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 | 19 |
Details | BINDING SITE FOR RESIDUE MTA A 401 |
Chain | Residue |
A | GLN72 |
A | ASP149 |
A | VAL152 |
A | ASP178 |
A | ALA179 |
A | ASP196 |
A | SER198 |
A | PRO203 |
A | ALA204 |
A | THR206 |
A | JFQ501 |
A | LEU88 |
A | GLN93 |
A | GLY124 |
A | GLY125 |
A | ASP127 |
A | CYS146 |
A | GLU147 |
A | ILE148 |
site_id | AC2 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE JFQ A 501 |
Chain | Residue |
A | ILE92 |
A | GLN93 |
A | TYR102 |
A | HIS103 |
A | ASP127 |
A | ASP196 |
A | SER197 |
A | ASP199 |
A | TYR264 |
A | ILE269 |
A | MTA401 |
A | HOH831 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 601 |
Chain | Residue |
A | LYS97 |
A | TRP234 |
A | HOH835 |
A | HOH858 |
A | HOH927 |
site_id | AC4 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE MTA B 401 |
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 | JFQ501 |
site_id | AC5 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE JFQ B 501 |
Chain | Residue |
B | ILE92 |
B | GLN93 |
B | TYR102 |
B | HIS103 |
B | ASP127 |
B | ASP196 |
B | SER197 |
B | ASP199 |
B | TYR264 |
B | ILE269 |
B | MTA401 |
B | HOH802 |
B | HOH981 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 602 |
Chain | Residue |
B | LYS97 |
B | LYS297 |
B | HOH946 |
B | HOH989 |
B | HOH990 |
C | TRP234 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE 1PG C 701 |
Chain | Residue |
C | TRP43 |
C | SER45 |
C | PHE47 |
C | HOH989 |
site_id | AC8 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE MTA C 401 |
Chain | Residue |
C | GLN72 |
C | LEU88 |
C | GLN93 |
C | GLY124 |
C | GLY125 |
C | ASP127 |
C | CYS146 |
C | GLU147 |
C | ILE148 |
C | VAL152 |
C | ASP178 |
C | ALA179 |
C | ASP196 |
C | SER198 |
C | PRO203 |
C | ALA204 |
C | THR206 |
C | LEU207 |
C | JFQ501 |
site_id | AC9 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE JFQ C 501 |
Chain | Residue |
C | ILE92 |
C | GLN93 |
C | TYR102 |
C | HIS103 |
C | ASP127 |
C | ASP196 |
C | SER197 |
C | ASP199 |
C | TYR264 |
C | ILE269 |
C | MTA401 |
C | HOH805 |
C | HOH875 |
site_id | BC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL C 601 |
Chain | Residue |
B | TRP234 |
C | LYS97 |
C | HOH832 |
C | HOH865 |
C | HOH958 |
C | HOH1010 |
C | HOH1015 |
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 | |