Structure of PDB 1efw Chain A

Receptor sequence
>1efwA (length=580) Species: 274 (Thermus thermophilus) [Search protein sequence]
MRRTHYAGSLRETHVGEEVVLEGWVNRRRDLGGLIFLDLRDREGLVQLVA
HPASPAYATAERVRPEWVVRAKGLVRLRPEPNPRLATGRVEVELSALEVL
AEAKTPPFPVDAGWRGEEEKEASEELRLKYRYLDLRRRRMQENLRLRHRV
IKAIWDFLDREGFVQVETPFLTKSTPEGARDFLVPYRHEPGLFYALPQSP
QLFKQMLMVAGLDRYFQIARCFRDEDLRADRQPDFTQLDLEMSFVEVEDV
LELNERLMAHVFREALGVELPLPFPRLSYEEAMERYGSDKPDLRFGLELK
EVGPLFRQSGFRVFQEAESVKALALPKALSRKEVAELEEVAKRHKAQGLA
WARVEEGGFSGGVAKFLEPVREALLQATEARPGDTLLFVAGPRKVAATAL
GAVRLRAADLLGLKREGFRFLWVVDFPLLEWDEEEEAWTYMHHPFTSPHP
EDLPLLEKDPGRVRALAYDLVLNGVEVGGGSIRIHDPRLQARVFRLLGIG
EEEQREKFGFFLEALEYGAPPHGGIAWGLDRLLALMTGSPSIREVIAFPK
NKEGKDPLTGAPSPVPEEQLRELGLMVVRP
3D structure
PDB1efw An intermediate step in the recognition of tRNA(Asp) by aspartyl-tRNA synthetase.
ChainA
Resolution3.0 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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.
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 rna A R27 R29 D30 L31 G32 G33 L34 F36 Q47 H51 P52 R64 R78 E80 N82 R84 E91 T105 P107 E125 R343 R27 R29 D30 L31 G32 G33 L34 F36 Q47 H51 P52 R64 R78 E80 N82 R84 E91 T105 P107 E125 R343
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1efw, PDBe:1efw, PDBj:1efw
PDBsum1efw
PubMed10843857
UniProtP36419|SYD_THETH Aspartate--tRNA(Asp) ligase (Gene Name=aspS)

[Back to BioLiP]