6J28
Crystal structure of the branched-chain polyamine synthase C9 mutein from Thermus thermophilus (Tth-BpsA C9) in complex with N4-aminopropylspermidine and 5'-methylthioadenosine
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005737 | cellular_component | cytoplasm |
A | 0006596 | biological_process | polyamine biosynthetic process |
A | 0016740 | molecular_function | transferase activity |
A | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
A | 0046872 | molecular_function | metal ion binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0006596 | biological_process | polyamine biosynthetic process |
B | 0016740 | molecular_function | transferase activity |
B | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
B | 0046872 | molecular_function | metal ion binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0006596 | biological_process | polyamine biosynthetic process |
C | 0016740 | molecular_function | transferase activity |
C | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
C | 0046872 | molecular_function | metal ion binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0006596 | biological_process | polyamine biosynthetic process |
D | 0016740 | molecular_function | transferase activity |
D | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 17 |
Details | binding site for residue N4P A 401 |
Chain | Residue |
A | ASP133 |
A | TYR295 |
A | TRP298 |
A | TYR300 |
A | TYR321 |
A | THR353 |
A | MTA402 |
A | HOH502 |
A | HOH554 |
A | GLN134 |
A | GLY135 |
A | ASP166 |
A | ASP167 |
A | ASP231 |
A | PRO232 |
A | GLU234 |
A | GLU265 |
site_id | AC2 |
Number of Residues | 17 |
Details | binding site for residue MTA A 402 |
Chain | Residue |
A | PHE132 |
A | ASP133 |
A | GLN134 |
A | GLY164 |
A | ASP165 |
A | ASP166 |
A | ASP186 |
A | ALA187 |
A | HIS211 |
A | ASP212 |
A | LEU213 |
A | ASP231 |
A | VAL233 |
A | PHE242 |
A | LEU345 |
A | TYR346 |
A | N4P401 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue FE A 403 |
Chain | Residue |
A | CYS97 |
A | CYS100 |
C | CYS97 |
C | CYS100 |
site_id | AC4 |
Number of Residues | 17 |
Details | binding site for residue N4P B 401 |
Chain | Residue |
B | ASP133 |
B | GLN134 |
B | GLY135 |
B | ASP166 |
B | ASP167 |
B | ASP231 |
B | PRO232 |
B | GLU234 |
B | GLU265 |
B | TYR295 |
B | TRP298 |
B | TYR300 |
B | TYR321 |
B | THR353 |
B | MTA402 |
B | HOH507 |
B | HOH516 |
site_id | AC5 |
Number of Residues | 15 |
Details | binding site for residue MTA B 402 |
Chain | Residue |
B | PHE132 |
B | ASP133 |
B | GLN134 |
B | GLY164 |
B | ASP165 |
B | ASP166 |
B | ASP186 |
B | ALA187 |
B | HIS211 |
B | ASP212 |
B | LEU213 |
B | ASP231 |
B | VAL233 |
B | TYR346 |
B | N4P401 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue FE B 403 |
Chain | Residue |
B | CYS97 |
B | CYS100 |
D | CYS97 |
D | CYS100 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue MES B 404 |
Chain | Residue |
A | ARG109 |
B | GLU296 |
B | ASN297 |
C | GLU94 |
site_id | AC8 |
Number of Residues | 15 |
Details | binding site for residue N4P C 401 |
Chain | Residue |
C | ASP133 |
C | GLN134 |
C | GLY135 |
C | ASP166 |
C | ASP167 |
C | ASP231 |
C | PRO232 |
C | GLU234 |
C | GLY260 |
C | THR262 |
C | TYR295 |
C | TYR300 |
C | TYR321 |
C | THR353 |
C | MTA402 |
site_id | AC9 |
Number of Residues | 16 |
Details | binding site for residue MTA C 402 |
Chain | Residue |
C | ASP186 |
C | ALA187 |
C | HIS211 |
C | ASP212 |
C | LEU213 |
C | ASP231 |
C | VAL233 |
C | PHE242 |
C | TYR346 |
C | N4P401 |
C | PHE132 |
C | ASP133 |
C | GLN134 |
C | GLY164 |
C | ASP165 |
C | ASP166 |
site_id | AD1 |
Number of Residues | 3 |
Details | binding site for residue MES C 403 |
Chain | Residue |
C | GLU219 |
C | VAL222 |
C | HIS223 |
site_id | AD2 |
Number of Residues | 16 |
Details | binding site for residue N4P D 401 |
Chain | Residue |
D | ASP133 |
D | GLN134 |
D | GLY135 |
D | ASP166 |
D | ASP167 |
D | ASP231 |
D | PRO232 |
D | GLU234 |
D | GLY260 |
D | THR262 |
D | TRP298 |
D | TYR300 |
D | TYR321 |
D | THR353 |
D | MTA402 |
D | HOH512 |
site_id | AD3 |
Number of Residues | 14 |
Details | binding site for residue MTA D 402 |
Chain | Residue |
D | PHE132 |
D | ASP133 |
D | GLN134 |
D | GLY164 |
D | ASP165 |
D | ASP166 |
D | ASP186 |
D | ALA187 |
D | HIS211 |
D | ASP212 |
D | LEU213 |
D | VAL233 |
D | TYR346 |
D | N4P401 |
site_id | AD4 |
Number of Residues | 9 |
Details | binding site for residue MES D 403 |
Chain | Residue |
B | ASN151 |
D | ARG53 |
D | LEU54 |
D | ARG56 |
D | PRO92 |
D | GLY93 |
D | GLY291 |
D | THR322 |
D | HOH515 |