Structure of PDB 1efw Chain A Binding Site BS01

Receptor Information
>1efw Chain A (length=580) Species: 274 (Thermus thermophilus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MRRTHYAGSLRETHVGEEVVLEGWVNRRRDLGGLIFLDLRDREGLVQLVA
HPASPAYATAERVRPEWVVRAKGLVRLRPEPNPRLATGRVEVELSALEVL
AEAKTPPFPVDAGWRGEEEKEASEELRLKYRYLDLRRRRMQENLRLRHRV
IKAIWDFLDREGFVQVETPFLTKSTPEGARDFLVPYRHEPGLFYALPQSP
QLFKQMLMVAGLDRYFQIARCFRDEDLRADRQPDFTQLDLEMSFVEVEDV
LELNERLMAHVFREALGVELPLPFPRLSYEEAMERYGSDKPDLRFGLELK
EVGPLFRQSGFRVFQEAESVKALALPKALSRKEVAELEEVAKRHKAQGLA
WARVEEGGFSGGVAKFLEPVREALLQATEARPGDTLLFVAGPRKVAATAL
GAVRLRAADLLGLKREGFRFLWVVDFPLLEWDEEEEAWTYMHHPFTSPHP
EDLPLLEKDPGRVRALAYDLVLNGVEVGGGSIRIHDPRLQARVFRLLGIG
EEEQREKFGFFLEALEYGAPPHGGIAWGLDRLLALMTGSPSIREVIAFPK
NKEGKDPLTGAPSPVPEEQLRELGLMVVRP
Ligand information
>1efw Chain C (length=73) [Search RNA sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
ggagcgguaguucagucgguuagaauaccugccugucacgcagggggucg
cggguucgagucccguccguucc
<<<<<<<..<<<<.........>>>>.<<<<<.......>>>>>.....<
<<<<.......>>>>>>>>>>>>
Receptor-Ligand Complex Structure
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PDB1efw An intermediate step in the recognition of tRNA(Asp) by aspartyl-tRNA synthetase.
Resolution3.0 Å
Binding residue
(original residue number in PDB)		R27 R29 D30 L31 G32 G33 L34 F36 Q47 H51 P52 R64 R78 E80 N82 R84 E91 T105 P107 E125 R343
Binding residue
(residue number reindexed from 1)		R27 R29 D30 L31 G32 G33 L34 F36 Q47 H51 P52 R64 R78 E80 N82 R84 E91 T105 P107 E125 R343
Enzymatic activity
Catalytic site (original residue number in PDB) R223 E225 R231 Q232 E476 G479 R531
Catalytic site (residue number reindexed from 1) R223 E225 R231 Q232 E476 G479 R531
Enzyme Commision number 6.1.1.12: aspartate--tRNA ligase.
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003676 nucleic acid binding
GO:0004812 aminoacyl-tRNA ligase activity
GO:0004815 aspartate-tRNA ligase activity
GO:0005524 ATP binding
GO:0016874 ligase activity
Biological Process
GO:0006412 translation
GO:0006418 tRNA aminoacylation for protein translation
GO:0006422 aspartyl-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:1efw, PDBe:1efw, PDBj:1efw
PDBsum1efw
PubMed10843857
UniProtP36419|SYD_THETH Aspartate--tRNA(Asp) ligase (Gene Name=aspS)

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