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1LYL

LYSYL-TRNA SYNTHETASE (LYSU) (E.C.6.1.1.6) COMPLEXED WITH LYSINE

Functional Information from GO Data
ChainGOidnamespacecontents
A0000049molecular_functiontRNA binding
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0003676molecular_functionnucleic acid binding
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004824molecular_functionlysine-tRNA ligase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006412biological_processtranslation
A0006418biological_processtRNA aminoacylation for protein translation
A0006430biological_processlysyl-tRNA aminoacylation
A0016020cellular_componentmembrane
A0016874molecular_functionligase activity
A0034605biological_processcellular response to heat
A0036260biological_processRNA capping
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
A0140640molecular_functioncatalytic activity, acting on a nucleic acid
B0000049molecular_functiontRNA binding
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0003676molecular_functionnucleic acid binding
B0004812molecular_functionaminoacyl-tRNA ligase activity
B0004824molecular_functionlysine-tRNA ligase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006412biological_processtranslation
B0006418biological_processtRNA aminoacylation for protein translation
B0006430biological_processlysyl-tRNA aminoacylation
B0016020cellular_componentmembrane
B0016874molecular_functionligase activity
B0034605biological_processcellular response to heat
B0036260biological_processRNA capping
B0042803molecular_functionprotein homodimerization activity
B0046872molecular_functionmetal ion binding
B0140640molecular_functioncatalytic activity, acting on a nucleic acid
C0000049molecular_functiontRNA binding
C0000166molecular_functionnucleotide binding
C0000287molecular_functionmagnesium ion binding
C0003676molecular_functionnucleic acid binding
C0004812molecular_functionaminoacyl-tRNA ligase activity
C0004824molecular_functionlysine-tRNA ligase activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006412biological_processtranslation
C0006418biological_processtRNA aminoacylation for protein translation
C0006430biological_processlysyl-tRNA aminoacylation
C0016020cellular_componentmembrane
C0016874molecular_functionligase activity
C0034605biological_processcellular response to heat
C0036260biological_processRNA capping
C0042803molecular_functionprotein homodimerization activity
C0046872molecular_functionmetal ion binding
C0140640molecular_functioncatalytic activity, acting on a nucleic acid
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE LYS A 505
ChainResidue
AGLY216
AGLY473
AGLU240
AARG262
AMET276
AGLU278
ATYR280
AASN424
APHE426
AGLU428

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE LYS B 505
ChainResidue
BGLY216
BALA238
BGLU240
BARG262
BGLU278
BTYR280
BASN424
BPHE426
BGLU428
BGLY473

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE LYS C 505
ChainResidue
CGLY216
CGLU240
CGLU278
CTYR280
CASN424
CPHE426
CGLU428
CGLY473
CGLY475

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING:
ChainResidueDetails
APHE415
AILE422
BPHE415
BILE422
CPHE415
CILE422

site_idSWS_FT_FI2
Number of Residues6
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
ALYS114
APHE156
BLYS114
BPHE156
CLYS114
CPHE156

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1asy
ChainResidueDetails
AARG480
AGLU278
AARG262

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1asy
ChainResidueDetails
BARG480
BGLU278
BARG262

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1asy
ChainResidueDetails
CARG480
CGLU278
CARG262

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1asy
ChainResidueDetails
AARG262

site_idCSA5
Number of Residues1
DetailsAnnotated By Reference To The Literature 1asy
ChainResidueDetails
BARG262

site_idCSA6
Number of Residues1
DetailsAnnotated By Reference To The Literature 1asy
ChainResidueDetails
CARG262

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PDB entries from 2024-11-06

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