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5XIF

Crystal Structure of Prolyl-tRNA Synthetase (PRS) from Toxoplasma gondii

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004812molecular_functionaminoacyl-tRNA ligase activity
A0004827molecular_functionproline-tRNA ligase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006418biological_processtRNA aminoacylation for protein translation
A0006433biological_processprolyl-tRNA aminoacylation
B0000166molecular_functionnucleotide binding
B0004812molecular_functionaminoacyl-tRNA ligase activity
B0004827molecular_functionproline-tRNA ligase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006418biological_processtRNA aminoacylation for protein translation
B0006433biological_processprolyl-tRNA aminoacylation
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue CL A 901
ChainResidue
AMET601
ATYR830

site_idAC2
Number of Residues1
Detailsbinding site for residue CL B 901
ChainResidue
BMET601

site_idAC3
Number of Residues1
Detailsbinding site for residue CL B 902
ChainResidue
BLYS377

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PDB entries from 2024-07-24

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