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6KIE

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

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
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue PO4 A 1101
ChainResidue
ATHR255
AGLY256

site_idAC2
Number of Residues3
Detailsbinding site for residue PO4 A 1102
ChainResidue
ASER718
ALYS719
ASER720

site_idAC3
Number of Residues3
Detailsbinding site for residue PO4 A 1103
ChainResidue
AASN56
AARG517
AHOH1222

site_idAC4
Number of Residues19
Detailsbinding site for residue LSS A 1104
ChainResidue
APRO51
ATYR52
APRO53
ATYR54
AGLY62
AHIS63
ASER66
AHIS91
AHIS251
ASER597
ASER673
AGLY674
AASP676
ALEU677
AHIS681
AHIS709
ALEU710
AHOH1222
APHE50

site_idAC5
Number of Residues7
Detailsbinding site for residue LEU A 1105
ChainResidue
ATHR293
ALEU294
AARG295
ATHR390
ASER396
AASP399
ATYR468

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 Residues4
DetailsBINDING: BINDING => ECO:0000305|PubMed:32232361, ECO:0007744|PDB:6LPF
ChainResidueDetails
ATYR54
ALEU594
ASER597
ATYR52

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ALYS719

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER167
ASER720

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q8BMJ2
ChainResidueDetails
ALYS970
ALYS1047

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PDB entries from 2024-05-15

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