3AL0

Crystal structure of the glutamine transamidosome from Thermotoga maritima in the glutamylation state.

Functional Information from GO Data

Chain	GOid	namespace	contents
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	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	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	0000049	molecular_function	tRNA binding
C	0000166	molecular_function	nucleotide binding
C	0004812	molecular_function	aminoacyl-tRNA ligase activity
C	0004818	molecular_function	glutamate-tRNA ligase activity
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006412	biological_process	translation
C	0006418	biological_process	tRNA aminoacylation for protein translation
C	0006424	biological_process	glutamyl-tRNA aminoacylation
C	0006450	biological_process	regulation of translational fidelity
C	0008270	molecular_function	zinc ion binding
C	0016874	molecular_function	ligase activity
C	0043039	biological_process	tRNA aminoacylation
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	17
Details	BINDING SITE FOR RESIDUE GSU C 1001

Chain	Residue
C	ARG132
C	GLY321
C	ASP323
C	HIS324
C	LEU350
C	ILE351
C	LEU359
C	LYS361
E	A76
C	ALA134
C	PRO135
C	SER136
C	GLY144
C	THR148
C	GLU168
C	TYR302
C	ARG320

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 1001

Chain	Residue
B	CYS23
B	CYS25
B	CYS39
B	CYS42

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Functional Information from PROSITE/UniProt

site_id	PS00178
Number of Residues	12
Details	AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. PspTGhLHVGGA

Chain	Residue	Details
C	PRO135-ALA146

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

Chain	Residue	Details
A	GLY139-ALA170

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

Chain	Residue	Details
B	MET148-PRO162

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00022

Chain	Residue	Details
C	LYS361
A	SER141

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Acyl-ester intermediate => ECO:0000250

Chain	Residue	Details
A	SER165

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