5XIG
Crystal Structure of Toxoplasma gondii Prolyl-tRNA Synthetase (TgPRS) in complex with Inhibitor 1
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 |
C | 0000166 | molecular_function | nucleotide binding |
C | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
C | 0004827 | molecular_function | proline-tRNA ligase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0006418 | biological_process | tRNA aminoacylation for protein translation |
C | 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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 20 |
Details | binding site for residue ANP A 1001 |
Chain | Residue |
A | ARG470 |
A | THR592 |
A | ARG594 |
A | MG1002 |
A | MG1003 |
A | 87F1004 |
A | HOH1110 |
A | HOH1125 |
A | HOH1131 |
A | HOH1158 |
A | HOH1159 |
A | GLU472 |
A | HOH1208 |
A | PHE479 |
A | LEU480 |
A | ARG481 |
A | THR482 |
A | PHE485 |
A | TRP487 |
A | GLN555 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue MG A 1002 |
Chain | Residue |
A | ARG470 |
A | ANP1001 |
A | HOH1110 |
A | HOH1125 |
A | HOH1159 |
A | HOH1208 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue MG A 1003 |
Chain | Residue |
A | ANP1001 |
A | HOH1132 |
A | HOH1158 |
A | HOH1223 |
A | HOH1228 |
A | HOH1234 |
site_id | AC4 |
Number of Residues | 11 |
Details | binding site for residue 87F A 1004 |
Chain | Residue |
A | PHE415 |
A | GLU418 |
A | THR439 |
A | GLU441 |
A | ARG470 |
A | THR558 |
A | HIS560 |
A | TRP589 |
A | ANP1001 |
A | HOH1159 |
A | HOH1213 |
site_id | AC5 |
Number of Residues | 21 |
Details | binding site for residue ANP B 1001 |
Chain | Residue |
B | ARG470 |
B | GLU472 |
B | LYS474 |
B | PHE479 |
B | LEU480 |
B | ARG481 |
B | THR482 |
B | PHE485 |
B | GLN555 |
B | THR592 |
B | ARG594 |
B | MG1002 |
B | MG1003 |
B | 87F1004 |
B | HOH1101 |
B | HOH1102 |
B | HOH1116 |
B | HOH1130 |
B | HOH1149 |
B | HOH1160 |
B | HOH1167 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue MG B 1002 |
Chain | Residue |
B | ARG470 |
B | ANP1001 |
B | HOH1101 |
B | HOH1102 |
B | HOH1109 |
B | HOH1116 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue MG B 1003 |
Chain | Residue |
B | ANP1001 |
B | HOH1137 |
B | HOH1160 |
B | HOH1167 |
B | HOH1173 |
B | HOH1179 |
site_id | AC8 |
Number of Residues | 12 |
Details | binding site for residue 87F B 1004 |
Chain | Residue |
B | PHE415 |
B | GLU418 |
B | THR439 |
B | GLU441 |
B | ARG470 |
B | TRP487 |
B | THR558 |
B | HIS560 |
B | SER588 |
B | TRP589 |
B | ANP1001 |
B | HOH1101 |
site_id | AC9 |
Number of Residues | 21 |
Details | binding site for residue ANP C 1001 |
Chain | Residue |
C | MG1003 |
C | 87F1004 |
C | HOH1102 |
C | HOH1115 |
C | HOH1125 |
C | HOH1129 |
C | HOH1135 |
C | HOH1140 |
C | HOH1145 |
C | HOH1147 |
C | ARG470 |
C | GLU472 |
C | PHE479 |
C | LEU480 |
C | ARG481 |
C | THR482 |
C | PHE485 |
C | GLN555 |
C | THR592 |
C | ARG594 |
C | MG1002 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue MG C 1002 |
Chain | Residue |
C | ARG470 |
C | ANP1001 |
C | HOH1102 |
C | HOH1115 |
C | HOH1135 |
C | HOH1145 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue MG C 1003 |
Chain | Residue |
C | ANP1001 |
C | HOH1140 |
C | HOH1147 |
C | HOH1177 |
C | HOH1178 |
C | HOH1185 |
site_id | AD3 |
Number of Residues | 9 |
Details | binding site for residue 87F C 1004 |
Chain | Residue |
C | PHE415 |
C | GLU418 |
C | THR439 |
C | GLU441 |
C | ARG470 |
C | THR558 |
C | HIS560 |
C | ANP1001 |
C | HOH1145 |
site_id | AD4 |
Number of Residues | 20 |
Details | binding site for residue ANP D 1001 |
Chain | Residue |
D | ARG470 |
D | GLU472 |
D | PHE479 |
D | LEU480 |
D | ARG481 |
D | THR482 |
D | PHE485 |
D | GLN555 |
D | THR592 |
D | ARG594 |
D | MG1002 |
D | MG1003 |
D | 87F1004 |
D | HOH1105 |
D | HOH1112 |
D | HOH1119 |
D | HOH1131 |
D | HOH1133 |
D | HOH1155 |
D | HOH1165 |
site_id | AD5 |
Number of Residues | 5 |
Details | binding site for residue MG D 1002 |
Chain | Residue |
D | ANP1001 |
D | HOH1102 |
D | HOH1120 |
D | HOH1131 |
D | HOH1165 |
site_id | AD6 |
Number of Residues | 6 |
Details | binding site for residue MG D 1003 |
Chain | Residue |
D | ANP1001 |
D | HOH1105 |
D | HOH1112 |
D | HOH1139 |
D | HOH1155 |
D | HOH1166 |
site_id | AD7 |
Number of Residues | 12 |
Details | binding site for residue 87F D 1004 |
Chain | Residue |
D | PHE415 |
D | GLU418 |
D | PRO438 |
D | THR439 |
D | GLU441 |
D | ARG470 |
D | TRP487 |
D | HIS491 |
D | THR558 |
D | HIS560 |
D | ANP1001 |
D | HOH1120 |