2F2A

Structure of tRNA-Dependent Amidotransferase GatCAB complexed with Gln

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003824	molecular_function	catalytic activity
A	0005524	molecular_function	ATP binding
A	0006412	biological_process	translation
A	0016874	molecular_function	ligase activity
A	0030956	cellular_component	glutamyl-tRNA(Gln) amidotransferase complex
A	0050567	molecular_function	glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity
B	0000166	molecular_function	nucleotide binding
B	0003824	molecular_function	catalytic activity
B	0005524	molecular_function	ATP binding
B	0006412	biological_process	translation
B	0016874	molecular_function	ligase activity
B	0016884	molecular_function	carbon-nitrogen ligase activity, with glutamine as amido-N-donor
B	0030956	cellular_component	glutamyl-tRNA(Gln) amidotransferase complex
B	0050566	molecular_function	asparaginyl-tRNA synthase (glutamine-hydrolyzing) activity
B	0050567	molecular_function	glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity
B	0070681	biological_process	glutaminyl-tRNAGln biosynthesis via transamidation
C	0000166	molecular_function	nucleotide binding
C	0005524	molecular_function	ATP binding
C	0006412	biological_process	translation
C	0006450	biological_process	regulation of translational fidelity
C	0016874	molecular_function	ligase activity
C	0030956	cellular_component	glutamyl-tRNA(Gln) amidotransferase complex
C	0050566	molecular_function	asparaginyl-tRNA synthase (glutamine-hydrolyzing) activity
C	0050567	molecular_function	glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity
C	0070681	biological_process	glutaminyl-tRNAGln biosynthesis via transamidation

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 601

Chain	Residue
B	HIS12
B	GLU124
B	GLU150
B	HOH636
B	HOH637
B	HOH638

---

site_id	AC2
Number of Residues	17
Details	BINDING SITE FOR RESIDUE GLN A 501

Chain	Residue
A	SER154
A	ASP174
A	THR175
A	GLY176
A	GLY177
A	SER178
A	PHE206
A	TYR309
A	TYR310
A	ARG358
A	ASP425
A	HOH508
A	HOH529
A	HOH701
A	ALA128
A	MET129
A	GLY130

---

Functional Information from PROSITE/UniProt

site_id	PS00571
Number of Residues	32
Details	AMIDASES Amidases signature. GGSSGGsAAaVAaglvplSlGsDtGgSIRqPA

Chain	Residue	Details
A	GLY152-ALA183

---

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

Chain	Residue	Details
B	LEU141-PRO155

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Charge relay system => ECO:0000255|HAMAP-Rule:MF_00120

Chain	Residue	Details
A	LYS79
A	SER154

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Acyl-ester intermediate => ECO:0000255|HAMAP-Rule:MF_00120

Chain	Residue	Details
A	SER178

---