6HCW
Crystal Structure of Lysyl-tRNA Synthetase from Cryptosporidium parvum complexed with L-lysine and a difluoro cyclohexyl chromone ligand
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000049 | molecular_function | tRNA binding |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003676 | molecular_function | nucleic acid binding |
| A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| A | 0004824 | molecular_function | lysine-tRNA ligase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| A | 0006430 | biological_process | lysyl-tRNA aminoacylation |
| A | 0016020 | cellular_component | membrane |
| B | 0000049 | molecular_function | tRNA binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003676 | molecular_function | nucleic acid binding |
| B | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| B | 0004824 | molecular_function | lysine-tRNA ligase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| B | 0006430 | biological_process | lysyl-tRNA aminoacylation |
| B | 0016020 | cellular_component | membrane |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | binding site for residue LYS A 601 |
| Chain | Residue |
| A | GLY249 |
| A | GLU471 |
| A | GLY516 |
| A | FYB602 |
| A | HOH740 |
| A | HOH772 |
| A | ALA250 |
| A | ALA271 |
| A | GLU273 |
| A | ARG295 |
| A | GLU311 |
| A | TYR313 |
| A | ASN467 |
| A | TYR469 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | binding site for residue FYB A 602 |
| Chain | Residue |
| A | ARG295 |
| A | GLU297 |
| A | THR302 |
| A | HIS303 |
| A | ASN304 |
| A | PHE307 |
| A | GLU464 |
| A | LEU465 |
| A | GLY518 |
| A | LEU519 |
| A | GLY520 |
| A | ARG523 |
| A | ILE534 |
| A | LYS601 |
| A | HOH740 |
| A | HOH772 |
| A | HOH851 |
| A | HOH1011 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | binding site for residue LYS B 601 |
| Chain | Residue |
| B | GLY249 |
| B | ALA250 |
| B | GLU273 |
| B | ARG295 |
| B | GLU311 |
| B | TYR313 |
| B | ASN467 |
| B | TYR469 |
| B | GLU471 |
| B | GLY516 |
| B | FYB602 |
| B | HOH754 |
| B | HOH804 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | binding site for residue FYB B 602 |
| Chain | Residue |
| B | ARG295 |
| B | GLU297 |
| B | THR302 |
| B | HIS303 |
| B | ASN304 |
| B | PHE307 |
| B | GLU464 |
| B | LEU465 |
| B | GLY518 |
| B | LEU519 |
| B | GLY520 |
| B | ARG523 |
| B | ILE534 |
| B | LYS601 |
| B | HOH754 |
| B | HOH892 |
| B | HOH1044 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | binding site for residue TRS B 603 |
| Chain | Residue |
| B | ASP358 |
| B | THR360 |
| B | PRO362 |
| B | SER374 |
| B | GLY377 |
| B | ASN428 |
| B | HOH749 |
| B | HOH755 |
| B | HOH887 |
