5FOG
Crystal structure of hte Cryptosporidium muris cytosolic leucyl-tRNA synthetase editing domain complex with a post-transfer editing analogue of norvaline (Nv2AA)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0002161 | molecular_function | aminoacyl-tRNA editing activity |
A | 0004823 | molecular_function | leucine-tRNA ligase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006418 | biological_process | tRNA aminoacylation for protein translation |
A | 0006429 | biological_process | leucyl-tRNA aminoacylation |
B | 0000166 | molecular_function | nucleotide binding |
B | 0002161 | molecular_function | aminoacyl-tRNA editing activity |
B | 0004823 | molecular_function | leucine-tRNA ligase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0006418 | biological_process | tRNA aminoacylation for protein translation |
B | 0006429 | biological_process | leucyl-tRNA aminoacylation |
C | 0000166 | molecular_function | nucleotide binding |
C | 0002161 | molecular_function | aminoacyl-tRNA editing activity |
C | 0004823 | molecular_function | leucine-tRNA ligase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0006418 | biological_process | tRNA aminoacylation for protein translation |
C | 0006429 | biological_process | leucyl-tRNA aminoacylation |
D | 0000166 | molecular_function | nucleotide binding |
D | 0002161 | molecular_function | aminoacyl-tRNA editing activity |
D | 0004823 | molecular_function | leucine-tRNA ligase activity |
D | 0005524 | molecular_function | ATP binding |
D | 0006418 | biological_process | tRNA aminoacylation for protein translation |
D | 0006429 | biological_process | leucyl-tRNA aminoacylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE VRT A 1542 |
Chain | Residue |
A | ALA286 |
A | ASP433 |
A | LYS496 |
A | HOH2006 |
A | HOH2007 |
A | HOH2049 |
A | THR287 |
A | LEU288 |
A | THR292 |
A | SER415 |
A | LYS418 |
A | GLY421 |
A | VAL423 |
A | THR424 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 1543 |
Chain | Residue |
A | TYR434 |
A | ARG438 |
A | LYS441 |
A | PRO460 |
site_id | AC3 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE VRT B 1542 |
Chain | Residue |
B | TYR258 |
B | ALA286 |
B | THR287 |
B | LEU288 |
B | ARG289 |
B | THR292 |
B | SER415 |
B | LYS418 |
B | GLY421 |
B | VAL423 |
B | THR424 |
B | SER430 |
B | ASP433 |
B | LYS496 |
B | HOH2009 |
B | HOH2010 |
B | HOH2052 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 1543 |
Chain | Residue |
A | PHE412 |
A | LYS449 |
B | TYR505 |
B | LYS518 |
B | CYS520 |
site_id | AC5 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE VRT C 1542 |
Chain | Residue |
C | ALA286 |
C | THR287 |
C | LEU288 |
C | THR292 |
C | SER415 |
C | LYS418 |
C | GLY421 |
C | VAL423 |
C | THR424 |
C | ASP433 |
C | LYS496 |
C | HOH2014 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO C 1543 |
Chain | Residue |
B | PHE407 |
B | GLU455 |
C | GLU462 |
C | ARG511 |
C | EDO1544 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO C 1544 |
Chain | Residue |
B | GLU455 |
B | LEU458 |
C | TYR294 |
C | PRO402 |
C | ARG511 |
C | EDO1543 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE K C 1545 |
Chain | Residue |
C | ALA398 |
C | THR401 |
C | TYR403 |
C | HOH2046 |
C | HOH2049 |
site_id | AC9 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE VRT D 1542 |
Chain | Residue |
D | ALA286 |
D | THR287 |
D | LEU288 |
D | THR292 |
D | SER415 |
D | LYS418 |
D | GLY421 |
D | VAL423 |
D | THR424 |
D | ASP433 |
D | LYS496 |
D | HOH2007 |
D | HOH2008 |
D | HOH2052 |
D | HOH2108 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE K D 1543 |
Chain | Residue |
D | ALA398 |
D | THR401 |
D | TYR403 |
D | HOH2034 |
D | HOH2035 |
D | HOH2038 |