2D6F

Crystal structure of Glu-tRNA(Gln) amidotransferase in the complex with tRNA(Gln)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004067	molecular_function	asparaginase activity
A	0005524	molecular_function	ATP binding
A	0006412	biological_process	translation
A	0006450	biological_process	regulation of translational fidelity
A	0006520	biological_process	amino acid metabolic process
A	0016874	molecular_function	ligase activity
A	0050567	molecular_function	glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity
B	0000166	molecular_function	nucleotide binding
B	0004067	molecular_function	asparaginase activity
B	0005524	molecular_function	ATP binding
B	0006412	biological_process	translation
B	0006450	biological_process	regulation of translational fidelity
B	0006520	biological_process	amino acid metabolic process
B	0016874	molecular_function	ligase activity
B	0050567	molecular_function	glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity
C	0000166	molecular_function	nucleotide binding
C	0003824	molecular_function	catalytic activity
C	0004812	molecular_function	aminoacyl-tRNA ligase activity
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0006412	biological_process	translation
C	0016874	molecular_function	ligase activity
C	0016884	molecular_function	carbon-nitrogen ligase activity, with glutamine as amido-N-donor
C	0050567	molecular_function	glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity
C	0070681	biological_process	glutaminyl-tRNAGln biosynthesis via transamidation
D	0000166	molecular_function	nucleotide binding
D	0003824	molecular_function	catalytic activity
D	0004812	molecular_function	aminoacyl-tRNA ligase activity
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0006412	biological_process	translation
D	0016874	molecular_function	ligase activity
D	0016884	molecular_function	carbon-nitrogen ligase activity, with glutamine as amido-N-donor
D	0050567	molecular_function	glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity
D	0070681	biological_process	glutaminyl-tRNAGln biosynthesis via transamidation

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 900

Chain	Residue
C	CYS26
C	CYS28
C	CYS79
C	GLU82

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 1900

Chain	Residue
D	CYS26
D	CYS28
D	CYS79
D	GLU82

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Functional Information from PROSITE/UniProt

site_id	PS00144
Number of Residues	9
Details	ASN_GLN_ASE_1 Asparaginase / glutaminase active site signature 1. IiSTGGTVA

Chain	Residue	Details
A	ILE95-ALA103

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site_id	PS00917
Number of Residues	11
Details	ASN_GLN_ASE_2 Asparaginase / glutaminase active site signature 2. GvVvaHGTDTM

Chain	Residue	Details
A	GLY170-MET180

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site_id	PS01234
Number of Residues	15
Details	GATB Glutamyl-tRNA(Gln) amidotransferase subunit B signature. LDRlgiPLVEItTdP

Chain	Residue	Details
C	LEU175-PRO189

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	ACT_SITE: ACT_SITE => ECO:0000250

Chain	Residue	Details
A	THR101
A	THR177
A	ASP178
A	LYS254
B	THR101
B	THR177
B	ASP178
B	LYS254

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Catalytic Information from CSA

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

Chain	Residue	Details
A	SER374

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

Chain	Residue	Details
B	SER374

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

Chain	Residue	Details
A	GLY376

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

Chain	Residue	Details
B	GLY376

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