Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6LPF

The crystal structure of human cytoplasmic LRS

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0002161	molecular_function	aminoacyl-tRNA deacylase activity
A	0004812	molecular_function	aminoacyl-tRNA ligase activity
A	0004819	molecular_function	glutamine-tRNA ligase activity
A	0004823	molecular_function	leucine-tRNA ligase activity
A	0005096	molecular_function	GTPase activator activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005764	cellular_component	lysosome
A	0005783	cellular_component	endoplasmic reticulum
A	0005829	cellular_component	cytosol
A	0006412	biological_process	translation
A	0006418	biological_process	tRNA aminoacylation for protein translation
A	0006425	biological_process	glutaminyl-tRNA aminoacylation
A	0006429	biological_process	leucyl-tRNA aminoacylation
A	0008361	biological_process	regulation of cell size
A	0012505	cellular_component	endomembrane system
A	0016604	cellular_component	nuclear body
A	0016874	molecular_function	ligase activity
A	0017101	cellular_component	aminoacyl-tRNA synthetase multienzyme complex
A	0032008	biological_process	positive regulation of TOR signaling
A	0034198	biological_process	cellular response to amino acid starvation
A	0043547	biological_process	positive regulation of GTPase activity
A	0071230	biological_process	cellular response to amino acid stimulus
A	0071233	biological_process	cellular response to L-leucine
A	0106074	biological_process	aminoacyl-tRNA metabolism involved in translational fidelity
A	1904263	biological_process	positive regulation of TORC1 signaling
A	1990253	biological_process	cellular response to leucine starvation
B	0000166	molecular_function	nucleotide binding
B	0002161	molecular_function	aminoacyl-tRNA deacylase activity
B	0004812	molecular_function	aminoacyl-tRNA ligase activity
B	0004819	molecular_function	glutamine-tRNA ligase activity
B	0004823	molecular_function	leucine-tRNA ligase activity
B	0005096	molecular_function	GTPase activator activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005764	cellular_component	lysosome
B	0005783	cellular_component	endoplasmic reticulum
B	0005829	cellular_component	cytosol
B	0006412	biological_process	translation
B	0006418	biological_process	tRNA aminoacylation for protein translation
B	0006425	biological_process	glutaminyl-tRNA aminoacylation
B	0006429	biological_process	leucyl-tRNA aminoacylation
B	0008361	biological_process	regulation of cell size
B	0012505	cellular_component	endomembrane system
B	0016604	cellular_component	nuclear body
B	0016874	molecular_function	ligase activity
B	0017101	cellular_component	aminoacyl-tRNA synthetase multienzyme complex
B	0032008	biological_process	positive regulation of TOR signaling
B	0034198	biological_process	cellular response to amino acid starvation
B	0043547	biological_process	positive regulation of GTPase activity
B	0071230	biological_process	cellular response to amino acid stimulus
B	0071233	biological_process	cellular response to L-leucine
B	0106074	biological_process	aminoacyl-tRNA metabolism involved in translational fidelity
B	1904263	biological_process	positive regulation of TORC1 signaling
B	1990253	biological_process	cellular response to leucine starvation

Functional Information from PDB Data

site_id	AC1
Number of Residues	21
Details	binding site for residue LSS A 1200

Chain	Residue
A	PHE50
A	HIS91
A	HIS251
A	LEU594
A	SER597
A	SER673
A	GLY674
A	ASP676
A	LEU677
A	HIS681
A	GLY708
A	PRO51
A	HIS709
A	LEU710
A	TYR52
A	PRO53
A	TYR54
A	HIS60
A	GLY62
A	HIS63
A	SER66

site_id	AC2
Number of Residues	21
Details	binding site for residue LSS B 1101

Chain	Residue
B	PHE50
B	PRO51
B	TYR52
B	PRO53
B	TYR54
B	GLY62
B	HIS63
B	SER66
B	HIS91
B	HIS251
B	SER597
B	ARG671
B	SER673
B	GLY674
B	ASP676
B	HIS681
B	HIS709
B	LEU710
B	HOH1287
B	HOH1354
B	HOH1597

site_id	AC3
Number of Residues	5
Details	binding site for residue GOL B 1102

Chain	Residue
B	GLY344
B	VAL345
B	VAL346
B	VAL349
B	LYS350

site_id	AC4
Number of Residues	15
Details	binding site for residue VRT B 1103

Chain	Residue
B	ALA292
B	THR293
B	LEU294
B	THR298
B	ILE380
B	LYS381
B	LYS384
B	VAL389
B	THR390
B	ASP399
B	LYS464
B	HOH1245
B	HOH1298
B	HOH1301
B	HOH1404

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	PRO53-THR64

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	498
Details	Region: {"description":"Editing domain","evidences":[{"source":"PubMed","id":"19426743","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	6
Details	Motif: {"description":"'HIGH' region","evidences":[{"source":"PubMed","id":"32232361","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"6LPF","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Motif: {"description":"'KMSKS' region","evidences":[{"source":"PubMed","id":"32232361","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"6LPF","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"32232361","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"6LPF","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q8BMJ2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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