Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2RKJ

Cocrystal structure of a tyrosyl-tRNA synthetase splicing factor with a group I intron RNA

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004812	molecular_function	aminoacyl-tRNA ligase activity
A	0004831	molecular_function	tyrosine-tRNA ligase activity
A	0005524	molecular_function	ATP binding
A	0006418	biological_process	tRNA aminoacylation for protein translation
A	0006437	biological_process	tyrosyl-tRNA aminoacylation
B	0000166	molecular_function	nucleotide binding
B	0004812	molecular_function	aminoacyl-tRNA ligase activity
B	0004831	molecular_function	tyrosine-tRNA ligase activity
B	0005524	molecular_function	ATP binding
B	0006418	biological_process	tRNA aminoacylation for protein translation
B	0006437	biological_process	tyrosyl-tRNA aminoacylation
E	0000166	molecular_function	nucleotide binding
E	0004812	molecular_function	aminoacyl-tRNA ligase activity
E	0004831	molecular_function	tyrosine-tRNA ligase activity
E	0005524	molecular_function	ATP binding
E	0006418	biological_process	tRNA aminoacylation for protein translation
E	0006437	biological_process	tyrosyl-tRNA aminoacylation
F	0000166	molecular_function	nucleotide binding
F	0004812	molecular_function	aminoacyl-tRNA ligase activity
F	0004831	molecular_function	tyrosine-tRNA ligase activity
F	0005524	molecular_function	ATP binding
F	0006418	biological_process	tRNA aminoacylation for protein translation
F	0006437	biological_process	tyrosyl-tRNA aminoacylation
I	0000166	molecular_function	nucleotide binding
I	0004812	molecular_function	aminoacyl-tRNA ligase activity
I	0004831	molecular_function	tyrosine-tRNA ligase activity
I	0005524	molecular_function	ATP binding
I	0006418	biological_process	tRNA aminoacylation for protein translation
I	0006437	biological_process	tyrosyl-tRNA aminoacylation
J	0000166	molecular_function	nucleotide binding
J	0004812	molecular_function	aminoacyl-tRNA ligase activity
J	0004831	molecular_function	tyrosine-tRNA ligase activity
J	0005524	molecular_function	ATP binding
J	0006418	biological_process	tRNA aminoacylation for protein translation
J	0006437	biological_process	tyrosyl-tRNA aminoacylation
M	0000166	molecular_function	nucleotide binding
M	0004812	molecular_function	aminoacyl-tRNA ligase activity
M	0004831	molecular_function	tyrosine-tRNA ligase activity
M	0005524	molecular_function	ATP binding
M	0006418	biological_process	tRNA aminoacylation for protein translation
M	0006437	biological_process	tyrosyl-tRNA aminoacylation
N	0000166	molecular_function	nucleotide binding
N	0004812	molecular_function	aminoacyl-tRNA ligase activity
N	0004831	molecular_function	tyrosine-tRNA ligase activity
N	0005524	molecular_function	ATP binding
N	0006418	biological_process	tRNA aminoacylation for protein translation
N	0006437	biological_process	tyrosyl-tRNA aminoacylation

Functional Information from PROSITE/UniProt

site_id	PS00178
Number of Residues	11
Details	AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. Pt.APsLHVGHL

Chain	Residue	Details
A	PRO104-LEU114

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	56
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:Q9Y2Z4

Chain	Residue	Details
A	TYR99
B	ASP143
B	TYR247
B	GLN251
B	ASP254
B	GLN273
E	TYR99
E	ASP103
E	ASP143
E	TYR247
E	GLN251
A	ASP103
E	ASP254
E	GLN273
F	TYR99
F	ASP103
F	ASP143
F	TYR247
F	GLN251
F	ASP254
F	GLN273
I	TYR99
A	ASP143
I	ASP103
I	ASP143
I	TYR247
I	GLN251
I	ASP254
I	GLN273
J	TYR99
J	ASP103
J	ASP143
J	TYR247
A	TYR247
J	GLN251
J	ASP254
J	GLN273
M	TYR99
M	ASP103
M	ASP143
M	TYR247
M	GLN251
M	ASP254
M	GLN273
A	GLN251
N	TYR99
N	ASP103
N	ASP143
N	TYR247
N	GLN251
N	ASP254
N	GLN273
A	ASP254
A	GLN273
B	TYR99
B	ASP103

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	LYS327
B	LYS327
E	LYS327
F	LYS327
I	LYS327
J	LYS327
M	LYS327
N	LYS327

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1d2r

Chain	Residue	Details
A	LYS324
A	LYS327

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1d2r

Chain	Residue	Details
B	LYS324
B	LYS327

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1d2r

Chain	Residue	Details
E	LYS324
E	LYS327

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1d2r

Chain	Residue	Details
F	LYS324
F	LYS327

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1d2r

Chain	Residue	Details
I	LYS324
I	LYS327

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1d2r

Chain	Residue	Details
J	LYS324
J	LYS327

site_id	CSA7
Number of Residues	2
Details	Annotated By Reference To The Literature 1d2r

Chain	Residue	Details
M	LYS324
M	LYS327

site_id	CSA8
Number of Residues	2
Details	Annotated By Reference To The Literature 1d2r

Chain	Residue	Details
N	LYS324
N	LYS327

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)