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6ILD

Crystal Structure of Human LysRS: P38/AIMP2 Complex II

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
C0017101cellular_componentaminoacyl-tRNA synthetase multienzyme complex
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue LYS A 601
ChainResidue
AGLY277
ATRP547
AGOL605
AHOH939
AALA278
AGLU301
AGLU339
ATYR341
AASN497
ATYR499
AGLU501
AGLY546

site_idAC2
Number of Residues7
Detailsbinding site for residue GOL A 602
ChainResidue
AHIS133
AGLY149
AGLU150
AGLY151
AILE235
AARG241
AHOH734

site_idAC3
Number of Residues6
Detailsbinding site for residue GOL A 603
ChainResidue
AARG323
ATHR330
AHIS331
AASN332
APHE335
AHOH737

site_idAC4
Number of Residues6
Detailsbinding site for residue MG A 604
ChainResidue
AGLU487
AGLU494
AHOH782
AHOH942
AHOH1020
AHOH1023

site_idAC5
Number of Residues10
Detailsbinding site for residue GOL A 605
ChainResidue
ATHR337
AGLU494
AILE495
ACYS496
AASN497
AGLY548
AGLY550
ALYS601
AHOH785
AHOH904

site_idAC6
Number of Residues11
Detailsbinding site for residue LYS B 601
ChainResidue
BGLY277
BALA278
BGLU301
BGLU339
BTYR341
BASN497
BTYR499
BGLU501
BGLY546
BGOL603
B45A605

site_idAC7
Number of Residues6
Detailsbinding site for residue MG B 602
ChainResidue
BGLU487
BGLU494
B45A605
BHOH740
BHOH763
BHOH962

site_idAC8
Number of Residues12
Detailsbinding site for residue GOL B 603
ChainResidue
BTHR337
BGLU494
BILE495
BCYS496
BASN497
BGLY548
BMET549
BGLY550
BLYS601
B45A605
BHOH770
BHOH866

site_idAC9
Number of Residues6
Detailsbinding site for residue GOL B 604
ChainResidue
BTYR347
BARG393
BASN395
BASP464
BHOH716
BHOH892

site_idAD1
Number of Residues17
Detailsbinding site for residue 45A B 605
ChainResidue
BARG323
BTHR330
BHIS331
BASN332
BPHE335
BGLU494
BARG553
BILE564
BLYS601
BMG602
BGOL603
BHOH763
BHOH771
BHOH831
BHOH960
BHOH962
BHOH981

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18272479","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26074468","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18272479","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23159739","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26074468","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18272479","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19524539","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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