6WOM

Crystal structure of Aspartyl-tRNA ligase from Elizabethkingia sp.

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue SO4 A 700

Chain	Residue
A	ARG68
A	LEU108
A	HOH829
A	HOH1165

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site_id	AC2
Number of Residues	2
Details	binding site for residue SO4 B 700

Chain	Residue
B	ARG68
B	HOH921

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