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9DPL

Human LysRS bound to cellular modified tRNA-Lys3 and AIMP2

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
A0000049molecular_functiontRNA binding
A0000166molecular_functionnucleotide binding
A0002276biological_processbasophil activation involved in immune response
A0002863biological_processpositive regulation of inflammatory response to antigenic stimulus
A0003877molecular_functionATP:ADP adenylyltransferase activity
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004824molecular_functionlysine-tRNA ligase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006412biological_processtranslation
A0006430biological_processlysyl-tRNA aminoacylation
A0008033biological_processtRNA processing
A0010165biological_processresponse to X-ray
A0015966biological_processdiadenosine tetraphosphate biosynthetic process
A0016020cellular_componentmembrane
A0016597molecular_functionamino acid binding
A0016740molecular_functiontransferase activity
A0016874molecular_functionligase activity
A0017101cellular_componentaminoacyl-tRNA synthetase multienzyme complex
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0043032biological_processpositive regulation of macrophage activation
A0045893biological_processpositive regulation of DNA-templated transcription
A0070371biological_processERK1 and ERK2 cascade
B0000049molecular_functiontRNA binding
B0000166molecular_functionnucleotide binding
B0002276biological_processbasophil activation involved in immune response
B0002863biological_processpositive regulation of inflammatory response to antigenic stimulus
B0003877molecular_functionATP:ADP adenylyltransferase activity
B0004812molecular_functionaminoacyl-tRNA ligase activity
B0004824molecular_functionlysine-tRNA ligase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006412biological_processtranslation
B0006430biological_processlysyl-tRNA aminoacylation
B0008033biological_processtRNA processing
B0010165biological_processresponse to X-ray
B0015966biological_processdiadenosine tetraphosphate biosynthetic process
B0016020cellular_componentmembrane
B0016597molecular_functionamino acid binding
B0016740molecular_functiontransferase activity
B0016874molecular_functionligase activity
B0017101cellular_componentaminoacyl-tRNA synthetase multienzyme complex
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0043032biological_processpositive regulation of macrophage activation
B0045893biological_processpositive regulation of DNA-templated transcription
B0070371biological_processERK1 and ERK2 cascade
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:18272479, ECO:0000269|PubMed:26074468
ChainResidueDetails
AGLY277
BGLY277

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:18272479, ECO:0000269|PubMed:23159739, ECO:0000269|PubMed:26074468
ChainResidueDetails
AGLU301
BGLU501
AGLU339
ATYR341
AASN497
AGLU501
BGLU301
BGLU339
BTYR341
BASN497

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:18272479
ChainResidueDetails
AARG323
AHIS331
AGLU494
AGLY550
BARG323
BHIS331
BGLU494
BGLY550

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N-acetylalanine => ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378
ChainResidueDetails
AALA2
BALA2

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS88
ALYS141
BLYS88
BLYS141

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:19524539
ChainResidueDetails
ASER207
BSER207

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q99MN1
ChainResidueDetails
ASER590
ASER596
BSER590
BSER596

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q99MN1
ChainResidueDetails
ATHR591
BTHR591

236371

PDB entries from 2025-05-21

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