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6LPF

The crystal structure of human cytoplasmic LRS

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0002161molecular_functionaminoacyl-tRNA editing 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
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 editing 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
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 Residues8
DetailsBINDING: BINDING => ECO:0000305|PubMed:32232361, ECO:0007744|PDB:6LPF
ChainResidueDetails
ATYR52
ATYR54
ALEU594
ASER597
BTYR52
BTYR54
BLEU594
BSER597

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ALYS719
BLYS719

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER167
ASER720
BSER167
BSER720

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q8BMJ2
ChainResidueDetails
ALYS970
ALYS1047
BLYS970
BLYS1047

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PDB entries from 2024-11-06

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