1EFW

Crystal structure of aspartyl-tRNA synthetase from Thermus thermophilus complexed to tRNAasp from Escherichia coli

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003676	molecular_function	nucleic acid binding
A	0004812	molecular_function	aminoacyl-tRNA ligase activity
A	0004815	molecular_function	aspartate-tRNA ligase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0006412	biological_process	translation
A	0006418	biological_process	tRNA aminoacylation for protein translation
A	0006422	biological_process	aspartyl-tRNA aminoacylation
A	0016874	molecular_function	ligase activity
B	0000166	molecular_function	nucleotide binding
B	0003676	molecular_function	nucleic acid binding
B	0004812	molecular_function	aminoacyl-tRNA ligase activity
B	0004815	molecular_function	aspartate-tRNA ligase activity
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0006412	biological_process	translation
B	0006418	biological_process	tRNA aminoacylation for protein translation
B	0006422	biological_process	aspartyl-tRNA aminoacylation
B	0016874	molecular_function	ligase activity

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Region: {"description":"Aspartate","evidences":[{"source":"HAMAP-Rule","id":"MF_00044","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	22
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00044","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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