Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6IY6

Crystal structure of human cytosolic aspartyl-tRNA synthetase (DRS) in complex with glutathion-S transferase (GST) domains from Aminoacyl tRNA synthase complex-interacting multifunctional protein 2 (AIMP2) and glutamyl-prolyl-tRNA synthetase (EPRS)

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	0004046	molecular_function	aminoacylase activity
A	0004812	molecular_function	aminoacyl-tRNA ligase activity
A	0004815	molecular_function	aspartate-tRNA ligase activity
A	0005515	molecular_function	protein binding
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	0016020	cellular_component	membrane
A	0016874	molecular_function	ligase activity
A	0017101	cellular_component	aminoacyl-tRNA synthetase multienzyme complex
A	0045202	cellular_component	synapse
A	0065003	biological_process	protein-containing complex assembly
A	0070062	cellular_component	extracellular exosome
B	0000166	molecular_function	nucleotide binding
B	0003676	molecular_function	nucleic acid binding
B	0003723	molecular_function	RNA binding
B	0004046	molecular_function	aminoacylase activity
B	0004812	molecular_function	aminoacyl-tRNA ligase activity
B	0004815	molecular_function	aspartate-tRNA ligase activity
B	0005515	molecular_function	protein binding
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	0016020	cellular_component	membrane
B	0016874	molecular_function	ligase activity
B	0017101	cellular_component	aminoacyl-tRNA synthetase multienzyme complex
B	0045202	cellular_component	synapse
B	0065003	biological_process	protein-containing complex assembly
B	0070062	cellular_component	extracellular exosome
C	0017101	cellular_component	aminoacyl-tRNA synthetase multienzyme complex
D	0017101	cellular_component	aminoacyl-tRNA synthetase multienzyme complex
E	0017101	cellular_component	aminoacyl-tRNA synthetase multienzyme complex
E	0043517	biological_process	positive regulation of DNA damage response, signal transduction by p53 class mediator
F	0017101	cellular_component	aminoacyl-tRNA synthetase multienzyme complex
F	0043517	biological_process	positive regulation of DNA damage response, signal transduction by p53 class mediator
G	0000166	molecular_function	nucleotide binding
G	0003676	molecular_function	nucleic acid binding
G	0003723	molecular_function	RNA binding
G	0004046	molecular_function	aminoacylase activity
G	0004812	molecular_function	aminoacyl-tRNA ligase activity
G	0004815	molecular_function	aspartate-tRNA ligase activity
G	0005515	molecular_function	protein binding
G	0005524	molecular_function	ATP binding
G	0005737	cellular_component	cytoplasm
G	0005829	cellular_component	cytosol
G	0006412	biological_process	translation
G	0006418	biological_process	tRNA aminoacylation for protein translation
G	0006422	biological_process	aspartyl-tRNA aminoacylation
G	0016020	cellular_component	membrane
G	0016874	molecular_function	ligase activity
G	0017101	cellular_component	aminoacyl-tRNA synthetase multienzyme complex
G	0045202	cellular_component	synapse
G	0065003	biological_process	protein-containing complex assembly
G	0070062	cellular_component	extracellular exosome
H	0000166	molecular_function	nucleotide binding
H	0003676	molecular_function	nucleic acid binding
H	0003723	molecular_function	RNA binding
H	0004046	molecular_function	aminoacylase activity
H	0004812	molecular_function	aminoacyl-tRNA ligase activity
H	0004815	molecular_function	aspartate-tRNA ligase activity
H	0005515	molecular_function	protein binding
H	0005524	molecular_function	ATP binding
H	0005737	cellular_component	cytoplasm
H	0005829	cellular_component	cytosol
H	0006412	biological_process	translation
H	0006418	biological_process	tRNA aminoacylation for protein translation
H	0006422	biological_process	aspartyl-tRNA aminoacylation
H	0016020	cellular_component	membrane
H	0016874	molecular_function	ligase activity
H	0017101	cellular_component	aminoacyl-tRNA synthetase multienzyme complex
H	0045202	cellular_component	synapse
H	0065003	biological_process	protein-containing complex assembly
H	0070062	cellular_component	extracellular exosome
I	0017101	cellular_component	aminoacyl-tRNA synthetase multienzyme complex
J	0017101	cellular_component	aminoacyl-tRNA synthetase multienzyme complex
K	0017101	cellular_component	aminoacyl-tRNA synthetase multienzyme complex
K	0043517	biological_process	positive regulation of DNA damage response, signal transduction by p53 class mediator
L	0017101	cellular_component	aminoacyl-tRNA synthetase multienzyme complex
L	0043517	biological_process	positive regulation of DNA damage response, signal transduction by p53 class mediator

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue ZN A 601

Chain	Residue
A	HIS204
A	GLU208
B	HIS204
B	GLU208

site_id	AC2
Number of Residues	4
Details	binding site for residue PO4 A 602

Chain	Residue
A	LEU344
A	ARG345
C	THR151
C	HIS153

site_id	AC3
Number of Residues	4
Details	binding site for residue PO4 A 603

Chain	Residue
A	LYS110
A	PRO150
G	ARG179
A	ASN109

site_id	AC4
Number of Residues	3
Details	binding site for residue PO4 A 604

Chain	Residue
A	HIS67
A	THR68
A	LYS110

site_id	AC5
Number of Residues	4
Details	binding site for residue PO4 A 605

Chain	Residue
A	HIS67
A	ARG81
A	GLU111
A	ILE185

site_id	AC6
Number of Residues	5
Details	binding site for residue PO4 A 606

Chain	Residue
A	ARG273
A	GLU424
A	ILE425
A	LEU426
A	SER427

site_id	AC7
Number of Residues	6
Details	binding site for residue PO4 A 607

Chain	Residue
A	LYS254
A	ASP290
A	SER427
A	ARG431
A	GLY469
A	GLY470

site_id	AC8
Number of Residues	4
Details	binding site for residue PO4 A 608

Chain	Residue
A	ASP367
A	GLU373
A	ASP417
A	GLU424

site_id	AC9
Number of Residues	3
Details	binding site for residue PO4 B 601

Chain	Residue
B	LEU344
B	ARG345
D	HIS153

site_id	AD1
Number of Residues	4
Details	binding site for residue PO4 B 602

Chain	Residue
B	HIS67
B	ARG81
B	GLU111
B	ILE185

site_id	AD2
Number of Residues	7
Details	binding site for residue PO4 B 603

Chain	Residue
B	GLN251
B	LYS254
B	ASP290
B	SER427
B	ARG431
B	GLY469
B	GLY470

site_id	AD3
Number of Residues	4
Details	binding site for residue PO4 B 604

Chain	Residue
B	HIS67
B	THR68
B	LYS110
H	ARG179

site_id	AD4
Number of Residues	4
Details	binding site for residue PO4 B 605

Chain	Residue
B	ASP367
B	GLU373
B	ASP417
B	GLU424

site_id	AD5
Number of Residues	3
Details	binding site for residue PO4 G 601

Chain	Residue
G	LEU344
G	ARG345
I	HIS153

site_id	AD6
Number of Residues	6
Details	binding site for residue PO4 G 602

Chain	Residue
G	GLN251
G	LYS254
G	ASP290
G	ARG431
G	GLY469
G	GLY470

site_id	AD7
Number of Residues	3
Details	binding site for residue PO4 G 603

Chain	Residue
G	HIS67
G	THR68
G	LYS110

site_id	AD8
Number of Residues	4
Details	binding site for residue ZN H 601

Chain	Residue
G	HIS204
G	GLU208
H	HIS204
H	GLU208

site_id	AD9
Number of Residues	4
Details	binding site for residue PO4 H 602

Chain	Residue
H	LEU344
H	ARG345
J	THR151
J	HIS153

site_id	AE1
Number of Residues	5
Details	binding site for residue PO4 H 603

Chain	Residue
H	LYS254
H	ASP290
H	ARG431
H	GLY469
H	GLY470

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	Region: {"description":"Aspartate","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	16
Details	Region: {"description":"Binding site for the 3'-end of tRNA","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	28
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	8
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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