5B7N
Crystal structure of periplasmic 5-methylthioadenosine/S-adenosylhomocysteine nucleosidase from Aeromonas hydrophila
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0008782 | molecular_function | adenosylhomocysteine nucleosidase activity |
A | 0008930 | molecular_function | methylthioadenosine nucleosidase activity |
A | 0009116 | biological_process | nucleoside metabolic process |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
B | 0003824 | molecular_function | catalytic activity |
B | 0008782 | molecular_function | adenosylhomocysteine nucleosidase activity |
B | 0008930 | molecular_function | methylthioadenosine nucleosidase activity |
B | 0009116 | biological_process | nucleoside metabolic process |
B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 19 |
Details | binding site for residue SAH A 301 |
Chain | Residue |
A | ALA36 |
A | MET220 |
A | GLU221 |
A | ARG240 |
A | ASN244 |
A | HOH468 |
A | HOH495 |
A | HOH538 |
A | HOH558 |
A | HOH585 |
B | ARG153 |
A | MET37 |
A | THR104 |
A | ALA105 |
A | GLY106 |
A | GLU198 |
A | TRP199 |
A | GLU218 |
A | GLU219 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue GOL A 302 |
Chain | Residue |
A | LYS122 |
A | SER165 |
A | ARG184 |
A | TYR213 |
A | HOH401 |
A | HOH440 |
A | HOH569 |
site_id | AC3 |
Number of Residues | 19 |
Details | binding site for residue SAH B 301 |
Chain | Residue |
A | ARG153 |
B | ALA36 |
B | MET37 |
B | THR104 |
B | ALA105 |
B | GLY106 |
B | GLU198 |
B | TRP199 |
B | GLU218 |
B | GLU219 |
B | MET220 |
B | GLU221 |
B | ARG240 |
B | ASN244 |
B | HOH493 |
B | HOH508 |
B | HOH619 |
B | HOH632 |
B | HOH644 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue GOL B 302 |
Chain | Residue |
B | LYS122 |
B | PHE124 |
B | TYR213 |
B | HOH446 |
B | HOH528 |
B | HOH567 |
B | HOH598 |