4NCX
Crystal Structure of Prolyl-tRNA synthetase (ProRS, Proline--tRNA ligase) from Plasmodium falciparum 3D7
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 |
B | 0000166 | molecular_function | nucleotide binding |
B | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
B | 0004827 | molecular_function | proline-tRNA ligase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0006418 | biological_process | tRNA aminoacylation for protein translation |
B | 0006433 | biological_process | prolyl-tRNA aminoacylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO A 801 |
Chain | Residue |
A | ALA290 |
A | SER536 |
A | LYS537 |
A | TYR538 |
A | ILE595 |
A | HOH938 |
A | HOH1029 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE EDO A 802 |
Chain | Residue |
A | LYS422 |
A | HOH962 |
A | HOH990 |
A | HOH1015 |
A | HOH1133 |
A | HOH1207 |
A | LEU309 |
A | LYS381 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 803 |
Chain | Residue |
A | GLN475 |
A | THR478 |
A | GLY510 |
A | ARG514 |
A | HOH934 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE EDO A 804 |
Chain | Residue |
A | GLU312 |
A | HOH915 |
A | HOH1063 |
B | PRO289 |
B | ALA290 |
B | TYR293 |
B | LYS537 |
B | EDO801 |
B | HOH1134 |
site_id | AC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL A 805 |
Chain | Residue |
A | THR321 |
B | PHE393 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL A 806 |
Chain | Residue |
A | PRO533 |
A | HOH1034 |
A | HOH1056 |
A | HOH1098 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO B 801 |
Chain | Residue |
A | EDO804 |
A | HOH967 |
B | SER536 |
B | LYS537 |
B | TYR538 |
B | ILE595 |
B | HOH1134 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 802 |
Chain | Residue |
B | ASP525 |
B | LYS527 |
B | ASP617 |
B | ASN619 |
B | GLU688 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|Ref.7, ECO:0007744|PDB:6T7K |
Chain | Residue | Details |
A | ARG390 | |
A | HIS480 | |
B | ARG390 | |
B | HIS480 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
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 |
Chain | Residue | Details |
A | ARG401 | |
A | GLN475 | |
A | THR512 | |
B | ARG401 | |
B | GLN475 | |
B | THR512 |