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4YE6

The crystal structure of the intact human GlnRS

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004819molecular_functionglutamine-tRNA ligase activity
A0004860molecular_functionprotein kinase inhibitor activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005759cellular_componentmitochondrial matrix
A0005829cellular_componentcytosol
A0006412biological_processtranslation
A0006418biological_processtRNA aminoacylation for protein translation
A0006425biological_processglutaminyl-tRNA aminoacylation
A0006469biological_processnegative regulation of protein kinase activity
A0007420biological_processbrain development
A0017101cellular_componentaminoacyl-tRNA synthetase multienzyme complex
A0019901molecular_functionprotein kinase binding
A0032873biological_processnegative regulation of stress-activated MAPK cascade
A0032991cellular_componentprotein-containing complex
A0043039biological_processtRNA aminoacylation
A0045892biological_processnegative regulation of DNA-templated transcription
A2001234biological_processnegative regulation of apoptotic signaling pathway
Functional Information from PROSITE/UniProt
site_idPS00178
Number of Residues12
DetailsAA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. PepNGiLHIGHA
ChainResidueDetails
APRO270-ALA281

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00962
ChainResidueDetails
AGLU271
AHIS277
AASP303
ATYR438
ATHR457
AARG486
AVAL494

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378
ChainResidueDetails
AALA2

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648
ChainResidueDetails
ASER70

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS309

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER495

222415

PDB entries from 2024-07-10

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