4ZAJ

2.2 Angstrom Crystal Structure of a Human Arginyl-tRNA Synthetase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004812	molecular_function	aminoacyl-tRNA ligase activity
A	0004814	molecular_function	arginine-tRNA ligase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0006418	biological_process	tRNA aminoacylation for protein translation
A	0006420	biological_process	arginyl-tRNA aminoacylation

Functional Information from PROSITE/UniProt

site_id	PS00178
Number of Residues	12
Details	AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. PniAKeMHVGHL

Chain	Residue	Details
A	PRO129-LEU140

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	5
Details	BINDING: BINDING => ECO:0000269|PubMed:24859084, ECO:0007744|PDB:4Q2T

Chain	Residue	Details
A	PHE200
A	GLU211
A	SER384
A	VAL388
A	LYS412

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site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: N-acetylmethionine => ECO:0000269|PubMed:37316325, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378

Chain	Residue	Details
A	MET1

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