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1IRX

Crystal structure of class I lysyl-tRNA synthetase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000049molecular_functiontRNA binding
A0000166molecular_functionnucleotide binding
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004824molecular_functionlysine-tRNA ligase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006412biological_processtranslation
A0006418biological_processtRNA aminoacylation for protein translation
A0006430biological_processlysyl-tRNA aminoacylation
A0046872molecular_functionmetal ion binding
B0000049molecular_functiontRNA binding
B0000166molecular_functionnucleotide binding
B0004812molecular_functionaminoacyl-tRNA ligase activity
B0004824molecular_functionlysine-tRNA ligase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006412biological_processtranslation
B0006418biological_processtRNA aminoacylation for protein translation
B0006430biological_processlysyl-tRNA aminoacylation
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 600
ChainResidue
AASP95
ACYS99
AHIS100
AHIS106

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 601
ChainResidue
ACYS177
AHIS180
ACYS199
AHIS203

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 600
ChainResidue
BCYS99
BHIS100
BHIS106
BASP95

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN B 602
ChainResidue
BCYS177
BTYR197
BCYS199

Functional Information from PROSITE/UniProt
site_idPS00178
Number of Residues10
DetailsAA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. P..SGyVHVGNF
ChainResidueDetails
APRO30-PHE39

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBINDING:
ChainResidueDetails
AASP95
BCYS99
BHIS100
BHIS106
BCYS177
BHIS180
BCYS199
BHIS203
ACYS99
AHIS100
AHIS106
ACYS177
AHIS180
ACYS199
AHIS203
BASP95

226707

PDB entries from 2024-10-30

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