8I1W

The asymmetric structure of homodimeric E. coli TrpRS bound with tryptophanyl adenylate at one of its two active pockets

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004812	molecular_function	aminoacyl-tRNA ligase activity
A	0004830	molecular_function	tryptophan-tRNA ligase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006412	biological_process	translation
A	0006418	biological_process	tRNA aminoacylation for protein translation
A	0006436	biological_process	tryptophanyl-tRNA aminoacylation
B	0000166	molecular_function	nucleotide binding
B	0004812	molecular_function	aminoacyl-tRNA ligase activity
B	0004830	molecular_function	tryptophan-tRNA ligase activity
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006412	biological_process	translation
B	0006418	biological_process	tRNA aminoacylation for protein translation
B	0006436	biological_process	tryptophanyl-tRNA aminoacylation

Functional Information from PROSITE/UniProt

site_id	PS00178
Number of Residues	10
Details	AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. P..SGeLTIGNY

Chain	Residue	Details
A	PRO12-TYR21

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00140

Chain	Residue	Details
A	GLN11
A	GLY19
A	ASP135
A	GLY147
A	VAL186
A	LYS195
B	GLN11
B	GLY19
B	ASP135
B	GLY147
B	VAL186
B	LYS195

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