7QC1

Crystal Structure of Prolyl-tRNA synthetase (ProRS, Proline-tRNA ligase) from Plasmodium falciparum in complex with MAT436

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
D	0000166	molecular_function	nucleotide binding
D	0004812	molecular_function	aminoacyl-tRNA ligase activity
D	0004827	molecular_function	proline-tRNA ligase activity
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0006418	biological_process	tRNA aminoacylation for protein translation
D	0006433	biological_process	prolyl-tRNA aminoacylation
I	0000166	molecular_function	nucleotide binding
I	0004812	molecular_function	aminoacyl-tRNA ligase activity
I	0004827	molecular_function	proline-tRNA ligase activity
I	0005524	molecular_function	ATP binding
I	0005737	cellular_component	cytoplasm
I	0006418	biological_process	tRNA aminoacylation for protein translation
I	0006433	biological_process	prolyl-tRNA aminoacylation

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269\|Ref.7, ECO:0007744\|PDB:6T7K

site_id	SWS_FT_FI2
Number of Residues	9
Details	BINDING: BINDING => ECO:0000269\|PubMed:25817387, ECO:0000269\|PubMed:27798837, ECO:0000269\|Ref.4, ECO:0007744\|PDB:4OLF, ECO:0007744\|PDB:4Q15, ECO:0007744\|PDB:4YDQ