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8XP4

Crystal Structure of human lysyl-tRNA synthetase with acetyllysine

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003676molecular_functionnucleic acid binding
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004824molecular_functionlysine-tRNA ligase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006418biological_processtRNA aminoacylation for protein translation
A0006430biological_processlysyl-tRNA aminoacylation
B0000166molecular_functionnucleotide binding
B0003676molecular_functionnucleic acid binding
B0004812molecular_functionaminoacyl-tRNA ligase activity
B0004824molecular_functionlysine-tRNA ligase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006418biological_processtRNA aminoacylation for protein translation
B0006430biological_processlysyl-tRNA aminoacylation
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 Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS88
ALYS141
BLYS88
BLYS141

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:19524539
ChainResidueDetails
ASER207
BSER207

237423

PDB entries from 2025-06-11

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