Structure of PDB 2zue Chain A

Receptor sequence
>2zueA (length=628) Species: 53953 (Pyrococcus horikoshii) [Search protein sequence]
LMEIRESVKERIEEIIKEIAPQWEGEIELKETPDPKLGDFGTPIAFKLAK
LLKRPPIEIAEKIVEKLKLNLPEGIKDVKAVNGYINVFIDYPHFARILIN
DILAKGDRFGSSEIGKGKKVIVEHTSVNPTKPLHMGHARNAILGDVMARI
LRFLGYEVEVQNYIDDLGIQFAQVYWGYLRLKEEFERIMNELRERGLKDN
PIDHALGLLYVEVNRRLEDNPELENEIRDIMKKLESGELYGRKLAEEVVR
AQMVTTYKLGVKYDLLVWESDIVRRKLFEIALELLSKNENFYIPSDGKYR
GAFVMDLRKLFPDMKNPILVLRRSDGTATYTGKDIAYHLWKFGKIDVDLL
YKEWDSTTWTTAPDGKSMPNKFGNANIVINVIGAEQKHPQLAIKYALQLL
GFEDAAANLYHLAYEHVERPEGKFSGRKGTWVGFTVDEVIQEAVKRAREL
IEEKNPALSDEEKAEVAEKVGIGAIRYNLIKYSPDKKIIFRWEDVLNFEG
ESAPYIQYAHARCSSILRKAEEEGIKVDPETLFKNADFTKLSERERELVI
MLSKFPRIVEQAGKDVKPHLIAWFANELASLFNKFYMDHPVLKAEEGVRE
ARLLLVMAVEQVLKNALYLMGIEAPERM
3D structure
PDB2zue Modeling of tRNA-assisted mechanism of Arg activation based on a structure of Arg-tRNA synthetase, tRNA, and an ATP analog (ANP)
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K132 H135 H138
Catalytic site (residue number reindexed from 1) K131 H134 H137
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
Biological Process
GO:0006412 translation
GO:0006418 tRNA aminoacylation for protein translation
GO:0006420 arginyl-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:2zue, PDBe:2zue, PDBj:2zue
PDBsum2zue
PubMed19656186
UniProtO59147|SYR_PYRHO Arginine--tRNA ligase (Gene Name=argS)

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