3A4L
Crystal structure of archaeal O-phosphoseryl-tRNA(Sec) kinase
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
A | 0043915 | molecular_function | L-seryl-tRNA(Sec) kinase activity |
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 | 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 | 2 |
Details | BINDING: BINDING => ECO:0000255 |
Chain | Residue | Details |
A | GLY11 | |
B | GLY11 |