Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
B | 0003824 | molecular_function | catalytic activity |
C | 0003824 | molecular_function | catalytic activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE SPM A 501 |
Chain | Residue |
A | TRP51 |
A | GLU231 |
A | TYR264 |
A | PRO265 |
A | ILE269 |
A | MTA401 |
A | HOH631 |
A | GLN93 |
A | TYR102 |
A | HIS103 |
A | ASP127 |
A | ASP196 |
A | SER197 |
A | ASP199 |
A | GLN229 |
site_id | AC2 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE SPM B 502 |
Chain | Residue |
B | TRP51 |
B | GLN93 |
B | TYR102 |
B | HIS103 |
B | ASP127 |
B | ASP196 |
B | SER197 |
B | ASP199 |
B | GLN229 |
B | GLU231 |
B | TYR264 |
B | MTA402 |
B | HOH548 |
site_id | AC3 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE SPM C 503 |
Chain | Residue |
C | TRP51 |
C | GLN93 |
C | TYR102 |
C | HIS103 |
C | ASP127 |
C | ASP196 |
C | SER197 |
C | ASP199 |
C | GLU231 |
C | SER232 |
C | TYR264 |
C | PRO265 |
C | CYS268 |
C | ILE269 |
C | MTA403 |
C | HOH611 |
site_id | AC4 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE MTA A 401 |
Chain | Residue |
A | GLN72 |
A | GLN93 |
A | GLY124 |
A | GLY125 |
A | ASP127 |
A | CYS146 |
A | GLU147 |
A | ILE148 |
A | ASP149 |
A | VAL152 |
A | GLU177 |
A | ASP178 |
A | ALA179 |
A | ASP196 |
A | SER198 |
A | PRO203 |
A | ALA204 |
A | THR206 |
A | LEU207 |
A | SPM501 |
site_id | AC5 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE MTA B 402 |
Chain | Residue |
B | GLN72 |
B | LEU88 |
B | GLN93 |
B | GLY124 |
B | GLY125 |
B | ASP127 |
B | CYS146 |
B | GLU147 |
B | ILE148 |
B | ASP149 |
B | VAL152 |
B | ASP178 |
B | ALA179 |
B | ASP196 |
B | SER197 |
B | SER198 |
B | PRO203 |
B | ALA204 |
B | THR206 |
B | LEU207 |
B | SPM502 |
site_id | AC6 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE MTA C 403 |
Chain | Residue |
C | PRO203 |
C | ALA204 |
C | THR206 |
C | SPM503 |
C | GLN72 |
C | LEU88 |
C | GLN93 |
C | GLY124 |
C | ASP127 |
C | CYS146 |
C | GLU147 |
C | ILE148 |
C | ASP149 |
C | VAL152 |
C | ASP178 |
C | ALA179 |
C | ASP196 |
C | SER198 |
Functional Information from PROSITE/UniProt
site_id | PS01330 |
Number of Residues | 14 |
Details | PABS_1 Polyamine biosynthesis (PABS) domain signature. VLVVGGGdGgiIrE |
Chain | Residue | Details |
A | VAL120-GLU133 | |