5XIP
Crystal Structure of Eimeria tenella Prolyl-tRNA Synthetase (EtPRS) in complex with Halofuginone
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 | 17 |
| Details | binding site for residue ANP A 1001 |
| Chain | Residue |
| A | ARG390 |
| A | THR478 |
| A | THR512 |
| A | ARG514 |
| A | MG1002 |
| A | HFG1003 |
| A | HOH1101 |
| A | HOH1102 |
| A | HOH1103 |
| A | GLU392 |
| A | PHE399 |
| A | LEU400 |
| A | ARG401 |
| A | THR402 |
| A | PHE405 |
| A | GLN475 |
| A | ALA476 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 1002 |
| Chain | Residue |
| A | ARG390 |
| A | ANP1001 |
| A | HOH1101 |
| A | HOH1102 |
| A | HOH1103 |
| A | HOH1104 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | binding site for residue HFG A 1003 |
| Chain | Residue |
| A | PHE335 |
| A | PRO358 |
| A | THR359 |
| A | GLU361 |
| A | ARG390 |
| A | TRP407 |
| A | PHE454 |
| A | THR478 |
| A | HIS480 |
| A | ANP1001 |
| A | HOH1104 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | binding site for residue ANP B 1001 |
| Chain | Residue |
| B | ARG390 |
| B | GLU392 |
| B | LEU400 |
| B | ARG401 |
| B | THR402 |
| B | PHE405 |
| B | GLN475 |
| B | THR478 |
| B | THR512 |
| B | ARG514 |
| B | MG1002 |
| B | HFG1003 |
| B | HOH1101 |
| B | HOH1102 |
| B | HOH1103 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 1002 |
| Chain | Residue |
| B | ANP1001 |
| B | HOH1101 |
| B | HOH1102 |
| B | HOH1103 |
| B | HOH1104 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | binding site for residue HFG B 1003 |
| Chain | Residue |
| B | PHE335 |
| B | VAL339 |
| B | PRO358 |
| B | THR359 |
| B | GLU361 |
| B | ARG390 |
| B | TRP407 |
| B | PHE454 |
| B | THR478 |
| B | HIS480 |
| B | ANP1001 |
| B | HOH1103 |
| site_id | AC7 |
| Number of Residues | 17 |
| Details | binding site for residue ANP C 1001 |
| Chain | Residue |
| C | ARG390 |
| C | GLU392 |
| C | PHE399 |
| C | ARG401 |
| C | THR402 |
| C | PHE405 |
| C | GLN475 |
| C | ALA476 |
| C | THR478 |
| C | THR512 |
| C | ARG514 |
| C | MG1002 |
| C | HFG1003 |
| C | HOH1101 |
| C | HOH1102 |
| C | HOH1103 |
| C | HOH1104 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue MG C 1002 |
| Chain | Residue |
| C | ANP1001 |
| C | HOH1101 |
| C | HOH1102 |
| C | HOH1103 |
| C | HOH1104 |
| site_id | AC9 |
| Number of Residues | 13 |
| Details | binding site for residue HFG C 1003 |
| Chain | Residue |
| C | ANP1001 |
| C | HOH1103 |
| C | GLU338 |
| C | VAL339 |
| C | PRO358 |
| C | THR359 |
| C | GLU361 |
| C | ARG390 |
| C | TRP407 |
| C | PHE454 |
| C | THR478 |
| C | HIS480 |
| C | TRP509 |
| site_id | AD1 |
| Number of Residues | 16 |
| Details | binding site for residue ANP D 1001 |
| Chain | Residue |
| D | ARG390 |
| D | GLU392 |
| D | PHE399 |
| D | ARG401 |
| D | THR402 |
| D | PHE405 |
| D | GLN475 |
| D | ALA476 |
| D | THR512 |
| D | ARG514 |
| D | MG1002 |
| D | HFG1003 |
| D | HOH1101 |
| D | HOH1102 |
| D | HOH1103 |
| D | HOH1104 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue MG D 1002 |
| Chain | Residue |
| D | ARG390 |
| D | ANP1001 |
| D | HOH1101 |
| D | HOH1102 |
| D | HOH1103 |
| D | HOH1104 |
| site_id | AD3 |
| Number of Residues | 12 |
| Details | binding site for residue HFG D 1003 |
| Chain | Residue |
| D | VAL339 |
| D | PRO358 |
| D | THR359 |
| D | GLU361 |
| D | ARG390 |
| D | TRP407 |
| D | PHE454 |
| D | THR478 |
| D | HIS480 |
| D | TRP509 |
| D | ANP1001 |
| D | HOH1104 |
