3A4L
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 | 17 |
| Details | BINDING SITE FOR RESIDUE ANP A 301 |
| Chain | Residue |
| A | PRO13 |
| A | THR154 |
| A | HOH267 |
| A | HOH272 |
| A | HOH278 |
| A | HOH298 |
| A | HOH308 |
| A | HOH367 |
| A | MG401 |
| A | GLY14 |
| A | VAL15 |
| A | GLY16 |
| A | LYS17 |
| A | SER18 |
| A | THR19 |
| A | ARG116 |
| A | ARG120 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 401 |
| Chain | Residue |
| A | SER18 |
| A | HOH272 |
| A | HOH278 |
| A | HOH298 |
| A | ANP301 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE IOD A 402 |
| Chain | Residue |
| A | ARG223 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 261 |
| Chain | Residue |
| A | TYR143 |
| A | LYS144 |
| A | TRP145 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 262 |
| Chain | Residue |
| A | GLU45 |
| A | SER46 |
| A | PRO48 |
| A | HOH339 |
| B | HOH342 |
| site_id | AC6 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE ANP B 301 |
| Chain | Residue |
| B | PRO13 |
| B | GLY14 |
| B | VAL15 |
| B | GLY16 |
| B | LYS17 |
| B | SER18 |
| B | THR19 |
| B | ARG116 |
| B | ARG120 |
| B | THR154 |
| B | HOH283 |
| B | HOH285 |
| B | HOH326 |
| B | HOH356 |
| B | HOH393 |
| B | MG401 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 401 |
| Chain | Residue |
| B | SER18 |
| B | HOH267 |
| B | HOH283 |
| B | ANP301 |
| B | HOH393 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 261 |
| Chain | Residue |
| A | LYS228 |
| A | LYS232 |
| B | TYR143 |
| B | LYS144 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 262 |
| Chain | Residue |
| A | LYS22 |
| A | HOH371 |
| B | GLU45 |
| B | SER46 |
| B | PRO48 |
| B | HOH314 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
