tRNA ligase, cytoplasmic (Gene Name=YDR341C)

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