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 | 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 | 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 | 14 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
