5XIJ
Crystal Structure of Toxoplasma gondii Prolyl-tRNA Synthetase (TgPRS) in complex with Inhibitor 9
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 | 21 |
Details | binding site for residue ANP A 1001 |
Chain | Residue |
A | ARG470 |
A | THR592 |
A | ARG594 |
A | MG1002 |
A | MG1003 |
A | 8731004 |
A | HOH1101 |
A | HOH1104 |
A | HOH1118 |
A | HOH1123 |
A | HOH1124 |
A | GLU472 |
A | HOH1130 |
A | HOH1162 |
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 | HOH1101 |
A | HOH1104 |
A | HOH1118 |
A | HOH1124 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue MG A 1003 |
Chain | Residue |
A | ANP1001 |
A | HOH1115 |
A | HOH1130 |
A | HOH1190 |
A | HOH1191 |
A | HOH1199 |
site_id | AC4 |
Number of Residues | 11 |
Details | binding site for residue 873 A 1004 |
Chain | Residue |
A | PHE415 |
A | GLU418 |
A | PRO438 |
A | THR439 |
A | GLU441 |
A | ARG470 |
A | TRP487 |
A | THR558 |
A | HIS560 |
A | ANP1001 |
A | HOH1124 |
site_id | AC5 |
Number of Residues | 21 |
Details | binding site for residue ANP B 1001 |
Chain | Residue |
B | ARG470 |
B | GLU472 |
B | PHE479 |
B | LEU480 |
B | ARG481 |
B | THR482 |
B | PHE485 |
B | TRP487 |
B | GLN555 |
B | THR558 |
B | THR592 |
B | ARG594 |
B | MG1002 |
B | MG1003 |
B | 8731004 |
B | HOH1101 |
B | HOH1104 |
B | HOH1112 |
B | HOH1123 |
B | HOH1129 |
B | HOH1156 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue MG B 1002 |
Chain | Residue |
B | ARG470 |
B | ANP1001 |
B | HOH1104 |
B | HOH1112 |
B | HOH1123 |
B | HOH1128 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue MG B 1003 |
Chain | Residue |
B | ANP1001 |
B | HOH1101 |
B | HOH1129 |
B | HOH1145 |
B | HOH1156 |
B | HOH1161 |
site_id | AC8 |
Number of Residues | 11 |
Details | binding site for residue 873 B 1004 |
Chain | Residue |
B | PHE415 |
B | GLU418 |
B | PRO438 |
B | THR439 |
B | GLU441 |
B | ARG470 |
B | HIS491 |
B | PHE534 |
B | HIS560 |
B | ANP1001 |
B | HOH1128 |
site_id | AC9 |
Number of Residues | 22 |
Details | binding site for residue ANP C 1001 |
Chain | Residue |
C | MG1002 |
C | MG1003 |
C | 8731004 |
C | HOH1102 |
C | HOH1104 |
C | HOH1106 |
C | HOH1118 |
C | HOH1135 |
C | HOH1140 |
C | HOH1145 |
C | HOH1153 |
C | ARG470 |
C | GLU472 |
C | PHE479 |
C | LEU480 |
C | ARG481 |
C | THR482 |
C | PHE485 |
C | TRP487 |
C | GLN555 |
C | THR592 |
C | ARG594 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue MG C 1002 |
Chain | Residue |
C | ARG470 |
C | ANP1001 |
C | HOH1102 |
C | HOH1104 |
C | HOH1106 |
C | HOH1135 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue MG C 1003 |
Chain | Residue |
C | ANP1001 |
C | HOH1118 |
C | HOH1139 |
C | HOH1145 |
C | HOH1153 |
C | HOH1174 |
site_id | AD3 |
Number of Residues | 10 |
Details | binding site for residue 873 C 1004 |
Chain | Residue |
C | PHE415 |
C | GLU418 |
C | PRO438 |
C | THR439 |
C | GLU441 |
C | ARG470 |
C | TRP487 |
C | HIS560 |
C | ANP1001 |
C | HOH1135 |
site_id | AD4 |
Number of Residues | 21 |
Details | binding site for residue ANP D 1001 |
Chain | Residue |
D | ARG470 |
D | GLU472 |
D | LYS474 |
D | PHE479 |
D | ARG481 |
D | THR482 |
D | PHE485 |
D | GLN555 |
D | THR558 |
D | THR592 |
D | ARG594 |
D | MG1002 |
D | MG1003 |
D | 8731004 |
D | HOH1101 |
D | HOH1118 |
D | HOH1125 |
D | HOH1128 |
D | HOH1137 |
D | HOH1148 |
D | HOH1152 |
site_id | AD5 |
Number of Residues | 6 |
Details | binding site for residue MG D 1002 |
Chain | Residue |
D | ARG470 |
D | ANP1001 |
D | HOH1101 |
D | HOH1115 |
D | HOH1118 |
D | HOH1125 |
site_id | AD6 |
Number of Residues | 6 |
Details | binding site for residue MG D 1003 |
Chain | Residue |
D | ANP1001 |
D | HOH1128 |
D | HOH1148 |
D | HOH1150 |
D | HOH1163 |
D | HOH1167 |
site_id | AD7 |
Number of Residues | 11 |
Details | binding site for residue 873 D 1004 |
Chain | Residue |
D | PHE415 |
D | GLU418 |
D | PRO438 |
D | THR439 |
D | GLU441 |
D | ARG470 |
D | TRP487 |
D | PHE534 |
D | HIS560 |
D | ANP1001 |
D | HOH1125 |