1YID

Crystal structure of tryptophanyl tRNA synthetase II from Deinococcus radiodurans in complex with ATP.

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	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	0006412	biological_process	translation
B	0006418	biological_process	tRNA aminoacylation for protein translation
B	0006436	biological_process	tryptophanyl-tRNA aminoacylation
C	0000166	molecular_function	nucleotide binding
C	0004812	molecular_function	aminoacyl-tRNA ligase activity
C	0004830	molecular_function	tryptophan-tRNA ligase activity
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0006412	biological_process	translation
C	0006418	biological_process	tRNA aminoacylation for protein translation
C	0006436	biological_process	tryptophanyl-tRNA aminoacylation

Functional Information from PDB Data

Chain	Residue
B	ATP3000

site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE ATP B 3000

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..TGaLHLGHL

Chain	Residue	Details
B	PRO31-LEU40

Functional Information from SwissProt/UniProt