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7F97

Plasmodium falciparum Prolyl-tRNA Synthetase (PfPRS) in Complex with L-proline and compound L97

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
C0000166molecular_functionnucleotide binding
C0004812molecular_functionaminoacyl-tRNA ligase activity
C0004827molecular_functionproline-tRNA ligase activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0006418biological_processtRNA aminoacylation for protein translation
C0006433biological_processprolyl-tRNA aminoacylation
D0000166molecular_functionnucleotide binding
D0004812molecular_functionaminoacyl-tRNA ligase activity
D0004827molecular_functionproline-tRNA ligase activity
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0006418biological_processtRNA aminoacylation for protein translation
D0006433biological_processprolyl-tRNA aminoacylation
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues48
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25817387","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27798837","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2014","submissionDatabase":"PDB data bank","title":"Crystal Structure of Prolyl-tRNA synthetase (ProRS, Proline--tRNA ligase)from Plasmodium falciparum in complex with Halofuginone and AMPPNP.","authors":["Dranow D.M.","Edwards T.E.","Lorimer D."]}},{"source":"PDB","id":"4OLF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4Q15","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YDQ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"OCT-2019","submissionDatabase":"PDB data bank","title":"Crystal Structure of Prolyl-tRNA synthetase (ProRS, Proline--tRNA ligase) from Plasmodium falciparum in complex with NCP-26 and L-Proline.","authors":["Johansson C.","Wang J.","Tye M.","Payne N.C.","Mazitschek R.","Thompson A.","Arrowsmith C.H.","Bountra C.","Edwards A.","Oppermann U.C.T."]}},{"source":"PDB","id":"6T7K","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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