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6KR7

Crystal structure of methylated human leucyl-tRNA synthetase, Leu-AMS-bound form

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
A0012505cellular_componentendomembrane system
A0016874molecular_functionligase activity
A0017101cellular_componentaminoacyl-tRNA synthetase multienzyme complex
A0034198biological_processcellular response to amino acid starvation
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
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue LEU A 1401
ChainResidue
ALEU294
AVAL389
ATHR390
ASER396

site_idAC2
Number of Residues18
Detailsbinding site for residue LSS A 1402
ChainResidue
AGLY62
AHIS63
ASER66
AHIS91
AHIS251
ASER597
ASER673
AGLY674
AASP676
ALEU677
AHIS681
AHIS709
ALEU710
APRO51
ATYR52
APRO53
ATYR54
AHIS60

site_idAC3
Number of Residues2
Detailsbinding site for residue PO4 A 1403
ChainResidue
AASN56
AARG517

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 Residues249
DetailsRegion: {"description":"Editing domain","evidences":[{"source":"PubMed","id":"19426743","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
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 Residues4
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 Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"32232361","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"6LPF","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q8BMJ2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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