7YDG

Crystal structure of human SARS2 catalytic domain with a disease related mutation

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004812	molecular_function	aminoacyl-tRNA ligase activity
A	0004828	molecular_function	serine-tRNA ligase activity
A	0005524	molecular_function	ATP binding
A	0006418	biological_process	tRNA aminoacylation for protein translation
A	0006434	biological_process	seryl-tRNA aminoacylation
B	0000166	molecular_function	nucleotide binding
B	0004812	molecular_function	aminoacyl-tRNA ligase activity
B	0004828	molecular_function	serine-tRNA ligase activity
B	0005524	molecular_function	ATP binding
B	0006418	biological_process	tRNA aminoacylation for protein translation
B	0006434	biological_process	seryl-tRNA aminoacylation
C	0000166	molecular_function	nucleotide binding
C	0004812	molecular_function	aminoacyl-tRNA ligase activity
C	0004828	molecular_function	serine-tRNA ligase activity
C	0005524	molecular_function	ATP binding
C	0006418	biological_process	tRNA aminoacylation for protein translation
C	0006434	biological_process	seryl-tRNA aminoacylation
D	0000166	molecular_function	nucleotide binding
D	0004812	molecular_function	aminoacyl-tRNA ligase activity
D	0004828	molecular_function	serine-tRNA ligase activity
D	0005524	molecular_function	ATP binding
D	0006418	biological_process	tRNA aminoacylation for protein translation
D	0006434	biological_process	seryl-tRNA aminoacylation

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9N0F3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	4
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9JJL8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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