3A4M
Crystal structure of archaeal O-phosphoseryl-tRNA(Sec) kinase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0001717 | biological_process | conversion of seryl-tRNAsec to selenocys-tRNAsec |
A | 0002098 | biological_process | tRNA wobble uridine modification |
A | 0005524 | molecular_function | ATP binding |
A | 0016301 | molecular_function | kinase activity |
A | 0016310 | biological_process | phosphorylation |
A | 0016740 | molecular_function | transferase activity |
A | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
A | 0043915 | molecular_function | L-seryl-tRNA(Sec) kinase activity |
B | 0000166 | molecular_function | nucleotide binding |
B | 0001717 | biological_process | conversion of seryl-tRNAsec to selenocys-tRNAsec |
B | 0002098 | biological_process | tRNA wobble uridine modification |
B | 0005524 | molecular_function | ATP binding |
B | 0016301 | molecular_function | kinase activity |
B | 0016310 | biological_process | phosphorylation |
B | 0016740 | molecular_function | transferase activity |
B | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
B | 0043915 | molecular_function | L-seryl-tRNA(Sec) kinase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE ADP A 301 |
Chain | Residue |
A | GLY14 |
A | HOH268 |
A | HOH280 |
A | HOH287 |
A | HOH325 |
A | HOH337 |
A | MG401 |
A | VAL15 |
A | GLY16 |
A | LYS17 |
A | SER18 |
A | THR19 |
A | ARG116 |
A | ARG120 |
A | THR154 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 401 |
Chain | Residue |
A | SER18 |
A | HOH268 |
A | HOH269 |
A | HOH279 |
A | HOH280 |
A | ADP301 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE IOD A 402 |
Chain | Residue |
A | ARG199 |
A | ARG223 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 261 |
Chain | Residue |
A | GLU45 |
A | SER46 |
A | PHE47 |
A | PRO48 |
B | ALA25 |
B | VAL37 |
site_id | AC5 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE ADP B 301 |
Chain | Residue |
B | GLY14 |
B | VAL15 |
B | GLY16 |
B | LYS17 |
B | SER18 |
B | THR19 |
B | ARG116 |
B | ARG120 |
B | THR154 |
B | HOH267 |
B | HOH274 |
B | HOH275 |
B | HOH288 |
B | MG401 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 401 |
Chain | Residue |
B | SER18 |
B | HOH267 |
B | HOH274 |
B | HOH275 |
B | HOH285 |
B | ADP301 |
site_id | AC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE IOD B 402 |
Chain | Residue |
B | LYS131 |
B | ARG199 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 261 |
Chain | Residue |
A | LYS22 |
B | GLU45 |
B | SER46 |
B | PRO48 |
B | HOH342 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 262 |
Chain | Residue |
A | LYS232 |
A | HOH389 |
B | TYR143 |
B | LYS144 |
B | TRP145 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 263 |
Chain | Residue |
B | GLU56 |
B | LYS59 |
B | LYS193 |
B | LYS196 |
B | GLU197 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255 |
Chain | Residue | Details |
A | GLY11 | |
B | GLY11 |