3REX

Crystal structure of the archaeal asparagine synthetase A complexed with Adenosine monophosphate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004812	molecular_function	aminoacyl-tRNA ligase activity
A	0004816	molecular_function	asparagine-tRNA ligase activity
A	0005524	molecular_function	ATP binding
A	0006412	biological_process	translation
A	0006418	biological_process	tRNA aminoacylation for protein translation
A	0006421	biological_process	asparaginyl-tRNA aminoacylation
A	0016874	molecular_function	ligase activity
A	0046872	molecular_function	metal ion binding
B	0000166	molecular_function	nucleotide binding
B	0004812	molecular_function	aminoacyl-tRNA ligase activity
B	0004816	molecular_function	asparagine-tRNA ligase activity
B	0005524	molecular_function	ATP binding
B	0006412	biological_process	translation
B	0006418	biological_process	tRNA aminoacylation for protein translation
B	0006421	biological_process	asparaginyl-tRNA aminoacylation
B	0016874	molecular_function	ligase activity
B	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	21
Details	BINDING SITE FOR RESIDUE AMP A 295

Chain	Residue
A	ARG99
A	SER217
A	SER218
A	GLY264
A	ARG267
A	HOH312
A	HOH324
A	HOH388
A	HOH392
A	HOH394
A	HOH446
A	GLU101
A	HOH452
A	HOH463
A	ARG109
A	HIS110
A	SER111
A	PHE114
A	GLN116
A	GLU215
A	VAL216

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 296

Chain	Residue
A	ASP52
A	HOH388
A	HOH391
A	HOH392
A	HOH393
A	HOH421

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site_id	AC3
Number of Residues	16
Details	BINDING SITE FOR RESIDUE AMP B 295

Chain	Residue
B	ARG99
B	GLU101
B	ARG109
B	HIS110
B	SER111
B	PHE114
B	GLN116
B	GLU215
B	VAL216
B	SER217
B	SER218
B	GLY264
B	ARG267
B	HOH309
B	HOH327
B	HOH344

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