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 | 11 |
Details | BINDING SITE FOR RESIDUE 4MN A 401 |
Chain | Residue |
A | VAL91 |
A | HOH2008 |
A | HOH2061 |
A | ILE92 |
A | GLN93 |
A | TYR102 |
A | SER197 |
A | ASP199 |
A | GLN229 |
A | TYR264 |
A | ILE269 |
site_id | AC2 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE S4M A 501 |
Chain | Residue |
A | GLN72 |
A | GLN93 |
A | HIS103 |
A | GLY124 |
A | GLY125 |
A | ASP127 |
A | CYS146 |
A | GLU147 |
A | ILE148 |
A | VAL152 |
A | ASP178 |
A | ALA179 |
A | ASP196 |
A | SER198 |
A | PRO203 |
A | ALA204 |
A | THR206 |
A | LEU207 |
A | TYR264 |
site_id | AC3 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE 4MN B 401 |
Chain | Residue |
B | VAL91 |
B | ILE92 |
B | GLN93 |
B | TYR102 |
B | SER197 |
B | ASP199 |
B | GLN229 |
B | TYR264 |
B | ILE269 |
B | HOH2007 |
B | HOH2100 |
site_id | AC4 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE S4M B 501 |
Chain | Residue |
B | GLN72 |
B | LEU88 |
B | GLN93 |
B | TYR102 |
B | HIS103 |
B | GLY124 |
B | GLY125 |
B | ASP127 |
B | CYS146 |
B | GLU147 |
B | ILE148 |
B | VAL152 |
B | ASP178 |
B | ALA179 |
B | ASP196 |
B | SER198 |
B | PRO203 |
B | ALA204 |
B | THR206 |
B | TYR264 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 601 |
Chain | Residue |
B | LYS97 |
B | PHE100 |
C | LEU233 |
C | TRP234 |
C | VAL237 |
C | PHE313 |
site_id | AC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE 4MN C 401 |
Chain | Residue |
C | VAL91 |
C | ILE92 |
C | GLN93 |
C | TYR102 |
C | SER197 |
C | ASP199 |
C | TYR264 |
C | HOH2007 |
C | HOH2090 |
site_id | AC7 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE S4M C 503 |
Chain | Residue |
C | GLN72 |
C | LEU88 |
C | GLN93 |
C | TYR102 |
C | HIS103 |
C | GLY124 |
C | GLY125 |
C | ASP127 |
C | CYS146 |
C | GLU147 |
C | ILE148 |
C | VAL152 |
C | GLU177 |
C | ASP178 |
C | ALA179 |
C | ASP196 |
C | SER198 |
C | PRO203 |
C | ALA204 |
C | THR206 |
C | TYR264 |
site_id | AC8 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE 1PG C 602 |
Chain | Residue |
B | TYR298 |
B | ALA306 |
B | ALA307 |
B | LYS309 |
B | HOH2137 |
C | ASN258 |
C | ALA306 |
C | ALA307 |
C | LYS309 |
C | PRO311 |
C | HOH2140 |
C | HOH2148 |
B | ASN258 |
B | SER260 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE 1PG C 702 |
Chain | Residue |
B | SER45 |
B | PHE47 |
C | SER45 |
C | PHE47 |
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 | |