6C86
Crystal Structure of Lysyl-tRNA Synthetase from Cryptosporidium parvum complexed with L-Lysylsulfamoyl Adenosine
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 | 27 |
Details | binding site for residue KAA A 601 |
Chain | Residue |
A | GLY249 |
A | PHE307 |
A | GLU311 |
A | TYR313 |
A | GLU464 |
A | LEU465 |
A | CYS466 |
A | ASN467 |
A | TYR469 |
A | GLU471 |
A | GLY516 |
A | ALA250 |
A | TRP517 |
A | GLY518 |
A | GLY520 |
A | ARG523 |
A | HOH721 |
A | HOH810 |
A | HOH924 |
A | HOH929 |
A | ALA271 |
A | GLU273 |
A | ARG295 |
A | GLU297 |
A | THR302 |
A | HIS303 |
A | ASN304 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue EDO A 602 |
Chain | Residue |
A | ASN85 |
A | TRP445 |
A | HIS446 |
A | ARG447 |
A | GLU448 |
A | PRO450 |
A | HOH789 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue NA A 603 |
Chain | Residue |
A | THR361 |
A | HOH785 |
A | HOH1025 |
B | HOH815 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue SO4 A 604 |
Chain | Residue |
A | ARG253 |
A | ARG253 |
A | HOH701 |
A | HOH701 |
B | ASN260 |
B | ASN260 |
site_id | AC5 |
Number of Residues | 25 |
Details | binding site for residue KAA B 601 |
Chain | Residue |
B | GLY249 |
B | ALA271 |
B | GLU273 |
B | ARG295 |
B | GLU297 |
B | THR302 |
B | HIS303 |
B | ASN304 |
B | PHE307 |
B | GLU311 |
B | TYR313 |
B | GLU464 |
B | LEU465 |
B | ASN467 |
B | TYR469 |
B | GLU471 |
B | GLY516 |
B | TRP517 |
B | GLY518 |
B | GLY520 |
B | ARG523 |
B | HOH746 |
B | HOH749 |
B | HOH933 |
B | HOH964 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue EDO B 602 |
Chain | Residue |
A | ARG227 |
A | ILE290 |
B | ARG227 |
B | GLU237 |
B | EDO603 |
B | HOH945 |
site_id | AC7 |
Number of Residues | 7 |
Details | binding site for residue EDO B 603 |
Chain | Residue |
A | ARG227 |
A | GLU237 |
A | HOH876 |
B | ARG227 |
B | ILE290 |
B | EDO602 |
B | HOH928 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue EDO B 604 |
Chain | Residue |
B | SER386 |
B | GLN387 |
B | GLU388 |
B | HOH800 |
B | HOH815 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue SO4 B 605 |
Chain | Residue |
B | HIS446 |
B | ARG447 |
B | GLU448 |
B | LYS449 |
B | PRO450 |
B | HOH878 |
site_id | AD1 |
Number of Residues | 3 |
Details | binding site for residue SO4 B 606 |
Chain | Residue |
A | LYS59 |
B | TRP445 |
B | GLN477 |
site_id | AD2 |
Number of Residues | 1 |
Details | binding site for residue CL B 607 |
Chain | Residue |
B | CYS354 |