Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3KFU

Crystal structure of the transamidosome

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003676	molecular_function	nucleic acid binding
A	0003723	molecular_function	RNA binding
A	0004812	molecular_function	aminoacyl-tRNA ligase activity
A	0004815	molecular_function	aspartate-tRNA ligase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006412	biological_process	translation
A	0006418	biological_process	tRNA aminoacylation for protein translation
A	0006422	biological_process	aspartyl-tRNA aminoacylation
A	0016874	molecular_function	ligase activity
A	0017101	cellular_component	aminoacyl-tRNA synthetase multienzyme complex
A	0050560	molecular_function	aspartate-tRNA(Asn) ligase activity
B	0000166	molecular_function	nucleotide binding
B	0003676	molecular_function	nucleic acid binding
B	0003723	molecular_function	RNA binding
B	0004812	molecular_function	aminoacyl-tRNA ligase activity
B	0004815	molecular_function	aspartate-tRNA ligase activity
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006412	biological_process	translation
B	0006418	biological_process	tRNA aminoacylation for protein translation
B	0006422	biological_process	aspartyl-tRNA aminoacylation
B	0016874	molecular_function	ligase activity
B	0017101	cellular_component	aminoacyl-tRNA synthetase multienzyme complex
B	0050560	molecular_function	aspartate-tRNA(Asn) ligase activity
C	0000166	molecular_function	nucleotide binding
C	0003676	molecular_function	nucleic acid binding
C	0003723	molecular_function	RNA binding
C	0004812	molecular_function	aminoacyl-tRNA ligase activity
C	0004815	molecular_function	aspartate-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	0006422	biological_process	aspartyl-tRNA aminoacylation
C	0016874	molecular_function	ligase activity
C	0017101	cellular_component	aminoacyl-tRNA synthetase multienzyme complex
C	0050560	molecular_function	aspartate-tRNA(Asn) ligase activity
D	0000166	molecular_function	nucleotide binding
D	0003676	molecular_function	nucleic acid binding
D	0003723	molecular_function	RNA binding
D	0004812	molecular_function	aminoacyl-tRNA ligase activity
D	0004815	molecular_function	aspartate-tRNA ligase activity
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006412	biological_process	translation
D	0006418	biological_process	tRNA aminoacylation for protein translation
D	0006422	biological_process	aspartyl-tRNA aminoacylation
D	0016874	molecular_function	ligase activity
D	0017101	cellular_component	aminoacyl-tRNA synthetase multienzyme complex
D	0050560	molecular_function	aspartate-tRNA(Asn) ligase activity
E	0000166	molecular_function	nucleotide binding
E	0003824	molecular_function	catalytic activity
E	0005524	molecular_function	ATP binding
E	0006412	biological_process	translation
E	0016874	molecular_function	ligase activity
E	0030956	cellular_component	glutamyl-tRNA(Gln) amidotransferase complex
E	0050567	molecular_function	glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity
F	0003824	molecular_function	catalytic activity
F	0016874	molecular_function	ligase activity
F	0016884	molecular_function	carbon-nitrogen ligase activity, with glutamine as amido-N-donor
G	0000166	molecular_function	nucleotide binding
G	0005524	molecular_function	ATP binding
G	0006412	biological_process	translation
G	0006450	biological_process	regulation of translational fidelity
G	0016874	molecular_function	ligase activity
G	0050566	molecular_function	asparaginyl-tRNA synthase (glutamine-hydrolyzing) activity
G	0050567	molecular_function	glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity
G	0070681	biological_process	glutaminyl-tRNAGln biosynthesis via transamidation
H	0000166	molecular_function	nucleotide binding
H	0003824	molecular_function	catalytic activity
H	0005524	molecular_function	ATP binding
H	0006412	biological_process	translation
H	0016874	molecular_function	ligase activity
H	0030956	cellular_component	glutamyl-tRNA(Gln) amidotransferase complex
H	0050567	molecular_function	glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity
I	0003824	molecular_function	catalytic activity
I	0016874	molecular_function	ligase activity
I	0016884	molecular_function	carbon-nitrogen ligase activity, with glutamine as amido-N-donor
J	0000166	molecular_function	nucleotide binding
J	0005524	molecular_function	ATP binding
J	0006412	biological_process	translation
J	0006450	biological_process	regulation of translational fidelity
J	0016874	molecular_function	ligase activity
J	0050566	molecular_function	asparaginyl-tRNA synthase (glutamine-hydrolyzing) activity
J	0050567	molecular_function	glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity
J	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 F 673

Chain	Residue
F	CYS22
F	CYS24
F	CYS38
F	CYS41

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG F 674

Chain	Residue
F	HOH677
F	HIS11
F	GLU120
F	GLU146
F	HOH675
F	HOH676

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN I 467

Chain	Residue
I	CYS22
I	CYS24
I	CYS38
I	CYS41

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG I 468

Chain	Residue
I	HIS11
I	GLU120
I	GLU146
I	HOH469
I	HOH470
I	HOH471

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
E	GLY139-ALA170

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

Chain	Residue	Details
F	LEU137-PRO151

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	Region: {"description":"Aspartate","evidences":[{"source":"HAMAP-Rule","id":"MF_02075","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	25
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02075","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	16
Details	Site: {"description":"Interaction with tRNA"}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Site: {"description":"Important for tRNA non-discrimination","evidences":[{"source":"HAMAP-Rule","id":"MF_02075","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Active site: {"description":"Charge relay system","evidences":[{"source":"HAMAP-Rule","id":"MF_00120","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2
Details	Active site: {"description":"Acyl-ester intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_00120","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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