Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6LPF

The crystal structure of human cytoplasmic LRS

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0002161molecular_functionaminoacyl-tRNA deacylase activity
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004819molecular_functionglutamine-tRNA ligase activity
A0004823molecular_functionleucine-tRNA ligase activity
A0005096molecular_functionGTPase activator activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005764cellular_componentlysosome
A0005783cellular_componentendoplasmic reticulum
A0005829cellular_componentcytosol
A0006412biological_processtranslation
A0006418biological_processtRNA aminoacylation for protein translation
A0006425biological_processglutaminyl-tRNA aminoacylation
A0006429biological_processleucyl-tRNA aminoacylation
A0008361biological_processregulation of cell size
A0012505cellular_componentendomembrane system
A0016604cellular_componentnuclear body
A0016874molecular_functionligase activity
A0017101cellular_componentaminoacyl-tRNA synthetase multienzyme complex
A0032008biological_processpositive regulation of TOR signaling
A0034198biological_processcellular response to amino acid starvation
A0043547biological_processpositive regulation of GTPase activity
A0071230biological_processcellular response to amino acid stimulus
A0071233biological_processcellular response to L-leucine
A0106074biological_processaminoacyl-tRNA metabolism involved in translational fidelity
A1904263biological_processpositive regulation of TORC1 signaling
A1990253biological_processcellular response to leucine starvation
B0000166molecular_functionnucleotide binding
B0002161molecular_functionaminoacyl-tRNA deacylase activity
B0004812molecular_functionaminoacyl-tRNA ligase activity
B0004819molecular_functionglutamine-tRNA ligase activity
B0004823molecular_functionleucine-tRNA ligase activity
B0005096molecular_functionGTPase activator activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005764cellular_componentlysosome
B0005783cellular_componentendoplasmic reticulum
B0005829cellular_componentcytosol
B0006412biological_processtranslation
B0006418biological_processtRNA aminoacylation for protein translation
B0006425biological_processglutaminyl-tRNA aminoacylation
B0006429biological_processleucyl-tRNA aminoacylation
B0008361biological_processregulation of cell size
B0012505cellular_componentendomembrane system
B0016604cellular_componentnuclear body
B0016874molecular_functionligase activity
B0017101cellular_componentaminoacyl-tRNA synthetase multienzyme complex
B0032008biological_processpositive regulation of TOR signaling
B0034198biological_processcellular response to amino acid starvation
B0043547biological_processpositive regulation of GTPase activity
B0071230biological_processcellular response to amino acid stimulus
B0071233biological_processcellular response to L-leucine
B0106074biological_processaminoacyl-tRNA metabolism involved in translational fidelity
B1904263biological_processpositive regulation of TORC1 signaling
B1990253biological_processcellular response to leucine starvation
Functional Information from PDB Data
site_idAC1
Number of Residues21
Detailsbinding site for residue LSS A 1200
ChainResidue
APHE50
AHIS91
AHIS251
ALEU594
ASER597
ASER673
AGLY674
AASP676
ALEU677
AHIS681
AGLY708
APRO51
AHIS709
ALEU710
ATYR52
APRO53
ATYR54
AHIS60
AGLY62
AHIS63
ASER66

site_idAC2
Number of Residues21
Detailsbinding site for residue LSS B 1101
ChainResidue
BPHE50
BPRO51
BTYR52
BPRO53
BTYR54
BGLY62
BHIS63
BSER66
BHIS91
BHIS251
BSER597
BARG671
BSER673
BGLY674
BASP676
BHIS681
BHIS709
BLEU710
BHOH1287
BHOH1354
BHOH1597

site_idAC3
Number of Residues5
Detailsbinding site for residue GOL B 1102
ChainResidue
BGLY344
BVAL345
BVAL346
BVAL349
BLYS350

site_idAC4
Number of Residues15
Detailsbinding site for residue VRT B 1103
ChainResidue
BALA292
BTHR293
BLEU294
BTHR298
BILE380
BLYS381
BLYS384
BVAL389
BTHR390
BASP399
BLYS464
BHOH1245
BHOH1298
BHOH1301
BHOH1404

Functional Information from PROSITE/UniProt
site_idPS00178
Number of Residues12
DetailsAA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. PymNGrLHLGHT
ChainResidueDetails
APRO53-THR64

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues498
DetailsRegion: {"description":"Editing domain","evidences":[{"source":"PubMed","id":"19426743","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsMotif: {"description":"'HIGH' region","evidences":[{"source":"PubMed","id":"32232361","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"6LPF","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsMotif: {"description":"'KMSKS' region","evidences":[{"source":"PubMed","id":"32232361","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"6LPF","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"32232361","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"6LPF","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q8BMJ2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

238582

PDB entries from 2025-07-09

PDB statisticsPDBj update infoContact PDBjnumon