7QC2

Crystal Structure of Prolyl-tRNA synthetase (ProRS, Proline-tRNA ligase) from Plasmodium falciparum in complex with MAT334 and L-Proline

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004812	molecular_function	aminoacyl-tRNA ligase activity
A	0004827	molecular_function	proline-tRNA ligase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0006418	biological_process	tRNA aminoacylation for protein translation
A	0006433	biological_process	prolyl-tRNA aminoacylation

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	Binding 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"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Binding 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"}]}

Chain

Residue

Details

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