1BS2

YEAST 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	0005739	cellular_component	mitochondrion
A	0005829	cellular_component	cytosol
A	0006412	biological_process	translation
A	0006418	biological_process	tRNA aminoacylation for protein translation
A	0006420	biological_process	arginyl-tRNA aminoacylation
A	0032543	biological_process	mitochondrial translation
A	1990825	molecular_function	sequence-specific mRNA binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE ARG A 900

Chain	Residue
A	LYS79
A	GLN375
A	GLU148
A	SER151
A	ASN153
A	HIS162
A	TYR188
A	TYR347
A	ASP351
A	TYR369

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	PRO152-LEU163

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:11060012, ECO:0000269|PubMed:9736621, ECO:0007744|PDB:1BS2, ECO:0007744|PDB:1F7U

Chain	Residue	Details
A	GLU148
A	TYR347
A	ASP351
A	GLN375

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:9736621, ECO:0007744|PDB:1BS2

Chain	Residue	Details
A	HIS162

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: N-acetylalanine => ECO:0007744|PubMed:22814378

Chain	Residue	Details
A	ALA2

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198

Chain	Residue	Details
A	SER15

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	3
Details	M-CSA 235

Chain	Residue	Details
A	LYS156	attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor
A	HIS159	electrostatic stabiliser, hydrogen bond donor
A	HIS162	electrostatic stabiliser, hydrogen bond donor

---